P3296
Protein G Sepharose™, Fast Flow
recombinant, expressed in E. coli, aqueous ethanol suspension
동의어(들):
Protein G-Agarose, Fast Flow from Streptococcus sp.
제품 이름
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
저장 등급
3 - Flammable liquids
wgk
WGK 3
flash_point_f
115.0 °F - closed cup
flash_point_c
46.1 °C - closed cup
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
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
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
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
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