CSPS (SULT1A3) (NM_177552) Human Recombinant Protein

SKU
TP760848
Purified recombinant protein of Human sulfotransferase family, cytosolic, 1A, phenol-preferring, member 3 (SULT1A3), full length, with N-terminal HIS tag, expressed in E. coli, 50ug
$261.00
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Specifications
Product Data
Species Human
Expression Host E. coli
Expression cDNA Clone or AA Sequence
Protein Sequence
A DNA sequence encoding human full-length SULT1A3
Tag N-His
Predicted MW 34 kDa
Concentration >0.05 µg/µL as determined by microplate BCA method
Purity > 80% as determined by SDS-PAGE and Coomassie blue staining
Buffer 25 mM Tris-HCl, pH 8.0, 150 mM NaCl, 1% sarkosyl, 10% glycerol
Note For testing in cell culture applications, please filter before use. Note that you may experience some loss of protein during the filtration process.
Storage Store at -80°C.
Stability Stable for 12 months from the date of receipt of the product under proper storage and handling conditions. Avoid repeated freeze-thaw cycles.
Shipping Dry Ice
Reference Data
RefSeq NP_808220
Locus ID 6818
UniProt ID P0DMM9
Cytogenetics 16p11.2
RefSeq Size 1408
RefSeq ORF 885
Synonyms HAST; HAST3; M-PST; ST1A3; ST1A3/ST1A4; ST1A4; ST1A5; STM; TL-PST
Summary 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, Nov 2010]
Protein Pathways Sulfur metabolism
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Citations

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