Anti-SULT1B1 (C-term) antibody produced in rabbit

Sulfotransferases such as SULT1B1 catalyze the biotransformation of a large number of endogenous compounds such as neurotransmitters, steroids, bile acids, and thyroid hormones, as well as drugs and xenobiotics. Fujita et al. (1997) demonstrated that recombinant rat and human SULT1B1, expressed in E. coli, catalyzed sulfation of p-nitrophenol, 3,3-prime,5-triiodothyronine (T3), and dopamine, but not of beta-estradiol and dehydroepiandrosterone. SULT1B1 showed higher affinities for formation of T3 sulfate than did the phenol sulfotransferases ST1A3 (SULT1A1) or ST1A5. Wang et al. (1998) found that bacterially-expressed SULT1B1 sulfated small phenols such as 1-naphthol and p-nitrophenol and thyroid hormones, including 3,3-prime-diiodothyronine, triiodothyronine, reverse triiodothyronine, and thyroxine. No activity was detected against several sterols or dopamine.

SULT1B1 (NP_055280, 268-306)
This antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide selected from the C-terminal region of human SULT1B1.

Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide.