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This is one of two neighboring genes encoding similar proteins that each contain two rhodanese domains. Additionally we are shipping Thiosulfate Sulfurtransferase (Rhodanese) Antibodies (27) and Thiosulfate Sulfurtransferase (Rhodanese) Proteins (13) and many more products for this protein.
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TST mRNA expression in adipose tissue correlated positively with insulin sensitivity in adipose tissue and negatively with fat mass.
show that polymorphic variations that are distant from the active site differentially modulate the sulfurtransferase activity of human rhodanese to cyanide versus sulfite
Loss of Thiosulfate Sulfurtransferase is associated with decreased mucosal sulfide detoxification capacity in patients with Crohn's disease
silencing of the rhodanese gene caused not only a proportional decrease of 5 S rRNA import but also a general inhibition of mitochondrial translation, indicating the functional importance of the imported 5 S rRNA inside the organelle.
Proteomics was used to study colonic epithelial aging, for differential proteins in the human normal colonic epithelial tissues from young and old people. Rack1, EF-Tu and Rhodanese, three validated differential proteins, were further investigated.
A partially gluconoylated N-terminus of the His6-tagged molybdenum cofactor synthesis 3 (MOCS3)-rhodanese-like domain is identified which results in a heterogeneity of the protein but does not influence sulfurtransferase activity.
The USP8 recognition domain of NRDP1 has a novel protein fold that interacts with a conserved peptide loop of the rhodanese domain.
Results identified two regulatory variants between fat and lean mice: one overlaps an evolutionary constrained Tst intronic element and the other resides in the seed region of a predicted 3'UTR (show UTS2R ELISA Kits) miRNA binding site.
Elevated adipose Tst expression correlated with indices of metabolic health across diverse mouse strains. Transgenic overexpression of Tst in adipocytes protected mice from diet-induced obesity and insulin (show INS ELISA Kits)-resistant diabetes. Tst-deficient mice showed markedly exacerbated diabetes.
increased sensitivity to cyanide, generally reported in old mice, may be due in part to a decrease in the activity of brain rhodanese
active rhodanese lacking nonessential sulfhydryl groups contains an unstable C-terminal domain and can be bound, inactivated, and reactivated by GroEL
Data suggest that inhibition of rhodanese activity is a result of the formation of stable S-nitrosorhodanese, and that low molecular weight nitric oxide donors are much more effective than such known inhibitors of this enzyme.
This is one of two neighboring genes encoding similar proteins that each contain two rhodanese domains. The encoded protein is localized to the mitochondria and catalyzes the conversion of thiosulfate and cyanide to thiocyanate and sulfite. In addition, the protein interacts with 5S ribosomal RNA and facilitates its import into the mitochondria. Alternative splicing results in multiple transcript variants.
, Thiosulfate sulfurtransferase
, Thiosulfate sulphurtransferase (rhodanese)
, thiosulfate sulfurtransferase, mitochondrial
, thiosulfate sulfurtransferase (rhodanese)