Anti-SULT2A (N-term) antibody produced in rabbit

One of the major roles of the sulfotransferases (ST) in the metabolism of drugs and endogenous compounds is the conversion of these substances into more hydrophilic water-soluble sulfate conjugates that can be easily excreted. Sulfation may also play a regulatory role for many endogenous compounds, such as steroids and neurotransmitters, by altering the biologic properties of these compounds. Otterness et al. (1992), Kong et al. (1992), and Comer et al. (1993) reported the cloning of cDNAs encoding liver dehydroepiandrosterone (DHEA) sulfotransferase. The predicted protein has 285 amino acids. Although Northern blot analysis of human liver RNA detected transcripts of 3 different sizes, Southern blot analysis of human DNA suggested that only 1 gene is present in the genome. This gene has an important role in the sulfation of both bile acids and steroids in the liver and adrenals. The human adrenal form of this enzyme is physically, immunologically, and kinetically similar, perhaps identical, to the liver form. Dehydroepiandrosterone sulfate is quantitatively one of the major steroids secreted from the adrenal cortex.

SULT2A (NP_003158, 9-46)
This antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide selected from the N-terminal region of human SULT2A.

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