Recombinant Human SULT1A1 Protein (His Tag) | PKSH033358

Recombinant Human SULT1A1 Protein (His Tag) | PKSH033358 | Gentaur US, UK & Europe Disrtribition

Synonyms: Sulfotransferase 1A1; ST1A1; Aryl sulfotransferase 1; HAST1/HAST2; Phenol Sulfotransferase 1; Phenol-Sulfating Phenol Sulfotransferase 1; P-PST 1; ST1A3; Thermostable Phenol Sulfotransferase; Ts-PST; SULT1A1; STP; STP1; OK/SW-cl.88

Active Protein: N/A

Activity: Recombinant Human Cytosolic Sulfotransferase Family 1A Member 1 is produced by our E.coli expression system and the target gene encoding Met1-Leu295 is expressed with a 6His tag at the N-terminus.

Protein Construction: Recombinant Human Cytosolic Sulfotransferase Family 1A Member 1 is produced by our E.coli expression system and the target gene encoding Met1-Leu295 is expressed with a 6His tag at the N-terminus.

Fusion Tag: N-6His

Species: Human

Expressed Host: E.coli

Shipping: This product is provided as liquid. It is shipped at frozen temperature with blue ice/gel packs. Upon receipt, store it immediately at<-20°C.

Purity: > 95 % as determined by reducing SDS-PAGE.

Endotoxin: < 1.0 EU per µg as determined by the LAL method.

Stability and Storage: Store at < -20°C, stable for 6 months. Please minimize freeze-thaw cycles.

Molecular Mass: 35.5 kDa

Formulation: Supplied as a 0.2 μm filtered solution of 20mM Tris-HCl, 150mM NaCl, 2mM DTT, pH 8.0.

Reconstitution: Not Applicable

Background: Sulfotransferase 1A1 (SULT1A1) is a cytosolic sulfotransferases that is expressed in the liver; lung; adrenal; brain; platelets; and skin. SULT1A1 is a phenol sulfotransferases with thermostable enzyme activity. SULT1A1 utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of catecholamines; phenolic drugs and neurotransmitters. It is responsible for the sulfonation and activation of minoxidil. SULT1A1 mediates the metabolic activation of carcinogenic N-hydroxyarylamines to DNA binding products and could so participate as modulating factor of cancer risk.

Research Area: N/A