Human Sulfotransferase Family 1A Member 1 (SULT1A1) Protein
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Description
Human Cytosolic Sulfotransferase Family 1A Member 1 Protein is a recombinant protein from Human produced in E. coli. 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.
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Product specifications
| Category | Proteins and Peptides |
| Immunogen Target | Cytosolic Sulfotransferase Family 1A Member 1 |
| Host | E. coli |
| Origin | Human |
| Observed MW | Molecular Weight: 35.5 kDa Sequence Fragment: Met1-Leu295 Tag: N-terminal 6 His tag Validity: The validity for this protein is 6 months. |
| Expression | Recombinant |
| Purity | > 95% (SDS-PAGE) |
| Size 1 | 10 µg |
| Size 2 | 50 µg |
| Tested Applications | SDS-PAGE |
| Buffer | 20mM Tris, 150mM NaCl, 1mM EDTA, pH 8.0. |
| Availability | Shipped within 5-15 working days. |
| Storage | Aliquot and store at < -20 °C. Avoid repeated freeze/thaw cycles. |
| Dry Ice | No |
| UniProt ID | P50225-1 |
| Background | Protein SULT1A1 |
| Status | RUO |
| Note | This product is for research use only. Not for human consumption, cosmetic, therapeutic or diagnostic use. |
Descripción
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Sulfotransferase enzymes catalyze the sulfate conjugation of many hormones, neurotransmitters, drugs, and xenobiotic compounds. These cytosolic enzymes are different in their tissue distributions and substrate specificities. The gene structure (number and length of exons) is similar among family members. This gene encodes one of two phenol sulfotransferases with thermostable enzyme activity. Multiple alternatively spliced variants that encode two isoforms have been identified for this gene.
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Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate(PAPS) as sulfonate donor to catalyze the sulfate conjugation of catecholamines, phenolic drugs and neurotransmitters. Has also estrogen sulfotransferase activity. responsible for the sulfonation and activation of minoxidil. Is Mediates the metabolic activation of carcinogenic N-hydroxyarylamines to DNA binding products and could so participate as modulating factor of cancer risk.
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