Human Hexosaminidase A/HEXA Alexa Fluor® 700-conjugated Antibody

Applications

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

Preparation and Storage

Background: Hexosaminidase A/HEXA

HEXA (beta-hexosaminidase subunit alpha; also hexaminidase subunit alpha) is a 50-56 kDa glycoprotein member of the glycosyl hydrolase #20 family of enzymes. It is found in the lysosomes of a variety of cell types including fibroblasts, lacrimal acinar cells, and neurons. beta -Hexosaminidase is a multimeric enzyme that cleaves aminoacetylhexosamines from multiple glycosylated molecules. It exists in three noncovalent isozyme forms, among which is an A form that is trimeric and composed of one alpha - and two beta -subunits, a B form that is tetrameric and contains two alpha - and two beta -subunits, and a dimeric S form that contains two alpha -subunits. The alpha - and beta -subunits are products of related but distinct genes. The beta -hexosiminidase A form acts on a wide range of substrates, while the B form activity is biased towards sulfated hexoses. Human HEXA is synthesized as a 529 aa (amino acid) prepro-precursor. It contains a 22 aa signal sequence, a 66 aa prosegment, and a 441 aa mature region that contains a catalytic domain (aa 167-488). The prosegment may undergo additional processing through His90, and this segment (≈ 6 kDa) is known to remain linked to the mature region via a disulfide bond. Notably, circulating HEXA is comprised only of subunit proforms whose MW may run some 10 kDa higher in SDS-PAGE. Over aa 23-529, human HEXA shares 85% and 57% aa sequence identity with mouse HEXA and the human HEXA beta -subunit proprecursor, respectively.

Product Datasheets

Related Research Areas

• Glycobiology-related Enzymes
• Lysosomal Enzymes
• Platelet Lysosome Molecules
• Search Bioprocessing Enzymes
• Search Glycobiology-related Enzymes