Description
Glutathione S-transferase mu 3, also known as GSTM3, is member of the glutathione s-transferase (GST) family of proteins. There are eight families of GST proteins, namely alpha, kappa, mu, omega, pi, sigma, theta and zeta, each of which is composed of proteins that have a variety of functions throughout the cell. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. Recombinant human GSTM3 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.
7801 | GSTM3 human recombinant DataSheet
Biomolecule/Target: GSTM3
Synonyms: Glutathione S-transferase mu 3, GST5, GSTB, GSTM3-3, GTM3
Alternates names: Glutathione S-transferase mu 3, GST5, GSTB, GSTM3-3, GTM3
Taglines: Functions in the detoxification of electrophilic compounds
NCBI Gene ID #: 2323
NCBI Gene Symbol: Flt3-L
Gene Source: Human
Accession #: P49771
Recombinant: Yes
Source: E. coli.
Purity by SDS-PAGEs: 98%
Assay: SDS-PAGE
Purity: N/A
Assay #2: N/A
Endotoxin Level: N/A
Activity (Specifications/test method): N/A
Biological activity: Specific activity > 4.7 units/mg, one unit is defined as the amount of enzyme that conjugate 1.0 µmole of 1-chloro-2, 4-dinitrobenzene (CDNB), with reduced glutathione per minute pH 6.5 at 25ºC.
Results: Specific activity > 4.7 units/mg
Binding Capacity: N/A
Unit Definition: One unit is defined as the amount of enzyme that conjugate 1.0 µmole of 1-chloro-2, 4-dinitrobenzene (CDNB), with reduced glutathione per minute pH 6.5 at 25ºC.
Molecular Weight: 29.1 kDa (249 aa, 1-225 aa)
Concentration: 1 mg/ml
Appearance: Liquid
Physical form description: 1 mg/ml solution 20 mM Tris-HCl buffer, pH 8.0, 10% glycerol, 1 mM DTT and 100 mM NaCl.
Reconstitution Instructions: N/A
Amino acid sequence: MGSSHHHHHH SSGLVPRGSH MGSHMSCESS MVLGYWDIRG LAHAIRLLLE FTDTSYEEKR YTCGEAPDYD RSQWLDVKFK LDLDFPNLPY LLDGKNKITQ SNAILRYIAR KHNMCGETEE EKIRVDIIEN QVMDFRTQLI RLCYSSDHEK LKPQYLEELP GQLKQFSMFL GKFSWFAGEK LTFVDFLTYD ILDQNRIFDP KCLDEFPNLK AFMCRFEALE KIAAYLQSDQ FCKMPINNKM AQWGNKPVC