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SULT1A1 Protein, Human, Recombinant (His Tag)

Product Specifications

Background

Sulfate conjugation catalyzed by cytosolic sulfotransferase (SULT) enzymes. The SULTs are Phase II drug-metabolizing enzymes that catalyze the addition of a sulfuryl moiety to both endogenous compounds, including steroids and neurotransmitters, and certain xenobiotics, including N-hydroxy-2-acetylaminoflourine and phenolic compounds, like alpha-naphthol. SULTs may be involved in the individual genetic disposition, species differences, and organotropisms for toxicological effects of chemicals. Particularly SULT1A1 (Sulfotransferase family, cytosolic, 1A, phenol-preferring, member 1), a member of the sulfotransferase 1 subfamily, which is a major pathway for drug metabolism in humans. Humans have at least 10 functional SULT genes. There has been an explosion in information on sulfotransferase polymorphisms and their functional consequences. An Arg213His polymorphism in SULT1A1 has a strong influence on the level of enzyme protein and activity in platelets, which have been widely used for phenotyping. Statistically significant associations were observed between the SULT1A1 genotype (Arg213His) and age, obesity and certain neoplasias (mammary, pulmonary, esophageal and urothelial cancer) . Furthermore, the polymorphism of the SULT1A1 may be closely associated with breast cancer.

Synonyms

HAST1/HAST2 Protein, Human; P-PST Protein, Human; PST Protein, Human; ST1A1 Protein, Human; ST1A3 Protein, Human; STP Protein, Human; STP1 Protein, Human; TSPST1 Protein, Human

Gene Name

Sulfotransferase family, cytosolic, 1A, phenol-preferring, member 1

UniProt

P50225-1

Expression System

E. coli

Tag

N-His

Endotoxin

Please contact us for more information.

Purity

> 95 % as determined by SDS-PAGE.

Activity

At Leading Biology, the biological activity of a recombinant protein is routinely measured using a bioassay, e.g. chemotaxis or cell proliferation assay, enzyme assay, or a functional ELISA. When a recombinant protein is an enzyme, specific activity is derived from an enzymatic assay. Each enzyme is tested for potency by cleavage of a substrate. We are in the process of updating the biological activity data. If you have any questions regarding this update, please feel free to contact our technical support team.

Form

Lyophilized

Buffer

Lyophilized from sterile 50mM Tris, 150mM NaCl, 10% glycerol, pH 8.0 Please contact us for any concerns or special requirements. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hard copy of CoA.

Function

Enzyme Proteins

Molecular Weight

The recombinant human SULT1A1 consisting of 301 amino acids and has a calculated molecular mass of 35 kDa. It migrates as an approximately 32 kDa band in SDS-PAGE under reducing conditions.

Storage Conditions

In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature. Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise. Stable for 1 year at -20°C or below from date of shipment. For maximum recovery of product, centrifuge the original vial after thawing and opening the cap. For long-term storage, aliquot and store at -20°C or below. Avoid repeated freeze-thaw cycles.

Product Datasheet

http://www.leading-biology.com/en/fastadmin/public/data/datasheet/S_Protein_datasheet/PH52366E1.pdf

Symbol

SULT1A1

Species

Human

Overview

A DNA sequence encoding the human SULT1A1 (P50225-1) (Glu 2-Leu 295) was fused with a polyhistidine tag at the N-terminus.

Uniprot URL

https://www.uniprot.org/uniprot/P50225-1

AA Sequence

Glu2-Leu295

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