SULT1C4 Human

Sulfotransferase Family, Cytosolic 1C, Member 4 Human Recombinant
Cat. No.
BT14306
Source
Escherichia Coli.
Synonyms
Sulfotransferase 1C4, SULT1C, SULT1C2, Sulfotransferase Family, Cytosolic 1C, Member 4, SULT1C4, ST1C4, Sulfotransferase 1C2, SULT1C#2.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 95.0% 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

SULT1C4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 322 amino acids (1-302 a.a) and having a molecular mass of 37.6kDa. SULT1C4 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Sulfotransferase 1C4 (SULT1C4) is a member of the SULT subfamily responsible for transferring a sulfo moiety from PAPS to phenol-containing compounds. Sulfotransferase enzymes catalyze the sulfate conjugation of various compounds, including hormones, neurotransmitters, drugs, and xenobiotics. These enzymes differ in their tissue distributions and substrate specificities. SULT1C4 specifically catalyzes the sulfonation of p-nitrophenol and N-hydroxy-2-acetylaminofluorene.
Description
Recombinant human SULT1C4, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 322 amino acids (with amino acids 1-302 being part of the SULT1C4 sequence) and has a molecular weight of 37.6 kDa. The protein is fused to a 20 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Physical Appearance
A colorless, sterile-filtered solution.
Formulation
The SULT1C4 protein solution is provided at a concentration of 1 mg/ml and contains 0.1M NaCl, 20% glycerol, and 1mM DTT.
Stability
For short-term storage (2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to freeze the product at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
The purity is determined to be greater than 95.0% using SDS-PAGE analysis.
Synonyms
Sulfotransferase 1C4, SULT1C, SULT1C2, Sulfotransferase Family, Cytosolic 1C, Member 4, SULT1C4, ST1C4, Sulfotransferase 1C2, SULT1C#2.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MALHDMEDFT FDGTKRLSVN YVKGILQPTD TCDIWDKIWN FQAKPDDLLI STYPKAGTTW TQEIVELIQN EGDVEKSKRA PTHQRFPFLE MKIPSLGSGL EQAHAMPSPR ILKTHLPFHL LPPSLLEKNC KIIYVARNPK DNMVSYYHFQ RMNKALPAPG TWEEYFETFL AGKVCWGSWH EHVKGWWEAK DKHRILYLFY EDMKKNPKHE IQKLAEFIGK KLDDKVLDKI VHYTSFDVMK QNPMANYSSI PAEIMDHSIS PFMRKGAVGD WKKHFTVAQN ERFDEDYKKK MTDTRLTFHF QF.

Product Science Overview

Introduction

Sulfotransferase Family, Cytosolic 1C, Member 4 (SULT1C4) is a member of the sulfotransferase (SULT) enzyme family. These enzymes play a crucial role in the metabolism of various endogenous and exogenous compounds by catalyzing the sulfate conjugation of hormones, neurotransmitters, drugs, and xenobiotic compounds . SULT1C4 is a protein-coding gene that belongs to the SULT1 subfamily, which is responsible for transferring a sulfo moiety from 3’-phospho-5’-adenylyl sulfate (PAPS) to phenol-containing compounds .

Gene Structure and Expression

The gene structure of SULT1C4, including the number and length of exons, is similar among family members . SULT1C4 is expressed in various tissues, and its expression pattern is distinct from other members of the SULT family. The gene is located on chromosome 2 and has several aliases, including SULT1C2 and ST1C4 .

Function and Substrate Specificity

SULT1C4 utilizes PAPS as a sulfonate donor to catalyze the sulfate conjugation of phenolic compounds . It can also sulfonate estrogenic compounds, although dietary flavonoids (phytoestrogens) and environmental estrogens, such as bisphenol A, are better substrates than 17beta-estradiol (E2) . Additionally, SULT1C4 mediates the sulfation of doxorubicin and its analog epirubicin, two antitumor anthracyclines .

Clinical Significance

Diseases associated with SULT1C4 include spondyloepiphyseal dysplasia with congenital joint dislocations and ovary sarcoma . The enzyme’s role in the metabolism of various compounds makes it a potential target for drug development and therapeutic interventions.

Research and Applications

Recombinant human SULT1C4 is used in research to study its enzymatic activity, substrate specificity, and potential therapeutic applications. Understanding the function and regulation of SULT1C4 can provide insights into its role in drug metabolism and the development of novel treatments for diseases associated with its dysfunction.

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