SULT1C2 Human

Sulfotransferase Family, Cytosolic 1C, Member 2 Human Recombinant
Cat. No.
BT14243
Source
Escherichia Coli.
Synonyms
Sulfotransferase 1C2, ST1C2, Sulfotransferase 1C1, SULT1C#1, humSULTC2, SULT1C2, SULT1C1, ST1C1.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

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.

Product Specs

Introduction
Sulfotransferase 1C2 (SULT1C2), a member of the sulfotransferase 1 superfamily, catalyzes the sulfation of phenolic compounds. These compounds include hormones and neurotransmitters. SULT1C2 utilizes PAPS (3'-phosphoadenosine-5'-phosphosulfate) as the sulfate donor. Alternative splicing results in two isoforms: a short and a long form. The sulfotransferase enzyme family is responsible for the sulfate conjugation of various substances, including hormones, neurotransmitters, drugs, and xenobiotic compounds.
Description

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.

Physical Appearance
A sterile, colorless solution.
Formulation

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.

Stability

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.

Purity
Purity is determined by SDS-PAGE analysis to be greater than 90.0%.
Synonyms
Sulfotransferase 1C2, ST1C2, Sulfotransferase 1C1, SULT1C#1, humSULTC2, SULT1C2, SULT1C1, ST1C1.
Source
Escherichia Coli.
Amino Acid Sequence

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.

Product Science Overview

Introduction

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 .

Gene and Protein Structure

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 .

Function and Mechanism

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

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 .

Applications and Importance

The study of recombinant SULT1C2 is essential for understanding the enzyme’s role in drug metabolism and the detoxification of harmful compounds. It also provides insights into the mechanisms underlying certain diseases and the development of potential therapeutic interventions .

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