Recombinant Human Sulfotransferase/SULT1C4 Protein (His Tag) | PKSH033088

Recombinant Human Sulfotransferase/SULT1C4 Protein (His Tag) | PKSH033088 | Gentaur US, UK & Europe Disrtribition

Synonyms: SULT1C4;Sulfotransferase;SULT1C2;hCG_27301;;

Active Protein: N/A

Activity: Recombinant Human Cytosolic Sulfotransferase Family 1C Member 4 is produced by our E.coli expression system and the target gene encoding Met1-Lys102 is expressed with a 6His tag at the N-terminus.

Protein Construction: Recombinant Human Cytosolic Sulfotransferase Family 1C Member 4 is produced by our E.coli expression system and the target gene encoding Met1-Lys102 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 lyophilized powder which is shipped with ice packs.

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

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

Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

Molecular Mass: 14.1 kDa

Formulation: Lyophilized from a 0.2 μm filtered solution of 4mM HCl.

Reconstitution: Please refer to the printed manual for detailed information.

Background: Human Sulfotransferase (SULT1C4) is an enzyme that in humans is encoded by the SULT1C4 gene, belongs to the sulfotransferase 1 family. SULT1C4 is expressed at high levels in fetal lung and kidney and at low levels in fetal heart, adult kidney, ovary and spinal chord. Sulfotransferase utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of drugs, xenobiotic compounds, hormones, and neurotransmitters. It shows activity towards p-nitrophenol and N-hydroxy-2-acetylamino-fluorene (N-OH-2AAF). SULT1C4 plays an important role incatalyzing the sulfate conjugation of many hormones, neurotransmitters, drugs, and xenobiotic compounds.

Research Area: N/A