Rabbit anti-Human HEXA Monoclonal Antibody

Uniprot Id

P06865

Target Species

Human

Target Name

HEXA

Target Full Name

Beta-hexosaminidase subunit alpha

Target Function

Hydrolyzes the non-reducing end N-acetyl-D-hexosamine and/or sulfated N-acetyl-D-hexosamine of glycoconjugates, such as the oligosaccharide moieties from proteins and neutral glycolipids, or from certain mucopolysaccharides. The isozyme S is as active as the isozyme A on the anionic bis-sulfated glycans, the chondroitin-6-sulfate trisaccharide (C6S-3), and the dermatan sulfate pentasaccharide, and the sulfated glycosphingolipid SM2. The isozyme B does not hydrolyze each of these substrates, however hydrolyzes efficiently neutral oligosaccharide. Only the isozyme A is responsible for the degradation of GM2 gangliosides in the presence of GM2A.

Target Involvement

GM2-gangliosidosis 1 (GM2G1)

Target Subcellular Location

Lysosome.

Target Protein Families

Glycosyl hydrolase 20 family

Target Synonyms

Beta hexosaminidase alpha chain precursor ; Beta hexosaminidase subunit alpha; Beta N acetylhexosaminidase; Beta N acetylhexosaminidase subunit alpha; Beta-hexosaminidase A; Beta-hexosaminidase subunit alpha; Beta-N-acetylhexosaminidase subunit alpha; Hexa; HEXA_HUMAN; Hexosaminidase A (alpha polypeptide); Hexosaminidase A alpha polypeptide; Hexosaminidase A; Hexosaminidase subunit A; MGC99608; N acetyl beta glucosaminidase; N acetyl beta glucosaminidase subunit alpha; N-acetyl-beta-glucosaminidase subunit alpha; TSD

Target Background

This gene encodes a member of the glycosyl hydrolase 20 family of proteins. The encoded preproprotein is proteolytically processed to generate the alpha subunit of the lysosomal enzyme beta-hexosaminidase. This enzyme, together with the cofactor GM2 activator protein, catalyzes the degradation of the ganglioside GM2, and other molecules containing terminal N-acetyl hexosamines. Mutations in this gene lead to an accumulation of GM2 ganglioside in neurons, the underlying cause of neurodegenerative disorders termed the GM2 gangliosidoses, including Tay-Sachs disease (GM2-gangliosidosis type I). Alternative splicing results in multiple transcript variants, at least one of which encodes a preproprotein that is proteolytically processed.