Skip to Content
Merck
All Photos(1)

Key Documents

View All Documentation

P3296

Millipore

Protein G Sepharose™, Fast Flow

recombinant, expressed in E. coli, aqueous ethanol suspension

Synonym(s):

Protein G-Agarose, Fast Flow from Streptococcus sp.

Sign Into View Organizational & Contract Pricing
All Photos(1)

About This Item

MDL number:
MFCD00165580
UNSPSC Code:
41106500
NACRES:
NA.56

recombinant

expressed in E. coli

form

aqueous ethanol suspension

analyte chemical class(es)

proteins (Immunoglobulins of various mammalian species)

extent of labeling

~2 mg per mL

technique(s)

affinity chromatography: suitable

matrix

Sepharose 4B Fast Flow

matrix activation

cyanogen bromide

matrix attachment

amino

matrix spacer

1 atom

storage temp.

2-8°C

Looking for similar products? Visit Product Comparison Guide

Related Categories

General description

Protein G is an immunoglobulin (IgG)-binding bacterial cell wall protein isolated from group G streptococcal strain, G-148. This protein can be extracted from the cells by papain digestion and purified by the sequential use of ion-exchange chromatography on DEAE-Sephadex, affinity chromatography on Sepharose-coupled human IgG, and gel chromatography on Sephadex G-200. The binding between protein G and various polyclonal and monoclonal IgG is basically pH dependent between 2.8 and 10, with the strongest binding at pH 4 and 5, and weakest at pH 10. It acts as a powerful reagent for the detection of IgG.
Protein G is an immunoglobulin (IgG)-binding bacterial cell wall protein isolated from group G streptococcal strain, G-148. This protein can be extracted from the cells by papain digestion and purified by the sequential use of ion-exchange chromatography on DEAE-Sephadex, affinity chromatography on Sepharose-coupled human IgG, and gel chromatography on Sephadex G-200. The binding between protein G and various polyclonal and monoclonal IgG is basically pH dependent between 2.8 and 10, with the strongest binding at pH 4 and 5, and weakest at pH 10. It acts as a powerful reagent for the detection of IgG.

P3296-5Ml′s updated product number is GE17-0618-01

Application

Protein G-Sepharose™ is used in affinity chromatography, protein chromatography, antibody purification and characterization, immunoaffinity matrices, protein A, G and L resins, protein interaction, and purification and detection. Protein G-Sepharose™ has been used to develop a strategy to confirm the presence of anti-erythropoietin neutralizing antibodies in human serum as well as to compare methods for depletion of albumin and IgG from equine serum.

Physical form

Suspension in 20% ethanol

Preparation Note

Prepared with recombinant streptococcal Protein G from which the albumin-binding region has been genetically deleted

Legal Information

Sepharose is a trademark of Cytiva

Pictograms

Flame
GHS02

Signal Word

Warning

Hazard Statements

H226

Hazard Classifications

Flam. Liq. 3

Storage Class Code

3 - Flammable liquids

WGK

WGK 3

Flash Point(F)

115.0 °F - closed cup

Flash Point(C)

46.1 °C - closed cup

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Aaron Pinnola et al.
The Journal of biological chemistry, 282(44), 32511-32519 (2007-09-11)
Poly(ADP-ribose) polymerase 1 protein (PARP1) mediates chromatin loosening and activates the transcription of inducible genes, but the mechanism of PARP1 regulation in chromatin is poorly understood. We have found that PARP1 interaction with chromatin is dynamic and that PARP1 is
B Akerström et al.
The Journal of biological chemistry, 261(22), 10240-10247 (1986-08-05)
Protein G, an IgG-binding molecule, was prepared from the cell walls of a group G streptococcal strain, G-148. The protein could be extracted from the cells by papain digestion and purified by the sequential use of ion-exchange chromatography on DEAE-Sephadex
Cristina Hidalgo-Carcedo et al.
Nature cell biology, 13(1), 49-58 (2010-12-21)
Collective cell migration occurs in a range of contexts: cancer cells frequently invade in cohorts while retaining cell-cell junctions. Here we show that collective invasion by cancer cells depends on decreasing actomyosin contractility at sites of cell-cell contact. When actomyosin
Kyle A Nilson et al.
Nucleic acids research, 45(19), 11088-11105 (2017-10-05)
Oxidative stress has pervasive effects on cells but how they respond transcriptionally upon the initial insult is incompletely understood. We developed a nuclear walk-on assay that semi-globally quantifies nascent transcripts in promoter-proximal paused RNA polymerase II (Pol II). Using this
G Yang et al.
Oncogene, 26(1), 91-101 (2006-06-27)
The t(8;21) chromosomal translocation that generates the fusion oncoprotein RUNX1-ETO predominates in leukemia patients of the French-American-British (FAB) class M2 subtype. The oncoprotein has the capacity to promote expansion of hematopoietic stem/progenitor cells and induces leukemia in association with other
View All Related Papers

Protocols

Immunoprecipitation Procedure

Techniques for protein antigen molecular weight determination, protein interactions, enzymatic activity, and post-translational modifications.

Immunoprecipitation Procedure

Techniques for protein antigen molecular weight determination, protein interactions, enzymatic activity, and post-translational modifications.

Immunoprecipitation Procedure

Techniques for protein antigen molecular weight determination, protein interactions, enzymatic activity, and post-translational modifications.

Immunoprecipitation Procedure

Techniques for protein antigen molecular weight determination, protein interactions, enzymatic activity, and post-translational modifications.

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service