Skip to Content
Merck
CN

P3296

Protein G Sepharose, Fast Flow

recombinant, expressed in E. coli, aqueous ethanol suspension

Synonym(s):

Protein G-Agarose, Fast Flow from Streptococcus sp.

Sign In to View Organizational & Contract Pricing.

Select a Size

Change View

About This Item

UNSPSC Code:
41106500
NACRES:
NA.56
MDL number:
Form:
aqueous ethanol suspension
Recombinant:
expressed in E. coli
Technical Service
Need help? Our team of experienced scientists is here for you.
Let Us Assist


recombinant

expressed in E. coli

Quality Level

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

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.

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

signalword

Warning

hcodes

Hazard Classifications

Flam. Liq. 3

Storage Class

3 - Flammable liquids

wgk

WGK 3

flash_point_f

115.0 °F - closed cup

flash_point_c

46.1 °C - closed cup

Regulatory Information

常规特殊物品

This item has



Choose from one of the most recent versions:

Certificates of Analysis (COA)

Lot/Batch Number

Don't see the Right Version?

If you require a particular version, you can look up a specific certificate by the Lot or Batch number.

Already Own This Product?

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

Visit the Document Library


Protocols

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

Related Content

Find protein research tools to prepare, isolate, and analyze proteins. Organized by how to extract, protect, purify, enrich, modify, and quantify proteins.

View All Related Content

Cordula M Stover et al.
Journal of immunology (Baltimore, Md. : 1950), 180(5), 3313-3318 (2008-02-23)
Properdin is a positive regulator of complement activation so far known to be instrumental in the survival of infections with certain serotypes of Neisseria meningitidis. We have generated a fully backcrossed properdin-deficient mouse line by conventional gene-specific targeting. In vitro
Debby Kruijsen et al.
Journal of immunology (Baltimore, Md. : 1950), 185(11), 6489-6498 (2010-10-26)
Following infection with respiratory syncytial virus (RSV), reinfection in healthy individuals is common and presumably due to ineffective memory T cell responses. In peripheral blood of healthy adults, a higher CD4(+)/CD8(+) memory T cell ratio was observed compared with the
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



Global Trade Item Number

SKUGTIN
P3296-2ML04061838249630
P3296-1ML04061838099730
P3296-5ML04061838087539