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GST-Tag

Principal name

GST-Tag antibody

Selected pictures

SM6024 - Western blot analysis: Recombinant GST (28 kDa) and GST-fusion protein (61 kDa) were resolved by SDS-PAGE, transferred to PVDF membrane and probed with anti-GST antibody (1:1000). Proteins were visualized using a goat anti-mouse secondary antibody conjugated to HRP and an ECL detection system. Arrows indicate GST and GST-fusion proteins (20 ng).

Gene ID

2950 (GSTP1)

Ncbi ID

6182, NP_000843.1

Available reactivities

Sj (Stapylococcus japonicum), E. coli (Escherichia coli), Mam (Mammalia), Hu (Human), Ms (Mouse), Rt (Rat)

Available hosts

Mouse, Rabbit, Goat, Chicken

Available applications

Enzyme Immunoassay (E), Western blot / Immunoblot (WB), Immunoprecipitation (IP), Immunocytochemistry/Immunofluorescence (ICC/IF), Frozen Sections (C), Immunoelectron Microscopy (EM), Flow Cytometry (F), Paraffin Sections (P), Dot blot (Dot), ELISA (capture) (E(capture)), ELISA (detection) (E(detection))

Background of GST-Tag antibody

Glutathione S-transferase (GST) represents a major group of detoxification enzymes. This enzyme acts by catalyzing the reaction of glutathione with an acceptor molecule to form an S-substituted glutathione (S=sulfur). The reactions utilizing glutathione contribute the transformation of a wide range of compounds, including carcinogens, therapeutic drugs, and products of oxidative stress. As well as its enzymatic activities, GST may also bind toxins and function as transport protein. Because of this, an early term for GSTs was ligandin. Glutathione S-transferase was originally separated from Schistosoma japonicum but currently isolated from recombinant E.coli source. Recombinant GST was expressed in E.coli and purified by conventional chromatography techniques.

General readings

This product has been used in:

Lehti K et al. Oligomerization through hemopexin and cytoplasmic domains regulates the activity and turnover of membrane-type 1 matrix metalloproteinase. J Biol Chem 277:8440-8 (2002).

Chen, P-L., Chen, C-F., Chen, Y., Xiao, J., Sharp, Z.D. and Lee, W-H. (1998) The BRC repeats in BRCA2 are Critical for RAD51 Binding and Resistance to Methyl Methanesulfonate Treatment. Proc Natl Acad Science, USA 95:5287-5292. 1998

Carlos M. Luque, Carmen M. Pérez-Ferreiro, Alicia Pérez-González, Ludwig Englmeier, Maria D. Koffa, and Isabel Correas. An Alternative Domain Containing a Leucine-rich Sequence Regulates Nuclear Cytoplasmic Localization of Protein 4.1R. J. Biol. Chem., Jan 2003; 278: 2686 - 2691. 2003