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P3296

Protein G Sepharose™, Fast Flow

recombinant, expressed in E. coli, aqueous ethanol suspension

Synonym(s):

Protein G-Agarose, Fast Flow from Streptococcus sp.

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About This Item

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

Key Documents

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Product Name

Protein G Sepharose™, Fast Flow, recombinant, expressed in E. coli, aqueous ethanol suspension

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

Quality Level

200

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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.

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

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

signalword

Warning

hcodes

H226

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
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Certificates of Analysis (COA)

Lot/Batch Number
MKCZ2196
0000376276
0000312799
0000376276
0000312799

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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
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
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
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
Yi-Jye Chern et al.
Cell death & disease, 10(7), 504-504 (2019-06-28)
Therapy-refractory disease is one of the main contributors of treatment failure in cancer. In colorectal cancer (CRC), SPARC can function as a sensitizer to conventional chemotherapy by enhancing apoptosis by interfering with the activity of Bcl-2. Here, we examine a
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