SULT2B1 Protein, Human (311a.a, His)

The SULT2B1 protein uses PAPS to catalyze sulfate conjugation, mainly sulfating cholesterol, and shows significant activity on steroids such as pregnenolone and DHEA. It plays a crucial role in epidermal cholesterol metabolism, regulating epidermal proliferation and differentiation. SULT2B1 Protein, Human (311a.a, His) is the recombinant human-derived SULT2B1 protein, expressed by E. coli , with C-6*His labeled tag. The total length of SULT2B1 Protein, Human (311a.a, His) is 311 a.a., with molecular weight of ~35.0 kDa.

SULT2B1 protein, a sulfotransferase utilizing 3'-phospho-5'-adenylyl sulfate (PAPS) as its sulfonate donor, holds a pivotal role in catalyzing sulfate conjugation, with a primary responsibility for sulfating cholesterol. Additionally, SULT2B1 demonstrates significant activity in sulfating steroids, particularly the 3beta-hydroxyl groups of molecules such as pregnenolone and dehydroepiandrosterone (DHEA). While it exhibits a preferential sulfonation of cholesterol, it also displays substantial activity with pregnenolone and DHEA. Beyond its enzymatic functions, SULT2B1 plays a crucial role in epidermal cholesterol metabolism, contributing to the regulation of epidermal proliferation and differentiation. Notably, it sulfonates pregnenolone but not cholesterol, underscoring its substrate selectivity and emphasizing its multifaceted involvement in the intricate processes governing cholesterol homeostasis and steroid metabolism.

Human

E. coli

C-6*His

O00204 (M1-E311)

6820  [NCBI]

MDGPAEPQIPGLWDTYEDDISEISQKLPGEYFRYKGVPFPVGLYSLESISLAENTQDVRDDDIFIITYPKSGTTWMIEIICLILKEGDPSWIRSVPIWERAPWCETIVGAFSLPDQYSPRLMSSHLPIQIFTKAFFSSKAKVIYMGRNPRDVVVSLYHYSKIAGQLKDPGTPDQFLRDFLKGEVQFGSWFDHIKGWLRMKGKDNFLFITYEELQQDLQGSVERICGFLGRPLGKEALGSVVAHSTFSAMKANTMSNYTLLPPSLLDHRRGAFLRKGVCGDWKNHFTVAQSEAFDRAYRKQMRGMPTFPWDE

Approximately 35.0 kDa

Greater than 85% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.