Anti-alpha2,6-Sialyltransferase Rabbit IgG Antibody

The accumulation of amyloid beta protein in the cerebral cortex in Alzheimer's disease (AD) is only one of the outcomes of proteolytic cleavage of amyloid precursor protein (APP). More than 50 different mutations in the APP gene can cause early-onset Alzheimer disease. Cleavage by beta- and gamma-secretase (amyloidogenic pathway) leads to production of amyloid-beta and soluble APP-beta, while cleavage by alpha-secretase (nonamyloidogenic pathway) results in a soluble form of APP, sAPP-alpha. Recent studies have identified a glycosyltransferase, ST6 beta-galactosamide alpha-2,6-sialyltranferase 1 (ST6GalI), that is also cleaved by beta-secretase. ST6GalI catalyzes the transfer of sialic acid from cytidine-5'-monophospho-N-acetylneuraminic acid (CMP-sialic acid) to galactose-containing substrates. It is also known as alpha-2,6-ST1, CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,6-sialyltransferase 1, sialyltransferase 1 (beta-galactoside alpha-2,6-sialytransferase), beta-galactoside alpha-2,6-sialyltransferase 1, sialyltransferase 1, 1ST6N, and SIAT1. In humans, beta-secretase cleavage of ST6GalI produces alpha-2,6-sialyltransferase (E44), while in rats it produces alpha-2,6-sialyltransferase (E41).