SRP6097
GSTA1 human
recombinant, expressed in E. coli, ≥90% (SDS-PAGE)
别名:
GST2, GSTA1-1, GTH1, Glutathione S-transferase alpha 1
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关于此项目
Form:
liquid
Assay:
≥90% (SDS-PAGE)
Biological source:
human
Recombinant:
expressed in E. coli
Mol wt:
25.6 kDa
biological source
human
recombinant
expressed in E. coli
assay
≥90% (SDS-PAGE)
form
liquid
mol wt
25.6 kDa
packaging
pkg of 100 μg
NCBI accession no.
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... GSTA1(2938)
General description
Glutathione S-transferase A1 in humans is encoded by the GSTA1 gene. Cytosolic and membrane-bound forms of glutathione S-transferase are encoded by two distinct supergene families. These enzymes function in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding these enzymes are known to be highly polymorphic. GSTA1 protects the cells from reactive oxygen species and is highly expressed in liver.
The gene encoding GSTA1 is localized on human chromosome 6p12.2.
Biochem/physiol Actions
GSTA1 (Glutathione S-transferase α1) is associated with the biosynthesis of steroids such as testosterone and progesterone. It plays a vital role in double bond isomerase activity. GSTA1 converts δ(5)-androstene-3,17-dione to δ(4)-androstene-3,17-dione. It has a role in the metabolism of several xenobiotics.
Physical form
1 mg/mL solution in 20 mM Tris-HCl buffer (pH 8.0) containing 1 mM DTT and 10% glycerol.
Preparation Note
Centrifuge the vial prior to opening.
Other Notes
MAEKPKLHYF NARGRMESTR WLLAAAGVEF EEKFIKSAED LDKLRNDGYL MFQQVPMVEI DGMKLVQTRA ILNYIASKYN LYGKDIKERA LIDMYIEGIA DLGEMILLLP VCPPEEKDAK LALIKEKIKN RYFPAFEKVL KSHGQDYLVG NKLSRADIHL VELLYYVEEL DSSLISSFPL LKALKTRISN LPTVKKFLQP GSPRKPPMDE KSLEEARKIF RF
signalword
Warning
hcodes
Hazard Classifications
Eye Irrit. 2
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
新产品
此项目有
Crystal structure of human glutathione S-transferase A3-3 and mechanistic implications for its high steroid isomerase activity.
Yijun G, et al.
Biochemistry, 43(43) (2004)
Functional polymorphism of human glutathione transferase A3: effects on xenobiotic metabolism and steroid biosynthesis.
Tetlow N, et al.
Pharmacogenetics, 657-663 (2004)
Knockout and transgenic mice in glutathione transferase research.
Henderson CJ and Wolf CR
Drug Metabolism Reviews, 43(2), 152-164 (2011)
Kaspars Tars et al.
Journal of molecular biology, 397(1), 332-340 (2010-01-20)
Glutathione transferases (GSTs) are abundant enzymes catalyzing the conjugation of hydrophobic toxic substrates with glutathione. In addition to detoxication, human GST A3-3 displays prominent steroid double-bond isomerase activity; e.g. transforming Delta(5)-androstene-3-17-dione into Delta(4)-androstene-3-17-dione (AD). This chemical transformation is a crucial
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