SULT1C2 Protein, Human (His)

The SULT1C2 protein utilizes PAPS to catalyze sulfate conjugation and has specific affinity for sulfonated p-nitrophenol. It selectively avoids sulfonated steroids, dopamine, acetaminophen or alpha-naphthol. SULT1C2 Protein, Human (His) is the recombinant human-derived SULT1C2 protein, expressed by E. coli , with N-6*His labeled tag.

SULT1C2 protein, a sulfotransferase utilizing 3'-phospho-5'-adenylyl sulfate (PAPS) as its sulfonate donor, plays a pivotal role in catalyzing sulfate conjugation, with a specific affinity for sulfonating p-nitrophenol, a small phenolic compound. Notably, SULT1C2 exhibits selectivity in its substrate preferences, as it does not sulfonate steroids, dopamine, acetaminophen, or alpha-naphthol. Additionally, this sulfotransferase catalyzes the sulfonation of N-Hydroxy-2-acetylaminofluorene, a carcinogenic compound, leading to the formation of highly reactive intermediates capable of generating DNA adducts. This enzymatic activity raises concerns about potential mutagenesis, emphasizing the intricate role of SULT1C2 in the metabolism of xenobiotic compounds and its implications for cellular processes associated with mutagenic risk.

Human

E. coli

N-6*His

O00338 (M1-L296)

6819  [NCBI]

Full Length

MALTSDLGKQIKLKEVEGTLLQPATVDNWSQIQSFEAKPDDLLICTYPKAGTTWIQEIVDMIEQNGDVEKCQRAIIQHRHPFIEWARPPQPSGVEKAKAMPSPRILKTHLSTQLLPPSFWENNCKFLYVARNAKDCMVSYYHFQRMNHMLPDPGTWEEYFETFINGKVVWGSWFDHVKGWWEMKDRHQILFLFYEDIKRDPKHEIRKVMQFMGKKVDETVLDKIVQETSFEKMKENPMTNRSTVSKSILDQSISSFMRKGTVGDWKNHFTVAQNERFDEIYRRKMEGTSINFCMEL

Approximately 30-37 kDa, based on SDS-PAGE under reducing conditions.

• 
  ≥ 90%, as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.