GSTT1
GSTT1 (glutathione S-transferase theta 1) is a cytoplasmic enzyme of the theta class that conjugates reduced glutathione to hydrophobic electrophiles. It belongs to the soluble glutathione S-transferases and also shows glutathione peroxidase activity with cumene hydroperoxide. Browse Assay Genie's current range of GSTT1 research reagents below, or read on for the biology behind the target.
GSTT1 catalyses the conjugation of reduced glutathione to a wide range of exogenous and endogenous hydrophobic electrophiles. Reported substrates include 1,2-epoxy-3-(4-nitrophenoxy)propane, phenethylisothiocyanate, 4-nitrobenzyl chloride and 4-nitrophenethyl bromide. The enzyme also displays glutathione peroxidase activity with cumene hydroperoxide, so it can act on organic hydroperoxides as well as on electrophilic compounds. Researchers studying xenobiotic metabolism and cellular defence against reactive chemicals often use GSTT1 as a reference point, whether they work with a GSTT1 antibody, a GSTT1 ELISA kit or recombinant GSTT1 protein.
Human glutathione S-transferases fall into five main classes: alpha, mu, pi, theta and zeta. GSTT1 belongs to the GST superfamily and the theta family, which also includes GSTT2 and GSTT2B. GSTT1 and GSTT2/GSTT2B share 55% amino acid sequence identity. The protein is found in the cytoplasm, and the GSTT1 gene is catalogued by HGNC in the group of soluble glutathione S-transferases. Mouse and rat each have a Gstt1 ortholog.
The GSTT1 gene is haplotype-specific and is absent from 38% of the population, so presence or absence of the gene is a recognised source of variation between individuals. NCBI Gene notes that GSTT1 and GSTT2/GSTT2B may play a role in human carcinogenesis. Alternative splicing of the gene results in multiple transcript variants.
GSTT1 conjugates reduced glutathione to many hydrophobic electrophiles, making it a key enzyme for studying how foreign and endogenous compounds are processed.
GSTT1 and GSTT2/GSTT2B share 55% sequence identity and may play a role in human carcinogenesis, a focus of cancer-related studies.
The GSTT1 gene is haplotype-specific and absent from 38% of the population, which makes it a useful subject for gene presence-or-absence analysis.
GSTT1 shows glutathione peroxidase activity with cumene hydroperoxide, relevant to work on organic hydroperoxide handling and glutathione-dependent reactions.
GSTT1 conjugates reduced glutathione to a wide variety of exogenous and endogenous hydrophobic electrophiles. It acts on substrates such as 4-nitrobenzyl chloride and 4-nitrophenethyl bromide, and it shows glutathione peroxidase activity with cumene hydroperoxide. The enzyme is classified as EC 2.5.1.18 and is found in the cytoplasm.
Both belong to the theta class of human glutathione S-transferases, which also includes GSTT2B. GSTT1 and GSTT2/GSTT2B share 55% amino acid sequence identity and may play a role in human carcinogenesis. Alternative splicing of the GSTT1 gene produces multiple transcript variants.
No. The GSTT1 gene is haplotype-specific and is absent from 38% of the population. Orthologs exist in other species, with Gstt1 named in both mouse and rat. Check the datasheet of any product for its validated reactivity.
Other theta-class glutathione S-transferases with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P30711; product specifications from Assay Genie datasheets.