SULT2B1 (Sulfotransferase 2B1; also ST2B1b and alcohol sulfotransferase) is a 45-48kD member of the sulfotransferase 1 family of enzymes.
SULT2B1 is widely expressed, being found in platelets, stratum granulosum keratinocytes, breast and prostatic epithelium, and syncytiotrophoblast cells.
SULT2B1 catalyzes the sulfonation of DHEA, a precursor for sex steroids, and cholesterol, which supports stratification of the epidermis.
Human SULT2B1 is 365aa in length.
There are PAPS binding sites between aa70-75 and 147-155, a myristoylation motif between aa255-259, and a Pro-rich region between aa305-364 that may extend enzyme half-life.
There is one 43kD splice form (ST2B1a) that shows an eight aa substitution for aa1-23.
It is expressed in fetal brain and generates pregnenolone sulfate, a steroid that modulates neurotransmitters.
Full-length human SULT2B1b shares only 71% aa identity with mouse SULT2B1.
Applications:Suitable for use in Western Blot.
Other applications not tested.
Recommended Dilution:Optimal dilutions to be determined by the researcher.
AA Sequence:MDGPAEPQIPGLWDTYEDDISEISQKLPGEYFRYKGVPFPVGLYSLESISLAENTQDVRDDDIFIITYPKSGTTWMIEIICLILKEGDPSWIRSVPIWERAPWCETIVGAFSLPDQYSPRLMSSHLPIQIFTKAFFSSKAKVIYMGRNPRDVVVSLYHYSKIAGQLKDPGTPDQFLRDFLKGEVQFGSWFDHIKGWLRMKGKDNFLFITYEELQQDLQGSVERICGFLGRPLGKEALGSVVAHSTFSAMKANTMSNYTLLPPSLLDHRRGAFLRKGVCGDWKNHFTVAQSEAFDRAYRKQMRGMPTFPWDEDPEEDGSPDPEPSPEPEPKPSLEPNTSLEREPRPNSSPSPSPGQASETPHPRPS
Storage and Stability:May be stored at 4°C for short-term only.
Aliquot to avoid repeated freezing and thawing.
Store at -20°C.
Aliquots are stable for at least 12 months.
For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
仕様
Size：100ug
Host：rabbit
Source Antibody：human
Grade：Affinity Purified
Purity：Purified by Protein A affinity chromatography.
Form：Supplied as a liquid in PBS, pH 7.2.
Specificity：Recognizes human SULT2B1.
Isotype：IgG
Calc Applications Abbrev：WB
Calc Crossreactivity：Hu
Immunogen：Full length human SULT2B1, aa1-365 (NP_814444.1).
