|Tested species reactivity||Human|
|Host / Isotype||Rabbit / IgG|
|Immunogen||KLH conjugated synthetic peptide between 592-624 amino acids from the C-terminal region of human PAPSS1|
|Purification||Size-exclusion - Dialysis, Ammonium sulfate precipitation|
|Contains||0.09% sodium azide|
|Storage Conditions||-20° C, Avoid Freeze/Thaw Cycles|
|Tested Applications||Dilution *|
|Western Blot (WB)||1:1000|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
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.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.