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This protein encoded by MPST catalyzes the transfer of a sulfur ion from 3-mercaptopyruvate to cyanide or other thiol compounds. Additionally we are shipping MPST Proteins (15) and MPST Kits (14) and many more products for this protein.
Showing 10 out of 43 products:
Cow (Bovine) Polyclonal MPST Primary Antibody for WB - ABIN2783349
Lo, Tsai, Tsai, Hua, Tsai, Huang, Tsai, Lai: Identification of over-expressed proteins in oral squamous cell carcinoma (OSCC) patients by clinical proteomic analysis. in Clinica chimica acta; international journal of clinical chemistry 2006
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Human Polyclonal MPST Primary Antibody for ICC, IF - ABIN4335380
Shibuya, Mikami, Kimura, Nagahara, Kimura: Vascular endothelium expresses 3-mercaptopyruvate sulfurtransferase and produces hydrogen sulfide. in Journal of biochemistry 2009
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Human Polyclonal MPST Primary Antibody for FACS, WB - ABIN392001
Akahoshi, Kamata, Kubota, Hishiki, Nagahata, Matsuura, Yamazaki, Yoshida, Yamada, Ishizaki, Suematsu, Kasahara, Ishii: Neutral aminoaciduria in cystathionine ?-synthase-deficient mice; an animal model of homocystinuria. in American journal of physiology. Renal physiology 2014
Human Polyclonal MPST Primary Antibody for WB - ABIN4890324
Panza, De Cicco, Armogida, Scognamiglio, Gigantino, Botti, Germano, Napolitano, Papapetropoulos, Bucci, Cirino, Ianaro: Role of the cystathionine γ lyase/hydrogen sulfide pathway in human melanoma progression. in Pigment cell & melanoma research 2014
3-Mercaptopyruvate sulphurtransferase and not cystathionine gamma-lyase is the primary regulator of coronary artery hydrogen sulfide production and function.
In this review, we discuss the roles of non-canonical Hippo/Mst signaling pathways in lymphocyte development and functions. [review]
distinct roles of each TUM1 isoform in the sulfur transfer processes in the cell
The crystal structure analysis allows us to propose a detailed mechanism for MST in which an Asp-His-Ser catalytic triad is positioned to activate the nucleophilic cysteine residue and participate in general acid-base chemistry
In all the investigated cell lines, the activity of MPST was higher than that of CST, which suggests that in these cells, the main pathway of sulfane sulfur formation is the MPST-catalyzed reaction.
Data suggest that impaired rhodanese expression is associated with increased whole cell reactive oxygen species as well as higher mitochondrial superoxide production and predicts mortality in hemodialysis patients.
This work is the first report of a functional genetic polymorphism affecting MPST and should help in investigation of disorders such as mercaptolactate-cysteine disulfiduria.
the findings of this study indicate that a deficiency in 3MST does not significantly affect endotoxemia, while a deficiency in CBS or CSE slightly ameliorates the outcome of LPS-induced endotoxemia in vivo.
Up-regulation of 3-MST was located in living neurons and followed neuronal autophagy after traumatic brain injury.
H2S3 and H2S are produced in the brain by 3-mercaptopyruvate sulfurtransferase.
behavioral abnormality in MST-KO mice is caused by MST function defects such as an antioxidant insufficiency or a new transducer, H2S (or HS(-)) and/or SOx deficiency.
SiRNA silencing of 3-MPST reduced basal bioenergetic parameters and prevented the stimulating effect of 3-MP on mitochondrial bioenergetics.
This protein encoded by this gene catalyzes the transfer of a sulfur ion from 3-mercaptopyruvate to cyanide or other thiol compounds. It may be involved in cysteine degradation and cyanide detoxification. There is confusion in literature between this protein (mercaptopyruvate sulfurtransferase, MPST), which appears to be cytoplasmic, and thiosulfate sulfurtransferase (rhodanese, TST, GeneID:7263), which is a mitochondrial protein. Deficiency in MPST activity has been implicated in a rare inheritable disorder known as mercaptolactate-cysteine disulfiduria (MCDU). Alternatively spliced transcript variants encoding same or different isoforms have been identified for this gene.
, human liver rhodanese
, thiosulfate sulfurtransferase (rhodanese)
, mercaptopyruvate sulfurtransferase
, thiosulfate sulfurtransferase
, mercaptopyruvate sulfurtransferase S homeolog