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TST (thiosulfate sulfurtransferase (rhodanese))

TST (thiosulfate sulfurtransferase (rhodanese))

ArtNr	18-003-44757
Hersteller	GENWAY
Menge	0.05 mg
Kategorie	Neuroscience Targets for Rodent Neurosciences Antibodies Immunohistochemistry Western Blot Primary Antibodies
Typ	Antibody
Applikationen	WB, IHC
Specific against	other
ECLASS 10.1	32160702
ECLASS 11.0	32160702
UNSPSC	12352203
Alias	GWB-CA7C04
Similar products	18-003-44757
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Genway ID:	GWB-CA7C04
Antigen Specificity:	Polyclonal antibody produced in rabbits immunized with a synthetic peptide corresponding to a region of Human TST.
ELISA Titre:	1:312500
Note:	Suggested starting concentrations are provided. Optimal dilutions should be determined by end-user. Differences in calculated versus apparent molecular weight may be due to post-translational modifications or protein hydrophobicity. TST is a mitochondrial matrix enzyme that is encoded by the nucleus. It may play roles in cyanide detoxification. the formation of iron-sulfur proteins. and the modification of sulfur-containing enzymes. The product contains two highly conservative domain
Function:	Formation of iron-sulfur complexes cyanide detoxification or modification of sulfur-containing enzymes. Other thiol compounds besides cyanide can act as sulfur ion acceptors. Also has weak mercaptopyruvate sulfurtransferase (MST) activity (By similarity).
Catalytic Activity:	Thiosulfate + cyanide = sulfite + thiocyanate.
Subunit:	Monomer.
Subcellular Location:	Mitochondrion matrix.
Domain:	The structure consists of 2 domains of very similar conformation suggesting a common evolutionary origin. However the sequences of the 2 domains are very different.
Similarity:	Contains 2 rhodanese domains. Summary: The product of this gene is a mitochondrial matrix enzyme that is encoded by the nucleus. It may play roles in cyanide detoxification the formation of iron-sulfur proteins and the modification of sulfur-containing enzymes. The gene product contains two highly conservative domains (rhodanese homology domains) suggesting these domains have a common evolutionary origin. Matthies. A. . (2005) Biochemistry 44 (21). 7912-7920.

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