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.
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