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
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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
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
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
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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
B Akerström et al.
Journal of immunology (Baltimore, Md. : 1950), 135(4), 2589-2592 (1985-10-01)
Protein G is an immunoglobulin (IgG)-binding bacterial cell wall protein recently isolated from group G streptococci. We have investigated the avidity of protein G for various monoclonal and polyclonal Ig of the IgG class, and compared it with the binding
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
Rajesh P Ringe et al.
Journal of virology, 94(6) (2019-12-20)
We covalently attached human immunodeficiency virus type 1 (HIV-1) Env SOSIP trimers to iron oxide nanoparticles (IO-NPs) to create a particulate immunogen for neutralizing antibody (NAb) induction. The attached trimers, ∼20 per particle, retained native-like antigenicity, judged by reactivity with
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
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