|Other Names||Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1, PAPS synthase 1, PAPSS 1, Sulfurylase kinase 1, SK 1, SK1, Sulfate adenylyltransferase, ATP-sulfurylase, Sulfate adenylate transferase, SAT, Adenylyl-sulfate kinase, 3'-phosphoadenosine-5'-phosphosulfate synthase, APS kinase, Adenosine-5'-phosphosulfate 3'-phosphotransferase, Adenylylsulfate 3'-phosphotransferase, PAPSS1, ATPSK1, PAPSS|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP2607b was selected from the C-term region of human PAPSS1. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Bifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway. The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yielding 3'-phosphoadenylylsulfate (PAPS: activated sulfate donor used by sulfotransferase). In mammals, PAPS is the sole source of sulfate; APS appears to be only an intermediate in the sulfate- activation pathway (PubMed:9576487, PubMed:9668121, PubMed:9648242, PubMed:14747722). Required for normal biosynthesis of sulfated L-selectin ligands in endothelial cells (PubMed:9576487).|
|Tissue Location||Expressed in testis, pancreas, kidney, thymus, prostate, ovary, small intestine, colon, leukocytes and liver Also expressed in high endothelial venules (HEV) cells and in cartilage.|
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Provided below are standard protocols that you may find useful for product applications.
Sulfotransferase (SULT) enzymes catalyze the sulfate conjugation of many drugs, xenobiotic compounds, hormones, and neurotransmitters. 3'-phosphoadenosine 5'-phosphosulfate (PAPS) synthase (PAPSS) catalyzes the biosynthesis of PAPS which serves as the universal sulfonate donor compound for all sulfotransferase reactions. In humans, PAPS is synthesized from adenosine 5-prime triphosphate (ATP) and inorganic sulfate by 2 isoforms, PAPSS1 and PAPSS2 (603005). Bifunctional PAPSS1 is comprised of an N-terminal APS kinase domain, and a C-terminal ATP sulfurylase domain. Full-length protein has significantly less APS kinase activity than the N-terminal fragment, suggesting that the C-terminal domain exerts a regulatory role on the N-terminal APS kinase activity. In humans there are two major isoforms: PAPSS1 and PAPSS2. In brain and skin PAPSS1 is the major isoform, whereas in liver, cartilage and adrenal glands PAPSS2 isoform expression dominates. The predicted 623-amino acid protein is 98% identical to mouse PAPS synthase. The N-terminal 268-amino acid region of human PAPS synthase resembles APS kinases from other organisms and contains 3 conserved nucleotide-binding motifs.
Biochemistry 43 (14), 4356-4365 (2004)IUBMB Life 55 (1), 1-11 (2003)Biochem. J. 365 (PT 2), 497-504 (2002)Biochem. Biophys. Res. Commun. 268 (2), 437-444 (2000)FASEB J. 14 (2), 345-354 (2000)
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