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Purification Strategy - Others
GE-HEALTHCARE
Handbook Protein Purification (pdf)
GE-HEALTHCARE Protein purification Applications (pdf)
GE-HEALTHCARE
Protein and Peptide Purification
- Technique selection guide (pdf)
GE-HEALTHCARE
Bio Process - Product guide (pdf)
GE-HEALTHCARE
Purifying Challenging Proteins: Membrane proteins, Multiprotein
complexes and Inclusion bodies (pdf)
GE-HEALTHCARE
ÄKTAdesign Purification Method handbook.
This handbook is intended to help you make full use of your
ÄKTAexplorer™ or ÄKTApurifier™
chromatography
system. The handbook is a collection of useful step-by-step protocols
to aid your everyday purification work. Detailed instructions and
recommendations
are presented
in a straightforward format, which should be easy to follow
without needing a high level of expertise in programming or in
chromatography. (pdf)
GE-HEALTHCARE
Purification of tagged proteins (pdf)
BIO
RAD Sample Preparation Handbook (pdf)
CLONTECH: Troubleshooting
Guide (pdf)
Test Tube
MERCK Cleaning and Regeneraton of Fractogel
EMD sorbents (pdf)
NOVAGEN
Benzonase Nuclease - Removal of Nucleic Acids(pdf)
NOVAGENBuffer
Compositin for Fusion Tag
Affinity Purification (pdf)
Pall Sorbent
Selection Guide (pdf)
Protein Sample Preparation
and Analysis Application Manual. Table of contents (pdf)
1.0 Introduction: 1.1
Proteomics Process Flo -. 1.2 Product Selection (pdf1)
2.0 Pre-Analytical Applications: 2.1
Abundant Protein Removal - 2.2 Protein Fractionation - 2.3 Detergent
Removal - 2.4 Concentration, Desalting,
and Buffer
Exchange - 2.5 Generic Clarification of Samples by Microporous
Filtration (Particulate Removal) - 2.6 Endotoxin Removal (pdf2)
3.0 Analysis: 3.1
Western Blotting - 3.2 Affinity Activated or Activatable Membranes (pdf3)
4.0 Purification Applications: 4.1
Mustang® Ion Exchange Membranes - 4.2 BioSepra® Chromatography
Resins - 4.3 Rapid
Purification
Development/Scouting
(Process Proteomics) - 4.4 Buffer Exchange, Desalting, and
Concentration
- 4.5 Final Product Clarification (pdf4)
5.0 Supporting Technologies: 5.1 Water Supply
- 5.2 Microbiology Testing (pdf5)
6.0 Technical Appendices: 6.1 Evaluation of
Chromatography Column Packing Efficiency - 6.2 Optional
Pre-Treatment to Improve Recovery
of Samples
from Ultrafiltration Spin Filters - 6.3 Vacuum Manifold for Use
with Multi-Well Filter Plates - 6.4
General Filtration Procedures
for
AcroPrep™ and AcroWell™ Filter Plates - 6.5
Chromatography Products Selection Guide - 6.6 BioSepra® Media - 6.7
Protein
Sample
Preparation and Analysis Media - 6.8 Chemical Compatibility Guide (pdf6)
TOSOH TOYOPEARL®
Orientation Sheet: Size Exclusion Chromatography, Ion Exchange
Chromatography, Hydrophobic Interaction Chromatography
and Affinity Chromatography (pdf)
TOSOH General Principles of Chromatography. Poster (pdf)
Removal
of Nucleic Acids - Various
Protocols
Columns
Pall Pall® LRC Columns
Chromatography Columns for Laboratory Applications (pdf) User Guide (pdf-II)
Purification of Recombinant Proteins
Structural Genomics Consortium Protein production and purification.
Nature Methods 2008, 5: 135-146 (pdf-I) (pdf-II)
GE-HEALTHCARE
The Recombinant Protein Handbook (pdf-I)
(pdf-II)
GE-HEALTHCARE
Purification of tagged proteins (pdf)
PIERCE:
Fusion Protein Fusion Protein Products (pdf)
SIGMA:
DETECTION AND PURIFICATION Detection
and Purification Selection Guide (pdf-I)
(pdf-II)
GST-Fusion Proteins
CLONTECH: Glutathione Resins
(pdf)
CLONTECH:
GST products Handbook
(pdf)
CLONTECH: Protein
Purification Products (pdf)
GE-HEALTHCARE
GST
fusion protein
Handbook (pdf)
GE-HEALTHCARE
Purification of tagged proteins (pdf)
GE-HEALTHCARE
Glutathione Sepharose™ High Performance
is an affinity chromatography medium designed for
easy, one-step
purification
of glutathione S-transferase (GST) tagged proteins (pdf)
GE-HEALTHCARE Separation of DnaK from pGEX-GST by ion exchange chromatography (pdf)
NOVAGENGST.Bind Kits(pdf)
NOVAGEN:
His-Tag
GST-Tag purification and
Detection tools (pdf)
NOVAGEN: Protein Purification and Detection. GST•Tag™ Fusions (pg.30-36) (pdf)
Small scale GST-fusion protein purification under nature conditions
poly His-Tagged
Fusion Proteins
NOVAGEN:
pET
purification manual
(pdf)
(pdf-2)
NOVAGEN:
Ni-NTA Hi-Bind Resins Protocols
(pdf)
NOVAGEN: Protein Purification and Detection. His•Tag® Fusions (pg.18-29) (pdf)
NOVAGEN:
His-Tag
GST-Tag purification and
Detection tools (pdf)
QIAGEN:
Ni-NTA purification manual
(pdf)
QIAGEN:
NiNTA cell lysis under nature
conditions (pdf)
QIAGEN: Ni-NTA
Superflow Cartridges are pre-filled with 1 ml or 5 ml Ni-NTA
Superflow and are ready to use for purification of 6xHis-tagged
proteins using a syringe, peristaltic
pump, or liquid chromatography system
(pdf)
MERCK-NOVAGEN: Metal Chelate Affinity Chromatography.
Ni-MAC™, Co-MAC™ and u-MAC™ Metal
Affinity Chromatography (MAC) Resins
and Cartridges (pdf)
(pdf-II)
(pdf-III)
IBA Tools for
protein expression & purification. 6xHis-tag &
Ni-NTA technology: The optimal partner for Strep-tag in
double tag proteins (pdf)
IBA: Expression and
purification of proteins using Strep-tag and/or
6xHistidine-tag. A comprehensive manual. (pdf)
IBA Mammalian
expression and purification system using Strep-tag and/or
6xHistidine-tag (pdf)
CLONTECH:
Talon Resin Protocol (pdf)
CLONTECH:
Talon Products (pdf)
CLONTECH: BD TalonTM Metal Affinity Resins
User Manual (pdf)
CLONTECH: Purification
in the presence of Beta Mercaptoethanol
(pdf)
CLONTECH: Protein
Purification Products (pdf)
CLONTECH: BD HAT Protein
Expression and Purification System User Manual (pdf)
GE-HEALTHCARE
Purification of tagged proteins (pdf)
GE-HEALTHCARE
Hi Trap Chelating
(pdf)
GE-HEALTHCARE
Hi Trap Chelating Application Note (pdf)
GE-HEALTHCARE
Chelating Sepharose
Fast Flow Instructions
(pdf)
GE-HEALTHCARE
His GraviTrap prepacked, single-use
column for purification of histidine-tagged proteins
by immobilized metal
affinity chromatography (IMAC) without any need for
a purification system. Negligible nickel leakage and is compatible with
denaturing and
reducing agents as well as a wide range of
additives. Short purification times. High protein binding capacity,
≈ 40 mg/column. Purifies
unclarified samples (pdf)
GE-HEALTHCARE
His SpinTrap™ is a prepacked, single-use
spin column for purifying histidine-tagged
proteins by immobilized
metal ion affinity chromatography (IMAC). The resin
has high protein binding capacity, low nickel ion (Ni2+) leakage, and
excellent compatibility
with denaturing agents plus a wide range of
additives. His SpinTrap is used with a standard microcentrifuge and one
purification run takes
approx. 10 min. His SpinTrap columns allow direct
purification of unclarified cell lysates. (pdf-I)
(pdf-II)
GE-HEALTHCARE
HisTrap™ FF crude. This pre-prepacked
column is intended for preparative purification
of
histidine-tagged recombinant proteins from
unclarified lysate without precentrifugation and filtration of the
sample. Leakage of Ni2+
is very low. The medium is compatible with all
commonly used aqueous buffers, reducing agents, denaturants such as 6 M
Gua-HCl
and 8 M urea, and a range of other additives (pdf)
GE-HEALTHCARE
Ni Sepharose and IMAC Sepharose selection guide (pdf)
GE-HEALTHCARE
IMAC Sepharose High Performance. Possible to charge
with various metal ions for optimized selectivity.
High protein binding capacity. Compatible with
commonly used reducing agents, such as DTT, DTE, TCEP, and
β-mercaptoethanol.
Stable in a wide range of
denaturants, detergents, and buffer systems.
(pdf)
GE-HEALTHCARE
Ni Sepharose High Performance
(pdf)
(pdf-II)
GE-HEALTHCARE
Article:
Addition of imidazole during binding improves
purity of histidine-tagged proteins (pdf)
GE-HEALTHCARE Article: Snags with tags: Some observations made
with (His)6-tagged proteins. The need to remove or omit the
affinity tag from the purification scheme.P.Ramage
et.al (pdf)
ACTIVE
MOTIVE: Ni-Ted Manual
(pdf)
AFFILAND:
Metal Purification
VIVASCIENCE:
Vivapure Metal Chelate Mini Spin
Columns (pdf-I)
(pdf-II)
(pdf-III)
(pdf-IV)
(pdf-V)
(pdf-VI) (pdf-VII)
(pdf-VIII)
Small scale His-Tag
fusion protein purification
under nature conditions
Small scale His-Tag fusion
protein purification
under denaturative
conditions
DYNAL Dynabeads TalonTM
(pdf)
Ni-NTA: Handling
and Reuse
SIGMA:
His Selected Nickel
Affinity Gel
(pdf)
PROMEGA:
MagneHisTM
Protein Purification System (pdf)
HISPANAGAR Chelate Agarose Beads (pdf-I) (pdf-II) (pdf-III)
SARTORIUS
Sartobind® IDA 75 - A Separation
Technology Based on Metal
Chelate Membrane Adsorbers - Operating Instructions (pdf)
PIERCE: HisGrab™ Nickel Coated 96-Well
Plates. Ideal for analyzing polyhistidine-tagged fusion proteins by ELISA-based
methods.
Can be used with colorimetric, chemiluminescent or
fluorescent detection methods. (pdf)
NUNC:
ProPur™ affinity spin columns contain a unique flow regulator,
FlowGo, which maximizes the contact time between the target
protein and
the resin. ProPur columns offer the speed of a spin column with the
yields and purities of a gravity column or a batch protocol. They are
ideal
for rapid small-scale and pilot purifications of
His-tagged proteins, method development, expression trials, solubility
determination and
separation of the proteolytically cleaved His tag
from the purified protein. (pdf-I)
Maltose
Binding Protein
GE-HEALTHCARE
MBPTrap™ HP is a ready to use HiTrap™ column for purifying
recombinant proteins tagged with maltose
binding protein (MBP). The column
is packed with Dextrin Sepharose™ High Performance based on
a 34 μm beadsized matrix. Purification of
MBP-tagged protein is done under
physiological conditions, which together with mild elution by
maltose, preserves the activity of the target
protein. (pdf-I)
(pdf-II)
GE-HEALTHCARE
Purification of tagged proteins (pdf)
NEW ENGLAND
BIOLAB: pMAL protein Fusion
and Purification System (pdf-I) (pdf-II)
Small
scale MBP-fusion protein
purification
Crystal Structures
of Fusion Proteins with
Large-Affinity tags. D.R.Smyth et.al.
Protein Science (2003),
12: 1313-1322 (pdf)
Calmodulin Binding Peptide
STRATAGENE:
CBP Calmodulin-Binding Peptide Affinity Tag System
(pdf-I)
(pdf-II)
(pdf-III)
NEW ENGLAND
BIOLAB: The IMPACT (Intein Mediated Purification with an Affinity Chitin-binding
Tag) system is a novel protein
purification
system which utilizes the inducible self-cleavage activity of protein splicing
elements (termed inteins) to separate the target protein
from the affinity tag. Each intein tag contains a chitin binding domain (CBD)
for the affinity purification of the fusion protein on a chitin resin.
Induction of on-column cleavage,
using thiol reagents such as dithiothreitol (DTT), releases the target
protein from the intein tag.
Able to
produce target protein without vector–derived amino acids (pdf)
NEW ENGLAND
BIOLAB: INTEIN-TM System
(pdf)
NEW ENGLAND
BIOLAB: INTEIN-TWIN System (pdf)
T7.Tag
NOVAGENT
7.Tag
Affinity Purification kit
(pdf)
(pdf-II pg 45-46)
Cellulose
Binding Domain
NOVAGEN CBIND
Kits (pdf)
NusA Protein
NOVAGEN Expression
of Soluble Heterologous
Proteins via Fusion with NusA Protein
- Article (pdf)
PROMEGA
PinPointTM
Xa Protein Purification
System The System
is designed for the production and purification
of fusion proteins that
are biotinylated in vivo. Biotinylated
fusion proteins are produced in E. coli and
are affinity-purified using the SoftLink™ Soft Release
Avidin Resin. This proprietary resin
allows elution of the fusion protein under
nondenaturing conditions. The PinPoint™ Vectors
feature the encoded endoproteinase
Factor Xa proteolytic site that provides
a way to separate the purification tag from the native
protein. (pdf)
SIGMA: Detection and Purification - FLAG® A Proven System for Detection and Purification of Proteins. (pdf)
GE-HEALTHCARE StrepTactin™ Sepharose™ High Performance is a chromatography medium for
purifying Strep(II)-tagged proteins. Purification
is done under physiological
conditions and mild elution preserves the activity of the target protein (pdf)
GE-HEALTHCARE
Purification of tagged proteins (pdf)
IBA: Expression and purification of proteins
using Strep-tag and/or 6xHistidine-tag.
A comprehensive manual. The Strep-tag II is a short peptide
(8
amino acids, WSHPQFEK), which binds with high selectivity to
Strep-Tactin, an engineered streptavidin. Elution of purified
recombinant
protein
is performed by desthiobiotin. (pdf)
IBA Tools for protein
expression & purification. Strep-tag® technology
and 6xHis-tag & Ni-NTA technology: Double tag protein
expression
and purification (pdf)
IBA Mammalian expression and purification system
using Strep-tag and/or 6xHistidine-tag (pdf)
IBA One-STrEP Kit. One-STrEP-tag Purification for the
Isolation and Identification of Protein Complexes in Mammalian
Cells.
A comprehensive manual (pdf)
NOVAGEN Strep•Tactin® Purification Kits. Strep•Tactin
protein is a streptavidin derivative developed for optimal
Strep•Tag II binding. The
binding affinity of Strep•Tag II for
Strep•Tactin is approximately 100 times higher than for
streptavidin. The purified target protein is competitively
eluted with 2.5 mM desthiobiotin,
an analog of biotin that reversibly binds Strep•Tactin.
(pdf-I) (pdf-II pg43-44) (pdf-III)
QIAGEN: Two-Step
Affinity Purification System Handbook -
For expressing, purifying, and detecting proteins
carrying a 6xHis
and
Strep-tag II. After elution from the Ni-NTA matrix using imidazole,
recombinant proteins (which also carry the Strep-tag II
epitope)
are loaded directly onto a Strep-Tactin matrix and eluted using either
biotin or desthiobiotin. (pdf-I)
(pdf-II)
STRATAGENE:
VariFlex™ bacterial protein
expression system. Include three different solubility
enhancement tags (SETs) which are
designed
to increase protein solubility, the streptavidin binding peptide (SBP)
purification tag, and a tag that allows for rapid soluble protein
quantification
(Q-tag) (pdf)
Fluorescent
Protein
BD BIOSCIENCES
BD Living Colors™ AcGFP1 Fluorescent Protein. A
novel monomeric green fluorescent protein for fusion tag
applications. Ideal for multicolor applications in flow cytometry and
fluorescence microscopy. (pdf)
BD BIOSCIENCES
BD Living Colors™ DsRed-Monomer
Fluorescent Protein. A novel monomeric red fluorescent
protein for fusion tag
applications. Ideal for multicolor applications in flow cytometry and
fluorescence microscopy. (pdf)
PROMEGA:
The HaloTag™ Interchangeable
Labeling Technology is a novel tool for imaging live
or fixed mammalian cells that express the
HaloTag™ Protein or protein fusions, analyzing
post-translational modification of labeled fusion proteins, and
isolating proteins and protein
complexes. The technology is based on efficient formation
of a covalent bond between a specially designed reporter protein
encoded by the
HaloTag™ pHT2 Vector and a specific ligand in living
cells, in solution or on a solid support. The HaloTag™
Ligand can carry a variety of
functionalities, including fluorescent labels, affinity
handles and attachments to a solid phase. The covalent bond forms
rapidly under general
physiological conditions, is highly specific and
essentially irreversible, yielding a complex that is stable even under
stringent conditions. The open
architecture of the technology enables use of different
ligands. Technical Manual. (pdf)
PROMEGA:
HaloLink™ Resin. The HaloTag
technology comprises the HaloTag polypeptide, which
can be fused to a protein of interest using
the HaloTag Vectors, and a system of interchangeable
synthetic ligands that covalently bind to the HaloTag polypeptide.
HaloLink Resin, allows
covalent and oriented surface immobilization of HaloTag
fusion proteins. The HaloLink Resin can be used in a variety of
applications including
enzyme immobilization, detection of protein:protein
interactions and purification of fusion proteins using protease
cleavage. (pdf)
Solubility enhancement tags
(SETs)
STRATAGENE: VariFlex™ bacterial protein expression system. Include
three different solubility enhancement tags (SETs)
which are
designed to
increase protein solubility, the streptavidin binding peptide (SBP)
purification tag, and a tag that allows for rapid soluble protein
quantification
(Q-tag) (pdf)
INVITROGEN: The Champion™ pET SUMO Protein Expression System utilizes
a small ubiquitinlike modifier
(SUMO) to allow expression,
purification, and generation of native proteins in E.
coli. SUMO fusions may increase the expression of recombinant proteins
and enhance the
solubilityof partially insoluble proteins. In
addition, the tertiary structure of the SUMO protein is specifically
recognized and cleaved by a
ubiquitin-like protein-processing enzyme, SUMO Protease
resulting in the production of native protein. (pdf)
LIFESENSORS SUMO Gene Fusion Technology (pdf)
LIFESENSORS
SUMO Gene Fusion Technology - New Methods for
Enhancing Protein Expression and Purification in Bacteria
(pdf-I)
(pdf-II)
(pdf-III)
LIFESENSORS SUMO Gene Fusion Technology - New Methods
for Enhancing Protein Expression
and Purification (intracellular and secretory
expression) in Insect cells (pdf)
LIFESENSORS
SUMO Gene Fusion Technology
- New Methods for Enhancing Protein
Expression and Purification (intracellular and
secretory
expression) in Mammalian cells (pdf)
LIFESENSORS SUMO Gene Fusion Technology - New Methods
for Enhancing Protein Expression
and Purification in Yeast cells:
Saccharomyces (pdf)
and Pichia (pdf)
LIFESENSORS SUMO Gene Fusion Technology - New Methods
for Rapid Recombinant Peptide Expression and Purification
(pdf)
TAKARA pCold TF DNA Vector is a fusion cold shock expression vector
that expresses Trigger Factor (TF)
chaperone as a soluble tag
(48 kDa) which facilitates
co-translational folding of newly expressed polypeptides. The vector
has a His-Tag sequence, and a multicloning site
(MCS). A lac operator is inserted
downstream of the cspA promoter to ensure strict regulation of
expression. Additionally, recognition sites
for HRV 3C Protease, Thrombin,
and Factor Xa are located between TF-Tag and the Multiple Cloning Site
(MCS) and function to facilitate
tag removal from the expressed
fusion protein. Most E. coli strains can serve as expression hosts. The
pCold TF DNA Vector provides cold
shock technology for high yield
protein expression combined with Trigger Factor (chaperone) expression
to facilitate correct protein folding,
thus enabling efficient soluble
protein production for otherwise intractable target proteins. (pdf-I)
Chaperone Plasmid Set / Chaperone
Competent Cells (pdf-II)
LYTAG and LYTAG Two Phase System
BIOMEDAL LYTAG system allows the single-step purification of proteins fusion to LYTAG and
C-LYTAG using LYTRAP resin, a
simple and efficient
chromatographic support. Binding conditions are gentle and do not
involve covalent modifications, in such a way that the fusion
protein is highly stable once
bound to the resin. LYTAG and C-LYTAG fusions protein are selectively
eluted using choline-containing buffers.
No unwanted amino acids after tag
elimination by enterokinase digestion (pdf)
BIOMEDAL LYTAG Two-Phase is a protein purification system based on the use of two aqueous components.
The method relies on the affinity
of the protein tag LYTAG for one of the two-phase components, allowing
recombinant protein separation
and
purification from cellular extracts or culture media. In the procedure, the
LYTAG-fused protein is retained in one of the aqueous phases while most
of the
undesired proteins can be removed by simply discarding the opposite phase. After
replenishing the system with fresh phase, the protein of interest
can be easily
recovered in it, with high purity, by reversing its localization with the
addition of choline, the specific LYTAG ligand. Purification can be easy
and safely performed at low
temperatures, requiring only a refrigerated centrifuge and an ice water
bath. Alternative to conventional solid resins. (pdf-I)
(pdf-II)
BIO-RAD
Profinity eXact fusion-tag system is an affinity tag-based protein
purification system that utilizes a modified form of the subtilisin
protease, which is immobilized
onto a chromatographic support and used to generate pure, tag-free
target protein in a single step.
The tag in this system is the
prodomain (prosignal sequence) of the subtilisin protease, a 75-amino
acid sequence that is fused to the
N-terminus of a target protein of
interest. The mature and prodomain subtilisin protease sequences have
been co-engineered to produce a
highly specific, high-affinity
interaction between the binding partners. Application of elution buffer
triggers subtilisin’s processing activity,
which quickly and precisely
cleaves the tag from the fusion protein and releases the purified
target protein. At the end of the purification
process, the tag remains tightly
bound to the resin and contains only its native amino acid sequence.
The structure and activity of the native
protein is maintained, and the
need for additional materials, such as cleavage enzymes and
purification resin for postcleavage enzyme removal,
is eliminated. (pdf-I)
(pdf-II)
(pdf-III)
Profinity eXact purification resin (pdf-IV)
(pdf-V)
Cleavage of Recombinant Proteins
Cleavage Sites Table for Fusion Proteins
Factor
Xa
Factor
Xa Cleavage of a MBP
fusion protein
NOVAGEN:
Factor-Xa kit
(pdf)
NOVAGEN: Restriction Grade Factor Xa. Factor Xa Cleavage Capture Kit . (pdf pg.54)
QIAGEN:
Factor
Xa and
Factor
Xa Removal resin
(pdf)
Thrombin
Thrombin Cleavage
of a GST fusion protein
NOVAGEN: Thrombin
kit (pdf)
NOVAGEN: Thrombin, Restriction Grade. Biotinylated Thrombin and Thrombin Cleavage Capture Kit (pdf pg.53)
Enterokinase
NEW
ENGLAND BIOLABS:
Enterokinase (pdf)
NOVAGEN:
Enterokinase
cleavage capture kit (pdf)
NOVAGEN: Recombinant
Enterokinase. Tag•off™ High Activity rEK is a highly
purified preparation of the catalytic subunit of human
enterokinase
that recognizes the identical
cleavage site as the native enzyme, AspAspAspAspLys↓. Enterokinase
Cleavage Capture Kit. Tag•off™ rEK Cleavage
Capture Kit (pdf pg.55-56)
ROCHE:
Enterokinase
(pdf)
PreScission
GE-HEALTHCARE
Application Note
(pdf)
GE-HEALTHCARE
Life Science News
(pdf)
TAGZyme
QIAGEN: His-tag
Removal by exoproteolytic
Digestion
(pdf)
TEV-Protease
INVITROGEN-
LIFE TECHNOLOGIES
TEV-Protease(pdf)
Mohanty A. et.al.
(2003) Inhibition of tobacco etch virus protease activity by
detergents. Protein Expression and Purification 27:
109–114 (pdf)
PROMEGA: ProTEV Protease is
an improved 50kDa version of the NIa protease from tobacco etch virus
(TEV) that has been engineered to be
more stable than native TEV protease
for prolonged enzymatic activity (pdf)
CARDIFF
UNIVERSITY - MOLECULAR
CELL BIOLOGY - EHRMAN LAB
TEV
NIa protease
NOVAGEN HRV 3C Protease (pdf) (pdf pg.57)
INVITROGEN
SUMO Protease
(pdf)
LIFESENSORS
SUMO Protease 1 (pdf)
(pdf-II)
(pdf-III)
Activated Resins
GE-HEALTHCARE
Affinity Manual
(pdf)
GE-HEALTHCARE
Affinity
Columns and Media
(pdf)
HiTrap NHS-activated HP, NHS-activated
Sepharose 4 Fast Flow (10-atom spacer
arms) is designed for the covalent coupling
through the primary amine of a ligand
and is the first choice for the preparation of
immunospecific media.
CNBr-activated Sepharose offers
a well-established option for the attachment of
larger ligands and as an alternative to NHS-activated
Sepharose. Proteins, peptides, amino acids
or nucleic acids can be coupled to CNBr-activated
Sepharose, under mild conditions, via
primary amino groups or similar nucleophilic
groups.
EAH Sepharose 4B for coupling small
ligands containing free acarboxyl groups via
a 10-atom spacer arm. Carbodiimide as the coupling
reagent. Phenolic groups may be attached
through others couple reagents. Thiol derivatives
can couple carboxyl groups in the presence of
carbodiimide and the thiol ester bond
may be cleaved specifically using hydroxylamine,
thus providing a simple and gentle method for
eluting the intact ligand-protein complex.
ECH Sepharose 4B for coupling
small ligands containing free amino groups via a
9-atom spacer arm. Carbodiimide as the coupling
reagent.
Epoxy-activated Sepharose 6B for
coupling through hydroxy, amino or thiol groups
via a 12-carbon spacer arm. It is particularly useful
for
coupling small ligands such as choline,
ethanolamine and sugars. The pre-activated matrix
is formed by reacting Sepharose 6B with the
bis oxirane, 1,4 bis-(2,3-epoxypropoxy-)butane.
Free oxirane groups couple via stable ether
bonds with hydroxyl-containing molecules
such as sugars, via alkylamine linkages
with ligands containing amino groups, and via
thioether linkages with ligands containing thiol
groups.
Thiopropyl Sepharose 6B for coupling
through a thiol group many types of small ligands
• Heavy metal ions and derivatives
can be used as ligands to react with thiol groups
forming mercaptides.
• Alkyl or aryl halide ligands
give thioether derivatives.
• Ligands containing C=O,
N=N and, under certain conditions, C=C bonds undergo
addition reactions.
The hydroxypropyl group acts as a small
spacer arm. Ligands containing amino groups can
be attached to Thiopropyl Sepharose 6B
or Activated Thiol-Sepharose 4B by multi-point
attachment or coupling through a small number
of groups using the heterobifunctional
thiolating reagent, SPDP. The coupled
molecules may be recovered by eluting with a reducing
agent.
GE-HEALTHCARE CNBr Activated Sepharose
Data File - React
with primary amines present on proteins, antibodies
and other
molecules. (pdf)
GE-HEALTHCARE
NHS Activated
Sepharose Data File -NHS (N-hydroxysuccinimide)
coupling forms a chemically
stable amide bond with ligands containing
primary amino groups. NHS-activated Sepharose®
4 Fast Flow provides a spacer arm
and is therefore particularly suitable
for immobilising small protein and peptide ligands. (pdf)
GE-HEALTHCARE Recommended carbodiimide coupling
procedure for CH Sepharose® 4B and AH Sepharose® 4B
(pdf)
BIO
RAD
Affi-Gel 10 and Affi-Gel 15 activated
immunoaffinity supports (N-hydroxysuccinimide
esters of a derivatized crosslinked agarose),
with a 10 and 15-atom spacer arm respectively,
that offer rapid, high efficiency coupling
for all ligands with a primary amino group aqueous
or non-aqueous solution. (pdf)
HISPANAGAR Amino Ethyl and Glyoxal Agarose
Beads (pdf-I) (pdf-II) (pdf-III)
Glyoxal Agarose Beads includes a broad selection of resins
for the immobilization of biomolecules through
amino groups (enzymes,
antibodies, etc). There are resins,
with either 4% or 6% agarose concentration, and
with various degrees of activation (very high/
high/low).
This permits the immobilization of biomolecules
in different size ranges.
Aminoethyl Agarose Beads covalently
bind the agarose to the acid groups of the
amino acid of the target biomolecules. There are
resins
with agarose concentration of 4% or 6%
and with a range of degrees of activation.
JENA BIOSCIENCE
Immobilized Nucleotides for Affinity
Chromatography (pdf) Immobilized
nucleotides provide a convenient
and rapid one-step purification procedure
for a large number of proteins such as kinases,
GTPases, chaperones, motor proteins, and others.
Jena Bioscience provides NTPs and dNTPs
that are linked to the matrix at various positions
of sugar, base or phosphate moiety of the
nucleotide; different types and lengths
of linkers and different types of chromatography
material ranging from bulk material to pre-made
columns that fit any machine
MERCK Fractogel EMD Amino
(pdf)
For immobilization of ligands with carboxy-functionional
groups.
MERCK Fractogel EMD Epoxy (M)
(pdf) Suitable for coupling
of low molecular weight ligands and pH stable
proteins. The epoxyde reacts
with primary amino groups, hydroxyl, and
sulfhydryl groups. The resulting affinity matrix
is very stable, due to the ether bonding of the ligand.
NOVAGEN Preactivated
Resins (pdf)
PreACT™ Agarose ALD is an activated chromatography matrix for simple
and efficient immobilization of small ligands to large
proteins under mild physiological conditions.
Is supplied in an activated form containing
bound reactive aldehyde groups. During
ligand coupling, aldehydes react with
primary amines on the ligand to form a Schiff-base.
In a further reaction, the Schiff-base linkage
is selectively converted into a stable,
secondary amine linkage.
PreACT Fractogel AZL is an activated
resin with a high density of tentacle-bonded
azlactone reactive groups suitable for the
coupling of proteins under physiological
conditions. The azlactone ring is opened by nucleophilic
attack of appropriate groups
present on the protein surface. Upon reaction
with amines, a stable amide bond forms between
the former carbonyl function of the azlactone.
PreACT Fractogel EPX is an activated
resin for the immobilization of low molecular
weight amine bearing ligands or alkaline-stable proteins.
Bonded epoxide groups react with primary
amino, hydroxyl and sulfhydryl groups to form
stable ether linkages.
PIERCE: Affinity Purification Handbook (pdf)
PIERCE Coupling different Functional
Groups: Tosyl, Tresyl
and Epoxy Activated Agarose. Alkylamine
Beads
Tosyl Activated Agarose Hydroxyls
on the surface of cross-linked beaded agarose
are reacted with p-toluenesulfonyl chloride (tosyl
chloride)
to yield a sulfonated support. These sulfonates
can couple to nucleophiles, such as primary
amines or thiols, to yield a stable affinity support.
The tosylated support also couples to
imidazole, or tyrosine hydroxyl groups. Tosyl Activated
Agarose couples more rapidly and more efficiently
to sulfhydryl groups than to primary amines.
Sulfhydryl coupling supports are convenient
when accessible free sulfhydryls exist in the protein,
or
when one can be easily generated through
reduction of a disulfide bond.
Tresyl Activated Agarose Hydroxyls
on the surface of agarose are reacted with
2,2,2-trifluoroethanesulfonyl chloride (tresyl
chloride) to yield
a sulfonated support. This sulfonated
support is approximately 100-fold more reactive
than a Tosyl agarose support. Tresyl Activated Agarose
can couple to nucleophiles, such as primary
amines or thiols, to yield a stable affinity
matrix.. The tresylated support also couples to
imidazole
and tyrosine hydroxyl groups. Tresyl Activated
Agarose couples more rapidly and more efficiently
to sulfhydryl groups than to primary amines.
ImmunoPure® Epoxy-Activated Agarose
Epoxide chemistry is a useful way to immobilize
ligands like proteins, carbohydrates, peptides
and
amino acids, containing nucleophiles,
such as amino,thiol and hydroxyl (including phenolic)
functional groups. Epoxide-activated supports
are
produced by the immobilization of bifunctional
oxiranes such as 1,4-butanediol diglycidyl
ether onto agarose supports, introducing a hydrophilic
spacer arm. These activated supports have
limited stability in aqueous media, so it is necessary
to use them quickly after they are generated
or
rehydrated. (pdf)
PIERCE CarboLink® Coupling Gel allows immobilization
of glycoproteins through their oxidized
carbohydrate moieties. Because
carbohydrates are located on the Fc portion
of antibody molecules, CarboLink® Gel has
the advantage of orienting the antibody
binding sites to remain unobstructed,
resulting in greater purification capability. (pdf)
PIERCE Coupling Proteins trough Sulfhydril
groups Pierce SulfoLink® Coupling Gel is designed
to efficiently react with thiol-containing
molecules and immobilize them through
a thioether linkage. The support contains an
iodoacetyl group at the end of a long spacer arm,
which reacts with sulfhydryls through
displacement of the iodine.
(pdf)
PIERCE: The AminoLink® Coupling Gel support is 4% cross-linked
beaded agarose that has been activated to
form aldehyde
functional
groups. The aldehydes react spontaneously with
primary amines found in lysine residues and
at the amino terminus of a
peptide
chain. Reductive amination of the resulting
Schiff base then forms a stable, secondary amine
linkage with minimal leakage
of the
ligand. (pdf)
PIERCE:
Batch and Spin Cup Methods for Affinity
Purification
of Proteins (pdf)
PIERCE: MicroLink™ Protein Coupling Kit allows immobilization
of small amounts (25-100 µg)
of purified antibody and other
proteins directly onto beaded agarose
gel to create a permanent affinity support. The
AminoLink® Plus Coupling Gel included
in this kit contains aldehyde functional
groups that react with primary amines present
on antibodies and other molecules.
Reductive amination of the resulting
Schiff bases forms a stable secondary amine linkage
with minimal leakage. (pdf)
PIERCE: MicroLink™ Peptide Coupling Kit. For sulfhydryl-containing
peptide or protein. This kit
uses UltraLink® Iodoacetyl Gel
that reacts specifically with free sulfhydryls
to form a stable thioether linkage. The support
contains a 15-atom spacer that reduces
steric hindrance, making binding interactions
with the coupled molecule efficient. (pdf)
PIERCE:
Ultra Link Immobilized Carboxy for Inmobilization
of Peptides using EDC. Useful for
coupling primary amine containing
ligands
like
small peptides (pdf)
PIERCE:
UltraLink® Iodoacetyl Gel binds
specifically to sulfhydryls when used under
specific conditions with the iodoacetyl
alkylating agent.
The 15-atom
spacer arm is especially ideal for conjugating
small peptides to the support. The support
will immobilize numerous types of
molecules
with a free sulfhydryl including antibodies,
other proteins and peptides. (pdf)
PIERCE:
Ultra Link Biosupport Medium with
Azlactone Groups. Couples nucleophiles
on ligands via a ring opening reaction to
attach
the ligand to the support through stable covalent
linkages. Amino-functional ligands will form
stable amide bonds at the end
of a
five-atom spacer.
(pdf)
SARTORIUS
Sartobind® Epoxy 75 - A Microporous
Coupling Membrane for Affinity Chromatography
- Operating Instructions -
Any molecule containing amino-, hydroxyl-
or thiol-groups may be immobilized by covalent
coupling to the epoxy-activated membrane.
The membrane is fitted into a filter holder
with Luer Lock connectors for easy handling
to quickly couple biomolecules like proteins
or peptides covalently. (pdf)
TOSOH
BIOSCIENCE Affinity Chromatography Activated
Resins (pdf)
TOYOPEARL AF-Tresyl-650M: For coupling
of proteins through amine
and thiol groups at slightly alkaline pH (7.0-8.0)
TOYOPEARL AF-Epoxy-650M: Useful for attaching low MW ligands at
high densities and for immobilization of carbohydrates
or glycoproteins
TOYOPEARL AF-Formyl-650M: (aldehide
bearing) For coupling
of proteins through amine groups at slightly alkaline
pH (7.0-9.0)
TOYOPEARL AF-Amino-650M: For coupling
ligands through their carboxylate groups (peptide
bond formation) or aldehyde groups
(reductive amination) present in carbohydrates
and glycoprotein ligands, or introduced
into the ligand by mild periodate oxidation. Reaction
at
slightly acidic pH (4.5-6.0)
TOYOPEARL AF-Amino-650M: Carbodiimide
mediated coupling reaction to amino groups
of proteins or low MW ligands. Reaction at
slightly acidic pH (4.5-6.0)
VIVASCIENCE: Vivapure Epoxy Coupling Kit - Mini Spin
Columns - Vivapure Epoxy Mini spin columns
provide a membrane to
which any desired protein, containing
amino-, sulfhydryl-, or hydroxyl-groups on its
surface is coupled covalently. (pdf)
Antibody Purification
GE-HEALTHCARE Antibody Purification Manual
(old pdf)
(new pdf)
GE-HEALTHCARE Application Note: Rapid optimisation and development of
an automated two-step purification procedure for
monoclonal IgG antibodies
(pdf)
GE-HEALTHCARE Capto adhere: a strong anion exchanger with multimodal
functionality ionic interaction, hydrogen bonding and
hydrophobic interaction.
Capto adhere is designed for post Protein A purification
of monoclonal antibodies. Removal of leached Protein A,
aggregates, host cell
proteins, nucleic acids and viruses from monoclonal antibodies
is performed in flowthrough mode at where the antibodies
pass directly through
the column while the contaminants are adsorbed. (pdf-I) (pdf-II) (pdf-III)
GE-HEALTHCARE
Kappa Select is an affinity chromatography medium designed for the
purification of Fab (kappa) with high binding capacity, purity
and yield. The
ligand binds to the constant region of the kappa light chain. Use for
the production of Fabs for clinical applications. (pdf)
BAC (BioAffinity Company) CaptureSelect Human IgA affinity matrix contains an affinity ligand that binds
to a unique domain that is present on all
subclasses of human IgA, with no cross
reactivity with IgM or IgG. (pdf-I) (pdf-II)
CaptureSelect IgM affinity matrix contains an
affinity ligand that is directed towards a unique domain that is present on both
human and mouse IgM
antibodies, and offers no cross-reactivity with human or
mouse IgA or IgM. (pdf)
CaptureSelect
Fab kappa affinity matrix: for all human antibodies containing kappa
light chains (pdf)
CaptureSelect Fab lambda affinity matrix: for all human antibodies
containing lambda light chains (pdf)
CaptureSelect
Human Fc affinity matrix: for all subclasses of human IgG (pdf)
CaptureSelect
Multi Species affinity matrix: for IgG from multiple species (pdf)
CaptureSelect Multi Species affinity matrix: for human IgG4 (pdf)
BIORAD
Affi-Prep® Protein A Matrix Instruction
Manual
(pdf)
BIORAD Affi-Gel® Protein A MAPS® II Kit - Instruction
Manual (pdf)
BIORAD Econo-Pac® Protein
A Kit Protein A Columns - Instruction Manual
(pdf)
BIO RAD
Immunoaffinity
Kit for IgG coupling trough Fc region
(pdf)
BIO RAD Protein
A removal from IgG on CHT Ceramic Hydroxyapatite Support (pdf)
BIOSEPRA
Purification of Antibodies-Article (pdf)
BIOSEPRA
Validated Alternatives to Protein A Sorbents
for Antibody
Production. (pdf)
BIOSEPRA
MBI HYPERCEL™ Mixed-mode sorbent for direct
capture of antibodies
(pdf)
CALBIOCHEM
Human IgG subclasses
(pdf)
CLONTECH:
Thiophilic
- Purification of Immunoglobulins
(pdf)
MERCK
Capture of Mouse Monoclonal
Antibodies by Cation
Exchange Chromatography
(pdf)
MILLIPORE Affinity Chromatography Media: ProSep®-vA Ultra
Media, ProSep-vA High Capacity Media, ProSep-A
High Capacity Media &
ProSep-rA
High Capacity Media. OPERATING INSTRUCTIONS ProSep-A affinity
media have been developed specifically for industrial
scale
purification of monoclonal antibodies where highly efficient
purification can be achieved using clarified bioreactor feedstock at
physiological
pH and salt concentration.
(pdf)
MILLIPORE
PROSEP-Thiosorb and PROSEP-Thiosorb M
Chromatography Media - for the
recovery and purification of Immunoglobulins (pdf)
Pall BioSepra® Protein A Ceramic HyperD® F sorbent.
High capacity affinity sorbent designed for process-scale purification
of
immunoglobulins G. (pdf) (pdf-II)
Pall Purification of mouse IgM from cell culture supernatant
by Cation Exchange Chromatography on CM Ceramic Hyper D F sorbent (pdf)
PIERCE: Antibody Technical Handbook. The handbook provides
an overview of antibody structure and types, as well as technical
information
on the
procedures, reagents and tools used to produce, purify, fragment and
label antibodies. (pdf-1) (pdf-2) (pdf-3)
PIERCE: Affinity Purification Handbook (pdf)
PIERCE: Binding Characteristics of Immunoglobulin Binding
Proteins and Thiophilic Gel (PowerPoint)
PIERCE: Fab
Preparation Kit enables efficient Fab generation from IgG. This kit
uses papain, a nonspecific thiol-endopeptidase, immobilized on agarose
resin.
Immobilized
enzyme is advantageous because digestion can be immediately stopped by
simply removing the IgG solution from the resin, resulting in a
digest that is
enzyme-free. Digestion by papain produces 50 kDa Fab and Fc fragments
(pdf)
PIERCE: Immobilized E. coli Lysate. Partially
purified bacterial proteins from a suspension
of E. coli cells (strain BMH 71-18) immobilized onto
agarose, provides a simple and
efficient method of removing E. coli-reactive proteins from antibody
preparations
(pdf_I)
(pdf-II)
PIERCE: Antibody Immobilization: Choosing the Best
Support (PowerPoint)
PIERCE:
Immobilized
Jacalin (human IgA and IgD binding lectin).
Jacalin
immobilized on supports such as agarose has been useful for the
purification of human serum or secratory IgA1
(pdf) (pdf-II)
PIERCE: T-Gel™ Purification Kit (pdf)
PIERCE:
Pierce® Protein L Agarose. Protein L binds to immunoglobulin kappa
light chains without interfering with the antigen-binding site and
binds a
wider range of Ig classes and
subclasses than other antibody-binding proteins such as Protein A or
Protein G. Protein L binds to all classes of Ig
(i.e., IgG, IgM, IgA, IgE and
IgD). Protein L also binds single chain variable fragments (Scfv) and
Fab fragments. Protein L only binds to immunoglobulins
containing light chains of type
kappa I, III, and IV in human and kappa I in mouse. Protein L also may
be specific for certain kappa subgroups in other species.
Protein L binds scfv without
interfering with antigen binding. Protein L binds weakly to rabbit
immunoglobulins and does not bind immunoglobulins from bovine,
goat or sheep; nor does it bind
to lambda light chains. (pdf)
SARTORIUS Sartobind Protein A 75 Membrane Adsorbers - Operating
Instructions
A
Separation Technology Based on Microporous Membranes (pdf)
VIVASCIENCE: Vivapure Protein A - Mini Spin Columns (pdf)
General
BIO RAD Polymixin matrix - For removal
of Endotoxin molecules (pdf)
GE-HEALTHCARE
VIII Select. Highly selective to recombinant b-domain depleted Factor
VIII a key recombinant blood factor used for treatment
of Hemophilia
A. . Efficient purification of recombinant b-domain. (pdf)
GE-HEALTHCARE
Kappa Select is an affinity chromatography medium designed for the
purification of Fab (kappa) with high binding capacity, purity
and yield. The
ligand binds to the constant region of the kappa light chain. Use for
the production of Fabs for clinical applications. (pdf)
MILLIPORE
Matrex Cellufine Sulfate - For concentration, purification
and depyrogenation of Virus, Viral/Microbial
Antigen,
Heparin binding proteins (pdf)
Pall BioSepra Blue Trisacryl®
M is an affinity chromatographic sorbent used for the purification
of a wide variety of enzymes and proteins such
as kinases, albumin, interferons, and some
coagulation factors. (pdf)
Pall BioSepra® Heparin HyperD® M composite chromatography
sorbent for the purification of biological molecules that bind to
heparin,
such as coagulation factors, growth factors,
lipoproteins. (pdf)
INVITROGEN:
Dynabeads® for protein complex isolation. Add your specific
antibody or interacting protein with tags to Dynabeads®, then
immunoprecipitate
your protein of interest. Once the beads are exposed
to a magnet, they are efficiently drawn to the tube wall, taking only
your protein complex with them.
As the process is gentle, yet very quick, complexes remain intact and
functional. The complexes can be resuspended in a small volume ready
for downstream
analysis with mass spectrometry, gels, etc. (pdf)
INVITROGEN:
Immunoprecipitation with Dynabeads® Protein A or Protein G.
The captured immune complexes are easily removed from the supernatant
by
magnetic separation. (pdf)
PIERCE: Seize™ X Immunoprecipitation
Kits. Recover protein without antibody protein band
interference. The Kit combine cross-linking
and affinity chromatography to offer a new and
improved immunoprecipitation method. First, the primary antibody is
bound and immobilized to
a Protein A or Protein G support using cross-linking
agent (DSS). This properly orients the antibody to "seize" protein from
crude cell lysate
applied to
the immobilized antibody support. Unbound proteins are then centrifuged
away and the protein is recovered by using an elution buffer.
(pdf -I)
(pdf-II)
(pdf-III)
(pdf-IV)
PIERCE: The Thermo Scientific
Pierce Direct IP Kit enables highly effective and efficient antigen immunoprecipitations
by directly immobilizing
purified antibodies onto an agarose support.
Immobilizing
the antibody provides faster and easier immunoprecipitations, enables
reuse
of the
immobilized antibody and results in purified antigen
free
from antibody contamination. Immunoprecipitation is achieved using less
than
10 μg of
antibody and a short coupling protocol to AminoLink
Resin.
The antigen sample is incubated with the immobilized antibody to form
the
immune
complex. The complex is washed to remove non-bound
material,
and a low pH elution buffer is used to dissociate the bound antigen
from
the
antibody. (pdf)
Lectins and Glycoprotein Purification
CLONTECH:
Glycoprotein Enrichment Resin is a phenylboronic acid-based
resin which provides quick, efficient, and specific enrichment of
glycoproteins
from complex samples such as human serum. The resin
consists of an m-aminophenylboronic acid ligand coupled to agarose
beads. The ligand binds
to cis-diol groups on sugar residues such as
mannose, galactose, or glucose that are present within the saccharide
moiety of glycoprotein molecules.
This complex can be dissociated by lowering the pH,
or by using an elution buffer containing either Tris or sorbitol. (pdf)
GE-HEALTHCARE
Con A Sepharose
4B (Con A binds molcules containing Alpha-D-mannopyranosyl,
Alpha-D-glucopyranosyl
and sterically related residues) (pdf-I) (pdf-II)
GE-HEALTHCARE
HiTrap Lectin Test Kit consists of four glycoprotein
binding columns, HiTrap Con A, HiTrap
Lentil Lectin,
HiTrap
Wheat Germ Lectin and HiTrap Peanut Lectin. (pdf)
GE-HEALTHCARE
HiTrap Wheat Germ Lectin (high
affinity to N-acetylglucosamine and reacts
strongly with the chitobiose core of N-linked
oligosaccharides and N-acetylneuraminic
acid) (pdf)
GE-HEALTHCARE
Lentil Lectin Sepharose 4B
(binds to polysaccharides and glycoconjugates
containing glucose or mannose
type
sugars) (pdf)
CALBIOCHEM
Lectins
(pdf)
EY Laboratories
Lectin
Catalog. Lectin carbohydrate binding chart. Immobilized lectins
and carbohydrates. Lectins kits. (pdf)
PIERCE:
Immobilized
Jacalin (human IgA and IgD binding lectin).
Jacalin immobilized on supports such as
agarose has been useful for the purification
of
human
serum or secratory IgA1
(pdf)
(pdf-II)
PIERCE: Glycoprotein Isolation Kit, WGA isolates glycoproteins
from complex protein mixtures using the lectin wheat germ agglutinin
(WGA)
immobilized on agarose. The WGA lectin preferentially binds N-acetyl
glucosamine (GlcNAC) and terminal GlcNAC structures that
are
commonly present in many serum and
membrane glycoproteins. WGA also has affinity for sialic acid. (pdf)
PIERCE: Glycoprotein Isolation Kit, ConA isolates glycoproteins
from complex protein mixtures using the lectin concanavalin A (ConA)
immobilized
on
agarose. The ConA lectin preferentially recognizes α-linked
mannose and, to a lesser extent,
terminal glucose residues. These
carbohydrates (pdf)
PROMETIC BIOSCIENCES Aminophenyl Boronate Affinity Chromatography for
capture of glycoproteins. The aminophenyl boronate-glycoprotein
covalent
bond can be subsequently disrupted to
elute the protein of interest with a pH change or by competitive
elution using a sugar such as
sorbitol. (pdf)
QIAGEN: Qproteome Glycoprotein Fractionation Handbook.
For the fractionation of glycoproteins in proteomic
samples (pdf)
Qproteome Total
Glycoprotein Kit. The Total Glycoprotein Spin Columns in the Qproteome
Total Glycoprotein Kit contain ConA
and WGA lectins. They are
used for a general enrichment of the total glycoprotein population from
a cell or serum sample.
Qproteome Mannose Glycoprotein Kit. The
ConA, GNA, and LCH lectin spin columns in the Qproteome Mannose
Glycoprotein
Kit are used for specific
enrichment of glycoproteins with mannose-rich glycan moieties. The
three lectins each bind different
subclasses of these moieties.
Qproteome Sialic Glycoprotein Kit. The
WGA, SNA, and MAL lectin spin columns in the Qproteome Sialic
Glycoprotein Kit
are used for specific enrichment
of glycoproteins with sialicacid-rich glycan moieties. The three
lectins each bind different
subclasses of these moieties.
Qproteome O-Glycan
Glycoprotein Kit. The AIL, and PNA lectin spin columns in the Qproteome
O-Glycan Glycoprotein Kit are
used for specific enrichment of
glycoproteins with a glycan structure of the type that are found on
T-antigens. The two lectins each
bind different subclasses of
these glycoproteins.
QIAGEN: Qproteome GlycoArrays is a simple, rapid, kit-based method
for determining the pattern and relative abundance of specific
mammalian glycosylation epitopes in a glycosylated protein. The
analysis can be performed on crude samples in growth media,
eliminating the need for time-consuming purification and
sample preparation steps. The technology consists of arrays of selected
lectins,
which are used to determine the glycosylation features of
the analyzed glycoproteins. (pdf)
Mimetics Ligands, Antibody fragments and Similar Technology
BAC (BioAffinity Company) CaptureSelect® Products. BAC BV provides unique products for affinity purification. These
CaptureSelect® products are
created by
BAC’s proprietary technology based on Camelid derived single
domain antibody fragments. These antibody fragments are produced
efficiently by our
host-vector system based on the yeast Saccharomyces cerevisiae,
enabling high level production with minimal purification effort as
well as easy
scale-up. CaptureSelect® products
possess a combination of unique properties such as stability, affinity, and
selectivity that provides
competitive benefits in terms of reduced cost of
purification, higher quality product, and increased flexibility in the
purification process.
Custom ligands. CaptureSelect® technology
enables new opportunities in the field of custom designed ligands. BAC has
developed an unique ligand
discovery program that is applicable to a wide
variety of target molecules, ranging from bacteria and viruses to proteins,
carbohydrates and even small
molecules like haptens and peptide tags. (pdf-1) (pdf-2) (pdf-3)
PROMETIC Mimetic Ligand™
Affinity Chromatography. The Mimetic Ligand adsorbent range
has been designed to enable
purification of many proteins, providing a general
technique that can replace ion-exchange, gel permeation and hydrophobic
interaction
chromatography, but with higher recovery and purity.
Mimetic Ligand Screening Column Kit contains 1ml pre-packed columns of
ten different
Mimetic LigandTM adsorbents, suitable for attachment
to automated chromatography work stations. (pdf)
SCIL Proteins Affilin™ molecules are small non-immunoglobulin proteins which
are designed for specific binding of proteins and small molecules.
New Affilin™
molecules can be quickly selected from libraries which are based on two
different human derived scaffold
proteins.Affilin™ molecules
can be further modified for various applications.
Additional functionalities can be generated through genetic fusions
with enzymes or effector domains.
Specific
labeling, chemically or with isotopes, extends the field of
applications for Scil Proteins individualised binding proteins.
Affilin™ proteins are
easily produced in the cytoplasm of E.
coli and are fully functional without further posttranslational
modifications such as
glycosylation. Affilin™ molecules will find
their applications in therapy, chromatography, in vivo and in vitro diagnostics and as research tools.
Albumin and Other Abundant Serum Proteins Removal
AGILENT
The Agilent Multiple Affinity Removal System
for Proteomics Sample Preparation.
Designed to remove greater than 98-99%
of six interfering high-abundant proteins using
Affinity-purified polyclonal antibodies to: albumin, IgG, IgA,
transferrin, haptoglobin,
and antitrypsin from human serum or three proteins
(albumin, IgG, and transferrin) from mouse serum samples (pdf-I)
(pdf-II)
(pdf-III)
(pdf-IV)
(pdf-V)
AGILENT
The
Agilent Multiple Affinity Removal System.
Designed to remove six interfering high-abundant
proteins from Monkey
Plasma for Proteomics Sample Preparation (pdf)
AGILENT Agilent
Human 14 Multiple Affinity Removal System Columns for the
Fractionation of High-Abundant Proteins from Human
Proteomic Samples (pdf)
GE-HEALTHCARE
Capto™ Blue a new affinity chromatography prototype resin
for purification or removal of HSA.Made by
immobilizing
Cibacron™ Blue to a new High Flow Agarose matrix (pdf)
CALBIOCHEM ProteoExtract™ Removal Kits (for Enhancing Resolution
of Low Abundance Proteins) (pdf)
NORGEN ProteoSpin™ Abundant Serum Protein Depletion Kit. The
kit depletes 70% of albumin, 90% of α-antitrypsin,
and 50% of transferin
and haptoglobin, enabling the visualization of
low abundance proteins. The kit is unique in that it is based
on an ion-exchange mechanism, silicon
carbide (SiC), and not the use of specific
antibodies. As a result, the kit can be used to deplete serum proteins
from a wide variety of samples,
including human and various animals. (pdf)
PIERCE: SwellGel® Blue Albumin Removal
Kit (pdf)
QIAGEN: Qproteome
Albumin/IgG Depletion Handbook. Fast and specific removal of albumin
and IgG from human serum and plasma samples.
Based on monoclonal antibodies that
bind HSA and human IgG with high affinity and specificity. (pdf)
SIGMA:
ProteoPrep 20 Plasma Immunodepletion
Kit is a complete kit with all necessary reagents
and consumable equipment to deplete 20
high abundance proteins from human
plasma or serum. This kit is designed to specifically remove the 20
proteins from human plasma.
Specifically, 8 mL of plasma may
be depleted in preparation for proteomic analysis, two-dimensional
electrophoresis (2DE), or
liquid chromatography (LC). (pdf).
VIVASCIENCE:
Vivapure® Anti-HSA Kit for Human Albumin Depletion
Highly
specific human albumin depletion with unique antibody fragments (pdf-I) (pdf-II) (pdf-IV)
(pdf-V)
Vivapure Anti-HSA Affinity Resin (pdf-III)
VIVASCIENCE:Vivapure® Anti-HSA/IgG Kits for Human Albumin and
Human Albumin/IgG Depletion (pdf)
Chromatofusing
GE-HEALTHCARE Chromatofusing Handbook (pdf)
GE-HEALTHCARE Ion Exchange Cromatography and Chromatofusing Handbook(pdf)
Crystallography
and Recombinant Methods
JENA Macromolecular
crystallography products. Crystallization Screens:
JBScreen Basic and JBScreen Membrane. Crystallization Optimization:
JBS Solubility Kit, JBS
Methylation Kit, JBScreen Plus, JBScreen Detergents, JBScreen Buffer
Kits and JBScreen Cryo (pdf)
JENA Crystallization Freshman Kit - Junior and Crystallization Freshman
Kit - Scholar are designed for screening of initial crystallization
conditions of
proteins, peptides, nucleic acids
and macromolecular complexes in order to grow single crystals suitable
for X-ray diffraction analysis. They include
everything you need to start your
crystallization experiment: pregreased sitting drop plates, cover
slides, our unique JBScreen reagents as well a
detailed user guide. (pdf-I) (pdf-II) (pdf-III) (pdf-IV) (pdf-V)
Derewenda
Z., The use of recombinant methods and molecular
engineering in protein crystallization. Methods
(2004), 34: 354–363
(pdf)
Smyth D.,
REVIEW Crystal structures of fusion proteins with
large-affinity tags.Protein Science (2003), 12:1313–1322 (pdf)
Geerlof A. et.al.
The
impact of protein characterization in structural
NORTHSTAR Enzyme Deglycosylation Kit. Contains all enzymes needed to
completely remove all N- & simple O-linked carbohydrates
from
glycoproteins (pdf)
QAbio
Enzymatic CarboRelease Kit will remove all
N-linked oligosaccharides and many O-linked oligosaccharides
from glycoproteins. N-links
(Asn-linked) are
removed using the enzyme PNGase F. In addition, all Ser/Thr-linked
(O-linked) Gal-(β1-3)-GalNAc-(α1) and all sialic acid
substituted
Gal-(β1-3)-GalNAc-(α1) will be removed using the combination
of Sialidase and O-Glycosidase. The addition of ß-Galactosidase
and
Hexosaminidase will assist in the deglycosylation of
larger O-link structures. (pdf)
PROZYME-GLYKO Enzymatic
Deglycosylation Kit. Contains all enzymes & reagents
needed to completely remove all N-linked & simple
O-linked
carbohydrates from glycoproteins (pdf)
ROCHE The
N-Glycosidase F Deglycosylation Kit can be used to
test for the existence of asparagine-linked glycan chains
on glycoproteins.
The
new Endoglycosidase H Deglycosylation Kit is useful
for testing the existence of “high mannose” type and
“hybrid” type asparagine-linked
glycan
chains on purified glycoproteins. (pdf-I)
(pdf-II)
SIGMA Deglycosylation
Selection Guide (pdf)
Expanded Bed Adsorption
GE-HEALTHCARE Introduction to Expanded Bed Adsorption (pdf)
GE-HEALTHCARE
Streamline Application Note (pdf)
GE-HEALTHCARE
Streamline Data File (pdf)
BIORAD
CHT Ceramic
Hydroxyapatite: Use in Expanded Bed Adsorption Mode
(pdf)
PALL BIOSEPRA Q & CM Ion Exchange Sorbents (pdf)
Gel Filtration
GE-HEALTHCARE Gel
Filtration Handbook (pdf)
GE-HEALTHCARE Gel Filtration of peptides - buffer conditions (pdf)
BioSepra Ultragel AcA - Size Exclusion Chromatography Sorbents (pdf)
MERCK Fractogel® EMD BioSEC (S) (pdf)
Pall Ultrogel®AcA Size Exclusion Chromatography Sorbents.
Polyacrylamide and agarose gel matrix (pdf)
Pall Trisacryl® GF05 M, LS Size Exclusion Chromatography
Sorbents. Designed for desalting and for the separation of small
molecules.
40-80 μm for M grade
& 80-160 μm for LS grade for fractionation at high flow with low
pressure, designed for industrial scale. (pdf)
TOSOH BIOSCIENCE
Size Exclusion Chromatography (pdf-I) (pdf-II) (pdf-III)
(pdf-IV)
BIORAD Bio-Gel® HT - Bio-Gel HTP DNA Grade Bio - Gel
HTP Hydroxyapatite - Instruction Manual (pdf)
BIORAD CHT Ceramic
Hydroxyapatite (pdf)
BIORAD CHT Ceramic
Hydroxyapatite: Use in Expanded Bed Adsorption Mode
(pdf)
BIORAD CFT Ceramic Fluoroapatite - A Chromatographic
Support for Protein Purifications Requiring Acidic Conditions
(pdf)
BIO RAD
Protein A removal from IgG on CHT Ceramic Hydroxyapatite Support
(pdf)
BIORAD Macro
Prep Chromatography Supports (pdf)
Pall
HA Ultragel Hydroxyapatite Chromatography
Sorbents
(pdf)
Ion Exchange Chromatography
GE-HEALTHCARE Ion Exchange Chromatography Manual (pdf)
GE-HEALTHCARE
Ion Exchange
Cromatography and Chromatofusing
Handbook (pdf)
GE-HEALTHCARE
Ion Exchange Media - Selection Guide
(pdf)
GE-HEALTHCARE Recommended buffers
for Anion Exchange Chromatography
GE-HEALTHCARE Recommended buffers for Cation
Exchange Chromatography
GE-HEALTHCARE Recommended Volatile
buffers systems for Ion Exchange Chromatography
GE-HEALTHCARE Capto adhere: a strong anion exchanger with multimodal
functionality ionic interaction, hydrogen bonding and
hydrophobic interaction.
Capto adhere is designed for post Protein A purification of
monoclonal antibodies. Removal of leached Protein A,
aggregates, host cell proteins,
nucleic acids and viruses from monoclonal antibodies is
performed in flowthrough mode at where the antibodies
pass directly through the
column while the contaminants are adsorbed. (pdf-I) (pdf-II) (pdf-III)
GE-HEALTHCARE Capto™ MMC: a multimodal cation exchanger.
Has
a multimodal ligand that may interact with target molecules
in several different ways. It
contains a carboxylic group and thus its features partly resemble those
of a weak cation exchanger. In addition to
the ionic interactions several other types of interactions are
involved, including hydrogen bonding and hydrophobic interaction. The design of
the ligand
enables binding of proteins at high conductivity.
(pdf-I)
(pdf-II)
(pdf-III)
GE-HEALTHCARE MacroCap™ SP is a highly porous
cation exchanger high available surface area for
adsorption of of large
biomolecules such as IgM and polyethylene glycol(PEG)-modified
proteins (i.e., PEGylated proteins) that are intended for use as
biopharmaceuticals.
(pdf)
GE-HEALTHCARE Q-Sepharose XL (anion exchange).
Q-Sepharose XL virus licensed. SP-Sepharose XL (cation
exchange) (pdf)
GE-HEALTHCARE Capto™ Q a strong anion
exchange medium for packed bed chromatography that
allows increased speed and
throughput in capture and intermediate purification. It combines high
capacity with high flow velocity and low backpressure (pdf)
BIORAD Macro-Prep
Ion Exchange Support - Instruction Manual
(pdf)
BIORAD UNOTMQ&S
Continuous (pdf) (pdf II)
BIOSEPRA Q, S, DEAE, CM Ceramic HyperD (pdf)
MERCK Cleaning and Regeneraton of Fractogel EMD sorbents
(pdf)
MERCK Ion
Exchange Chromatography Using Fractogel EMD
Tentacle Supports (pdf)
MERCK Fractoprep®
DEAE Weak Anion Exchange chromatography
(pdf)
MERCK Fractoprep®
SO3 - Strong Cation Exchange chromatography
(pdf)
MERCK Fractoprep®
TMAE Strong Anion Exchange (pdf)
MERCK Fractogel
EMD COO- (S) (M) Weak Cation
Exchange (pdf)
MERCK Fractogel
EMD DEAE (S) (M) Weak Anion Exchange (pdf)
MERCK Fractogel
EMD DMAE (S) (M) Weak Anion Exchange (pdf)
MERCK Fractogel EMD SE High Capacity (M) Strong Cation Exchange
(pdf)
MERCK Fractogel
EMD SO3- (S) (M)
Strong Cation Exchange (pdf)
MERCK Fractogel
EMD TMAE (S) (M) Strong Anion Exchange (pdf)
MERCK Fractogel
EMD TMAE High Capacity (M) Strong Anion Exchange
(pdf)
PIERCE
Pierce Strong Ion Exchange Spin Columns; use membrane-adsorbent
technology as a chromatographic matrix to fractionate proteins.
The spin column capacities are 4 mg
proteins/peptides for the mini and 60-80 mg protein for the maxi.
Actual capacity depends on the specific
protein sample, selected pH and salt condition.
(pdf)
Pall
Q,
S, DEAE, CM Ceramic HyperD ion exchangers. Of particular
value in process scale application, these sorbents are designed to
maintain
high dynamic binding capacity (DBC) under conditions
where conventional sorbents display significant capacity or
productivity limitations. (pdf)
Prepacked columns (pdf)
Pall BioSepra®
DEAE, CM and SP Trisacryl® M/LS. Spherical semi-rigid microbeads
of acrylic copolymers designed for ion exchange
chromatography of proteins. Microbial Stability. (pdf)
Pall Pall®
PRC Columns Prepacked Columns for Ion Exchange and Mixed-Mode Chromatography
(pdf)
Pall Purification of mouse IgM from cell culture supernatant
by Cation Exchange Chromatography on CM Ceramic Hyper D F sorbent (pdf)
SARTORIUS
SartobindTM - Membrane Adsorbers Discs and Cassettes
Reusable Sartobind Membrane Ion Exchangers for Adjustable Filter
Holders (pdf)
SARTORIUS Sartobind® Membrane
Adsorbers - A Separation Technology Based on Microporous
Membrane Ion Exchangers (pdf)
SARTORIUS Sartobind SingleSep
Disposable Capsules - A Separation Technology Based
on Microporous Membranes -Operating Instructions (pdf)
TOSOH BIOSCIENCE
TSK-GEL BioAssyst Series Ion Exchange Column (pdf)
TOSOH BIOSCIENCE
Ion Exchange Chromatography
(pdf)
VIVASCIENCE: Vivapure™
IEX kits include everything required for rapid purification
of protein samples or contaminant removal from protein
samples: clarification spin columns for initial
sample clearing, Vivapure spin columns and ready-to-use buffers in
different concentrations for
the protein bind-wash-elute
steps, and Vivaspin™ ultrafiltration devices for final sample
concentration and desalting. Basic and acidic protein
purification kits. (pdf)
Multimodal and Hydrophobic Charge-Induction
Chromatography
GE-HEALTHCARE Capto adhere: a strong anion exchanger with multimodal
functionality ionic interaction, hydrogen bonding and
hydrophobic interaction.
Capto adhere is designed for post Protein A purification of
monoclonal antibodies. Removal of leached Protein A,
aggregates, host cell proteins,
nucleic acids and viruses from monoclonal antibodies is
performed in flowthrough mode at where the antibodies
pass directly through the
column while the contaminants are adsorbed. (pdf-I) (pdf-II) (pdf-III)
GE-HEALTHCARE Capto™ MMC: a multimodal cation exchanger.
Has
a multimodal ligand that may interact with target molecules
in several different ways. It
contains a carboxylic group and thus its features partly resemble those
of a weak cation exchanger. In addition to
the ionic interactions several other types of interactions are
involved, including hydrogen bonding and hydrophobic interaction. The design of
the ligand
enables binding of proteins at high conductivity.
(pdf-I)
(pdf-II)
(pdf-III)
Pall BioSepra MEP
HYPER CELL Product Information (pdf)
Pall BioSepra MEP HYPER
CELL Product Note (pdf)
Pall Pall HEA and PPA HyperCel
operate on a "mixed-mode" mechanism, based on a combination of electrostatic
and hydrophobic properties
of the protein and ligands. Ligands: aliphatic (HEA
– hexylamine) and aromatic (PPA – phenylpropylamine)
amines, which offer different
selectivity and hydrophobicity options. (pdf)
Pall BioSepra Purification
of Antibodies (pdf) (pdf-II)
Pall BioSepra Validated Alternatives to Protein A Sorbents for Antibody
Production.
(pdf)
Pall Pall®
PRC Columns Prepacked Columns for Ion Exchange and Mixed-Mode Chromatography
(pdf)
CLONTECH: BD Phosphoprotein
Kit User Manual (pdf) (pdf-II) (pdf-III)
QIAGEN Phosphoprotein
Purification Kit. For purification
and analysis of phosphorylated proteins from eukaryotic
cells (pdf-I)
(pdf-II)
Polyubiquitin-modified proteins
PIERCE Ubiquitin
Enrichment Kit. For the isolation and study of
intracellular polyubiquitin-modified proteins. Through
the use of a
high-binding
affinity resin, polyubiquitinated proteins are isolated from cell or
tissue lysates. The bound proteins can then be eluted
from the affinity resin and analyzed using the anti-ubiquitin antibody. (pdf)
INTEGRITY BIOSOLUTION Protein Aggregation
(page)
Eiler S., Overexpression,
Purification, and Crystal Structure of Native
ER alphaLBD
Protein Expression
and Purification (2001) 22, 165–173 (pdf)
Bondos S., Detection and prevention of protein aggregation before, during, and after purification.
Analytical Biochemistry
Hamada H., Effect of additives on Protein Aggregation
Current Pharmac. Biotech. (2009), 10, 400-407 (pdf)
Philo J., Mechanisms of Protein Aggregation
Current Pharmac. Biotech.
(2009), 10, 348-351 (pdf)
NOVAGEN Enhancing
solubility during protein expression in E. Coli (site)
(site-II)
PROTEIN
EXPRESSION FACILITY OF THE HEBREW UNIVERSITY OF JERUSALEM
Heat
shock growth procedure
MOLECULAR PROBES Biotin-XX Microscale Protein Labeling Kit. This kit
has been optimized for labeling small amounts
(20–100 μg) of purified proteins with
molecular weights between 12 and 150 kDa, and contains everything
needed
to perform three labeling reactions and to separate
the resulting conjugates from excess reactive biotin.(pdf)
MOLECULAR PROBES
FluoReporter ®Biotin Quantitation Assay Kit for biotinylated
proteins. Sensitive fluorometric assay for
accurately
determining the number of biotin labels on a protein. The assay can
detect from 4 to 80 pmol of biotin in a sample. (pdf)
Protein Refolding
/ Inclusion Bodies
GE-HEALTHCARE
Purifying Challenging Proteins: Membrane proteins, Multiprotein
complexes and Inclusion bodies (pdf)
AVIDIS-TECHNOLOGY
Refolding Chromatography
Refolding
Chromatography with Mini-Chaperones (pdf)
BIO-VECTRA Vectrase AT - Folding Proteins
with Disulfide Bands
BIO-VECTRA Vectrase
CD - Quick Screening of Refolding
Conditions (pdf)
BIO-VECTRA Vectrase DK - Refolding at High Protein Concentration
BIO-VECTRA Vectrase
P - Protein Disulfide Isomerase (PDI) Mimic
(pdf-I)(pdf-II)
GENO-Protein
Foldase-Protein Folding Optimization Kit
NORGEN The ProteoSpin™ Inclusion Body Isolation Kit. Facilitates
the isolation of recombinant proteins in the form
of inclusion bodies from E.
coli. The
kit includes reagents specially formulated to achieve
rapid and high-quality purification of inclusion body proteins
using three processes:
1. Lysis
of bacterial cells to release inclusion bodies in solid form
2. Solubilization of purified inclusion bodies
3. Purification of the recombinant protein using
spin column chromatography with Norgen’s proprietary resin as an
ion-exchanger
Each spin column
is able to purify up to 12 mg of recombinant proteins
from 100 mL of culture. The kit is designed to purify both
acidic and
basic proteins. (pdf Maxi
Kit) (pdf Micro
Kit)
NOVAGEN Enhancing solubility
during protein expression in E. Coli (site)
(site-II)
NOVAGEN-Protein
Refolding kit (pdf)
NOVAGEN Information on Protein Refolding
(pdf)
NOVAGEN
iFOLD™ Protein
Refolding System . The system includes inclusion
body purification reagents combined with a dispensed 96-well
plate-based
protein refolding buffer matrix. (pdf-I)
(pdf-II)
NOVEXIN
The technology and reagents protect the protein
during vulnerable steps in the refolding process,
providing an opportunity for the
protein
to refold corrctly, reducing losses due to aggregation.
Employs
linear carbohydrate polymers of ~5kDa that enhance
protein solubility and stability through the formation
of reversible complexes with
proteins
without altering their structure and preventing
aggregation.
Protein Refolding Starter
Kit (pdf)
Stability P.A.C.
(pdf)
Acidic Protein Refolding Kit (pdf)
Basic Protein Refolding Kit (pdf)
Refolding Kit for Histidine-tagged proteins
(pdf-I) (pdf-II)
Bulk Protection and Release Reagents
(pdf)
PIERCE Pro-MatrixTM
Protein Refolding Kit (pdf)
Additives
Used to Increase Folding and Prevent Aggregation
PROTEIN
EXPRESSION FACILITY OF THE HEBREW UNIVERSITY OF JERUSALEM
Heat
shock growth procedure
PROTEIN
EXPRESSION AND PURIFICATION FACILITY OF THE
EUROPEAN MOLECULAR BIOLOGY LABORATORY
In
vitro denaturation and refolding
Contaminant Removal from Inclusion
Bodies Before Solubilization
UNIVERSITY OF OKLAHOMA School of Chemical
Engineering and Materials Science Recombinant Protein Solubility
Prediction
Recommended Reading
Altamirano M., Refolding Chromatography with Immobilized Mini-Chaperones.
PNAS 1997, 94: 3576-3578 (pdf)
Armstrong N., A
New Protein Folding Screen...etc. Protein Science
1999, 8: 1475-1483 (pdf)
Chen G.,
Overexpression of a Glutamate Receptor (GluR2) ligand
binding domain in E.Coli: Application of a novel protein
folding screen (pdf)
De Bernardez
Clark E.,Refolding of RecombinantProteins
. Current Opinion in Biotechnology 1998,9:157–163
(pdf)
De Bernardez Clark E.,
Protein refolding for industrial
processes. Current Opinion
in Biotechnology 2001, 12:202–207
(pdf).
Eiler S., Overexpression,
Purification, and Crystal Structure
of Native ER alphaLBD Protein
Expression and Purification (2001) 22,
165–173 (pdf)
Machida S., Cycloamylose as
an efficient artificial chaperone for
protein refolding. FEBS Letters 486
(2000) 131-135 (pdf)
Middelberg A., Preparative
Protein Folding. TRENDS in Biotechnology
2002, 20 (10):
437-443 (pdf)
Ming Li et al., In vitro
protein refolding by chromatographic
procedures. Protein Expr.
and Purif. 2004,33: 1-10
(pdf)
Tsumoto
K., Practical Considerations
in Refolding Proteins from Inclusion
Bodies. Protein Expr. and Purif.
2003,28: 1-8 (pdf)
Reverse
Phase Chromatography
GE-HEALTHCARE
Hydrophobic Interaction and
Reversed Phase Chromatography Principles and Methods (pdf)
GE-HEALTHCARE
Reverse Phase Chromatography
Manual (pdf)
TOSOH BIOSCIENCE
Reverse
Phase Chromatography Brochure (pdf)
VYDAC The Handbook of Analysis
and Purification of Peptides
and Proteins by Reverse-Phase HPLC
(pdf)
Simulated Moving Bed Chromatography
SEMBA Biosciences: Poster: Continuous highly efficient protein purification using simulated moving bed chromatography (pdf)
SEMBA Biosciences: Application Note: The Semba Octave™ Chromatography System. Simulated moving bed chromatography. Continuous Affi nity
Puri cation of Recombinant Proteins (pdf)
SEMBA Biosciences:
The Semba Octave™ Chromatography System. A simulated
moving bed chromatography system. Continuous unattended
purification,
milligrams to
grams. Compatible with chemical and biological samples. SMBC
emulates countercurrent separation where the mobile phase flows in the
opposite
direction of the stationary phase. The stationary phase is represented
by individual columns connected in series, and the mobile phase by
inlet streams
of Feed and Desorbent and outlet streams of Raffinate and Extract. (pdf)
Storage
of Purified Proteins
PROTEIN
EXPRESSION AND PURIFICATION FACILITY OF THE EUROPEAN
MOLECULAR BIOLOGY LABORATORY
Storage of Purified Proteins
PIERCE
Protein
stability and storage (pdf)
Thiophilic
Chromatography
CLONTECH:
Thiophilic - Purification of Immunoglobulins
(pdf)
CLONTECH: Protein
Purification Products (pdf)
GE-HEALTHCARE Activated Thiol Sepharose 4B reacts
with solutes containing thiol groups under
mild conditions to form mixed disulphides.
This reaction
forms the basis of covalent chromatography and
a procedure for immobilizing thiol containing biomolecules.
(pdf)
GE-HEALTHCARE
Thiopropyl Sepharose (pdf)
MERCK Fractogel Thiophilic (pdf)
PIERCE: T-Gel™ Purification
Kit (pdf)
MILLIPORE PROSEP-Thiosorb
and PROSEP-Thiosorb M Chromatography Media - for the recovery
and purification of Immunoglobulins (pdf)
ADEMTECH
Viro-Adembeads are specifically developed magnetic particles
to capture viruses from biological samples. Following incubation
in a virus
containing sample, Viro-Adembeads associated to viruses are recovered
and can be directly used to infect target cells increasing
infection efficiency. The mechanism
of virus capture is based on electrosteric interactions (pdf-I) (pdf-II)
GE-HEALTHCARE Q-Spharose XL (anion exchange). Q-Spharose
XL virus licensed. SP-Spharose XL (cation exchange)
(pdf)
GE-HEALTHCARE Rapid Adenovirus Purification
Using Q-Spharose XL (pdf-I) or Source 15Q (pdf-II)
GE-HEALTHCARE AVB
Sepharose™ High Performance is an affinity medium designed
for the purification of adeno associated
virus (AAV). The
ligand, a 14 kD recombinant protein, is attached to the base
matrix via a long, hydrophilic spacer arm to make it easily
available
for binding of the virus (pdf)
CLONTECH: Adeno-X™
Virus Purification Kits User Manual (pdf-I)
Protocol (pdf-II).
A complete filtration-based system for purifying
and
concentrating
recombinant adenovirus. It provides a superior
alternative to cesium chloride (CsCl) density gradient
centrifugation. Use an
adsorbent membrane
that selectively binds adenoviral particles based
on their distinctive surface-associated properties.
CHISSO Corp
MILLIPORE Matrex
Cellufine Sulfate - For concentration, purification
and depyrogenation of Virus, Viral/Microbial Antigen,
Heparin binding proteins (pdf-I)
(pdf_II) References:
(pdf-III)
Pall Dynamic High
Capacity Mustang® Q Membrane Units for Scaleable Anion
Exchange Chromatography Purification of Adenoviral
Vectors (pdf)
VIVASCIENCE:
Vivapure® AdenoPACK™ 100. Adenovirus
(Ad5) purification and concentration kit for up to 100 ml
cell culture volume.
AdenoPACK
syringe filters containing an ion exchange membrane
adsorber that binds adenoviral particles. (pdf-I) (pdf-II)
(pdf-III)
Entries
since September 2006
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