The Alpha 2,6-Sialyltransferase Antibody or ST6Gal-I Antibody is affinity-purified to recognize ST6Gal-I protein. The Alpha 2,6-Sialyltransferase Antibody is raised in rabbit using synthetic peptides and can be applied to Western blot (WB) detection of ST6Gal-I protein.
The accumulation of amyloid beta plaques in the cerebral cortex during Alzheimer's disease (AD) is only one of the outcomes of proteolytic cleavage of amyloid precursor protein (APP). Over 50 different mutations in the APP gene have been found to increase the chances of amyloid beta plaque generation, leading to early-onset Alzheimer disease. Cleavage of mutated APP by beta- and gamma-secretase (amyloidogenic pathway) leads to production of pathologic, insoluble amyloid-beta deposits as well as non-pathologic, soluble APP-beta (sAPP-beta), while cleavage by alpha-secretase (nonamyloidogenic pathway) results in only sAPP-alpha.
Recent studies have also identified that the glycosyltransferase ST6 beta-galactoside alpha-2,6-sialyltransferase (ST6Gal-I) is cleaved by beta-secretase (BACE1)1. ST6Gal-I catalyzes the transfer of an alpha 2,6-linked sialic acid to the N-glycans of certain receptors. 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, BACE1 cleavage of ST6Gal-I generates alpha-2,6-sialyltransferase (E44 form), while in rats it generates alpha-2,6-sialyltransferase (E41 form).