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SULT1A3 active protein

SULT1A3 Protein, Human, Recombinant (His Tag)

Gene Names
SULT1A3; STM; HAST; HAST3; M-PST; ST1A5; TL-PST; MGC117469; ST1A3/ST1A4
Purity
>94% as determined by SDS-PAGE
Synonyms
SULT1A3; SULT1A3 Protein; Human; Recombinant (His Tag); Human SULT1A3 Protein (His Tag); HAST Protein; HAST3 Protein; M-PST Protein; ST1A3 Protein; ST1A3/ST1A4 Protein; ST1A5 Protein; STM Protein; SULT1A4 Protein; TL-PST Protein; sulfotransferase family 1A member 3; SULT1A3 active protein
Ordering
For Research Use Only!
Host
E Coli
Purity/Purification
>94% as determined by SDS-PAGE
Form/Format
Lyophilized from sterile 20mM Tris, 500mM NaCl, pH7.4. Normally 5%-8% trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hard copy of CoA.
Sequence
Glu2-Leu295
Species
Human
Activity
Measured by its ability to transfer sulfate from PAPS to 1-Napthol. The specific activity is >150pmoles/min/ug.
Predicted N Terminal
Met
Tag
N-His
Protein Construction
A DNA sequence encoding the mature form of human SULT1A3 (NP_808220.1)(Glu2-Leu295) was expressed with a polyhistide tag at the N-terminus.
Reconstitution
A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
Preparation and Storage
Samples are stable for up to twelve months from date of receipt at -20 degree C to -80 degree C. Store it under sterile conditions at -20 degree C to -80 degree C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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.

SDS-Page

SDS-Page
Related Product Information for SULT1A3 active protein
Background: SULT1A3 belongs to the sulfotransferase 1 family. Sulfotransferase enzymes catalyze the sulfate conjugation of many hormones, neurotransmitters, drugs, and xenobiotic compounds. They are different in their tissue distributions and substrate specificities while their gene structure (number and length of exons) is similar. SULT1A3 gene encodes a phenol sulfotransferase with thermolabile enzyme activity. Four sulfotransferase genes are located on the p arm of chromosome 16; this gene and SULT1A4 arose from a segmental duplication. It is the most centromeric of the four sulfotransferase genes. Exons of this gene overlap with exons of a gene that encodes a protein containing GIY-YIG domains (GIYD1). SULT1A3 is expressed in liver, colon, kidney, lung, brain, spleen, small intestine, placenta and leukocyte. SULT1A3 is a sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of phenolic monoamines (neurotransmitters such as dopamine, norepinephrine and serotonin) and phenolic and catechol drugs.
References
Dajani R, et al. (1999) Kinetic properties of human dopamine sulfotransferase (SULT1A3) expressed in prokaryotic and eukaryotic systems: comparison with the recombinant enzyme purified from Escherichia coli. Protein Expr. Purif. 16 (1): 11-8.Dajani R, et al. (2000) X-ray crystal structure of human dopamine sulfotransferase, SULT1A3. J. Biol. Chem. 274 (53): 37862-8.Yasuda S, et al. (2011) Sulfation of chlorotyrosine and nitrotyrosine by human lung endothelial and epithelial cells: role of the human SULT1A3. Toxicol Appl Pharmacol. 251 (2): 104-9.Hildebrandt MA, et al. (2004) Human SULT1A3 pharmacogenetics: gene duplication and functional genomic studies. Biochem Biophys Res Commun. 321 (4): 870-8.Lu JH, et al. (2005) Crystal structure of human sulfotransferase SULT1A3 in complex with dopamine and 3'-phosphoadenosine 5'-phosphate. Biochem Biophys Res Commun. 335 (2): 417-23.

NCBI and Uniprot Product Information

NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Accession #
Molecular Weight
34,196 Da
NCBI Official Full Name
sulfotransferase 1A3/1A4
NCBI Official Synonym Full Names
sulfotransferase family, cytosolic, 1A, phenol-preferring, member 3
NCBI Official Symbol
SULT1A3
NCBI Official Synonym Symbols
STM; HAST; HAST3; M-PST; ST1A5; TL-PST; MGC117469; ST1A3/ST1A4
NCBI Protein Information
sulfotransferase 1A3/1A4; sulfokinase; OTTHUMP00000045746; OTTHUMP00000045747; phenol sulfotransferase 1A5; aryl sulfotransferase 1A3/1A4; dopamine-specific sulfotransferase; placental estrogen sulfotransferase; monoamine-sulfating phenosulfotransferase;
Protein Family

NCBI Description

Sulfotransferase enzymes catalyze the sulfate conjugation of many hormones, neurotransmitters, drugs, and xenobiotic compounds. These cytosolic enzymes are different in their tissue distributions and substrate specificities. The gene structure (number and length of exons) is similar among family members. This gene encodes a phenol sulfotransferase with thermolabile enzyme activity. Four sulfotransferase genes are located on the p arm of chromosome 16; this gene and SULT1A4 arose from a segmental duplication. This gene is the most centromeric of the four sulfotransferase genes. Read-through transcription exists between this gene and the upstream SLX1A (SLX1 structure-specific endonuclease subunit homolog A) gene that encodes a protein containing GIY-YIG domains. [provided by RefSeq]

Uniprot Description

SULT1A3: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of phenolic monoamines (neurotransmitters such as dopamine, norepinephrine and serotonin) and phenolic and catechol drugs. Belongs to the sulfotransferase 1 family. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: EC 2.8.2.1; Energy Metabolism - sulfur; Transferase

Chromosomal Location of Human Ortholog: 16p11.2

Cellular Component: cytosol

Molecular Function: sulfotransferase activity; aryl sulfotransferase activity

Biological Process: steroid metabolic process; cellular protein metabolic process; unfolded protein response, activation of signaling protein activity; flavonoid metabolic process; unfolded protein response; xenobiotic metabolic process; sulfation; catecholamine metabolic process; 3'-phosphoadenosine 5'-phosphosulfate metabolic process

Research Articles on SULT1A3

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Product Notes

The SULT1A3 (Catalog #AAA8120812) is an Active Protein produced from E Coli and is intended for research purposes only. The product is available for immediate purchase. The amino acid sequence is listed below: Glu2-Leu29 5. It is sometimes possible for the material contained within the vial of "SULT1A3, Active Protein" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.

Precautions

All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.

Disclaimer

Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.

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