P3296
Protein G Sepharose™, Fast Flow
recombinant, expressed in E. coli, aqueous ethanol suspension
동의어(들):
Protein G-Agarose, Fast Flow from Streptococcus sp.
재조합
expressed in E. coli
Quality Level
양식
aqueous ethanol suspension
분석물 화학적 분류
proteins (Immunoglobulins of various mammalian species)
라벨링 범위
~2 mg per mL
기술
affinity chromatography: suitable
Matrix
Sepharose 4B Fast Flow
기질 활성
cyanogen bromide
기질 부착
amino
기질 스페이서
1 atom
저장 온도
2-8°C
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일반 설명
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
애플리케이션
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.
물리적 형태
Suspension in 20% ethanol
제조 메모
Prepared with recombinant streptococcal Protein G from which the albumin-binding region has been genetically deleted
법적 정보
Sepharose is a trademark of Cytiva
신호어
Warning
유해 및 위험 성명서
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
Elena Kotova et al.
PLoS genetics, 5(2), e1000387-e1000387 (2009-02-21)
Recently, the nuclear protein known as Poly (ADP-ribose) Polymerase1 (PARP1) was shown to play a key role in regulating transcription of a number of genes and controlling the nuclear sub-organelle nucleolus. PARP1 enzyme is known to catalyze the transfer of
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
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
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
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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Techniques for protein antigen molecular weight determination, protein interactions, enzymatic activity, and post-translational modifications.
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