SULT1C2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 316 amino acids (1-296a.a.) and having a molecular mass of 37.0kDa.
SULT1C2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Recombinant human SULT1C2, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 316 amino acids (1-296a.a.) and has a molecular mass of 37.0 kDa. A 20 amino acid His-tag is fused to the N-terminus of SULT1C2. Purification is achieved using proprietary chromatographic techniques.
The SULT1C2 solution (1 mg/ml) is formulated in 20 mM Tris-HCl buffer (pH 8.0), 20% glycerol, 0.1 M NaCl, and 1 mM DTT.
For short-term storage (2-4 weeks), keep at 4°C. For extended periods, store frozen at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
MGSSHHHHHH SSGLVPRGSH MALTSDLGKQ IKLKEVEGTL LQPATVDNWS QIQSFEAKPD DLLICTYPKA GTTWIQEIVD MIEQNGDVEK CQRAIIQHRH PFIEWARPPQ PSGVEKAKAM PSPRILKTHL STQLLPPSFW ENNCKFLYVA RNAKDCMVSY YHFQRMNHML PDPGTWEEYF ETFINGKVVW GSWFDHVKGW WEMKDRHQIL FLFYEDIKRD PKHEIRKVMQ FMGKKVDETV LDKIVQETSF EKMKENPMTN RSTVSKSILD QSISSFMRKG TVGDWKNHFT VAQNERFDEI YRRKMEGTSI NFCMEL.
Sulfotransferase Family, Cytosolic 1C, Member 2 (SULT1C2) is a member of the sulfotransferase enzyme family, which plays a crucial role in the sulfate conjugation of various hormones, neurotransmitters, drugs, and xenobiotic compounds. These enzymes are cytosolic and exhibit distinct tissue distributions and substrate specificities .
The SULT1C2 gene is located on chromosome 2q12.3 and encodes a protein that belongs to the SULT1 subfamily . The gene structure, including the number and length of exons, is similar among family members . The SULT1C2 protein consists of 296 amino acids and is responsible for transferring a sulfo moiety from 3’-phospho-5’-adenylyl sulfate (PAPS) to phenol-containing compounds .
SULT1C2 catalyzes the sulfate conjugation of phenolic compounds, which is a critical process for the metabolism and detoxification of various endogenous and exogenous substances . Unlike some other sulfotransferases, SULT1C2 does not sulfonate steroids, dopamine, acetaminophen, or alpha-naphthol . It is particularly noted for catalyzing the sulfonation of the carcinogenic N-Hydroxy-2-acetylaminofluorene, leading to highly reactive intermediates capable of forming DNA adducts, potentially resulting in mutagenesis .
Recombinant SULT1C2 is produced using recombinant DNA technology, which involves cloning the SULT1C2 gene into an expression vector and introducing it into a host cell, such as Escherichia coli (E. coli). The host cells then express the SULT1C2 protein, which can be purified and used for various research and industrial applications .