gsts

HPGDS PGD2 Protein, Human, Recombinant (His) is expressed in E. coli expression system with His tag. The predicted molecular weight is 24.2 kDa and the accession number is O60760.

Hematopoietic Prostaglandin D Synthase (HPGDS) belongs to the GST superfamily and Sigma family. HPGDS contains one GST C-terminal domain and one GST N-terminal domain. HPGDS is highly expressed in adipose tissue, macrophages, and placenta, and it exists in the form of homodimer in living body. HPGDS is a cytosolic enzyme that isomerizes PGH(2). HPGDS is a bifunctional enzyme that catalyzes both the conversion of PGH2 to PGD2 and also shows low glutathione-peroxidase activity towards cumenehydroperoxide.

GSTK1 gene encodes a member of the kappa class of the glutathione transferase superfamily of enzymes that function in cellular detoxification. Glutathione S-transferases (GSTs) are a family of enzymes that catalyze a variety of reactions in both eukaryotes and prokaryotes. They catalyze the conjugation of reduced glutathione with potentially toxic, xenobiotic substrates, thus aiding excretion from the body. GSTK1(glutathione S-transferase kappa 1) is localized to the peroxisome and catalyzes the conjugation of glutathione to a wide range of hydrophobic substates facilitating the removal of these compounds from cells. GSTK1 functions in cellular detoxification.

GSTZ1 (Glutathione S-Transferase Zeta 1) is a Protein Coding gene. 3 alternatively spliced human isoforms have been reported. GSTZ1 gene is a member of the glutathione S-transferase (GSTs) super-family which encodes multifunctional enzymes important in the detoxification of electrophilic molecules, including carcinogens, mutagens, and several therapeutic drugs, by conjugation with glutathione. GSTZ1 is a bifunctional protein that has minimal glutathione-conjugating activity with ethacrynic acid and 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole and maleylacetoacetate isomerase activity. GSTZ1 catalyzes the glutathione-dependent oxygenation of dichloroacetic acid to glyoxylic acid. GSTZ1 participates in the catabolism of phenylalanine and tyrosine. Thus defects in GSTZ1 cause harsh metabolic disorders including alkaptonuria, phenylketonuria, and tyrosinemia.

Glutathione S-transferase P (GSTP1) is an enzyme that contains 1 GST C-terminal domain, 1 GST N-terminal domain. GSTP1 belongs to the GST superfamily, the GSTs are a family of enzymes that play an important role in detoxification by catalyzing the conjugation of many hydrophobic and electrophilic compounds with reduced glutathione. Based on their biochemical, immunologic, and structural properties, the soluble GSTs are categorized into 4 main classes: alpha, mu, pi, and theta. The glutathione S-transferase pi gene (GSTP1) is a polymorphic gene encoding active, functionally different GSTP1 variant proteins. Besides, it regulates negatively CDK5 activity via p25 p35 translocation to prevent neurodegeneration. It thought to function in xenobiotic metabolism and play a role in susceptibility to cancer, and other diseases.

GSTA1 (Glutathione S-Transferase Alpha 1) is a Protein Coding gene. This gene encodes a member of a family of enzymes that function to add glutathione to target electrophilic compounds. Glutathione S-transferases (GSTs) are involved in the detoxification of carcinogens and may be linked to carcinogenesis. As a vital component of GSTs, GSTA1 plays an important role in carcinogenesis. GSTA1 expression may be a target molecule in the early diagnosis and treatment of lung cancer. Human colonic adenocarcinoma (Caco-2) cells in culture undergo spontaneous differentiation into mature enterocytes in association with progressive increases in expression of glutathione S-transferase alpha-1 (GSTA1). GSTA1 levels may play a role in modulating enterocyte proliferation but do not influence differentiation or apoptosis. GSTA1 may play a key role during pregnancy.

Glutathione S-transferase Mu 2, also known as GST class-mu 2, GSTM2-2, and GSTM2, is a cytoplasm protein that belongs to the GST superfamily and Mu family. GSTM2 GST4 contains one GST C-terminal domain and one GST N-terminal domain. The glutathione S-transferases (GSTs) are a multigene family of enzymes largely involved in the detoxification of chemicals. Eight distinct classes of the soluble cytoplasmic mammalian glutathione S-transferases have been identified: alpha, kappa, mu, omega, pi, sigma, theta, and zeta. Butyrate, an important luminal component produced from the fermentation of dietary fibers, is an efficient inducer of GSTs and especially of GSTM2. Butyrate may act chemoprotective by increasing detoxification capabilities in the colon mucosa.