HEXA/Hexosaminidase A Protein, Human (sf9, His)

HEXA (hexosaminidase A) proteolytically hydrolyzes N-acetyl-D-hexosamine and/or sulfated residues in glycocomplexes, including oligosaccharides, glycolipids, and mucopolysaccharides. The activity of isoenzyme S towards anionic disulfated glycans is comparable to that of isoenzyme A, while isoenzyme B can effectively hydrolyze neutral oligosaccharides but cannot hydrolyze anionic disulfated substrates. HEXA/Hexosaminidase A Protein, Human (sf9, His) is the recombinant human-derived HEXA/Hexosaminidase A protein, expressed by Sf9 insect cells , with C-His labeled tag.

HEXA (Hexosaminidase A) protein plays a pivotal role in hydrolyzing the non-reducing end N-acetyl-D-hexosamine and/or sulfated N-acetyl-D-hexosamine residues found in various glycoconjugates, including oligosaccharide moieties from proteins, neutral glycolipids, and specific mucopolysaccharides. Isozyme S exhibits comparable activity to isozyme A on anionic bis-sulfated glycans such as chondroitin-6-sulfate trisaccharide (C6S-3), dermatan sulfate pentasaccharide, and the sulfated glycosphingolipid SM2. In contrast, isozyme B efficiently hydrolyzes neutral oligosaccharides but does not act on these anionic bis-sulfated substrates. Importantly, only isozyme A is responsible for the degradation of GM2 gangliosides in the presence of GM2A, showcasing its specificity and central role in this biochemical process.

Human

Sf9 insect cells

C-His

AAD13932.1 (L23-T529)

3073  [NCBI]

MTSSRLWFSLLLAAAFAGRATALWPWPQNFQTSDQRYVLYPNNFQFQYDVSSAAQPGCSVLDEAFQRYRDLLFGSGSWPRPYLTGKRHTLEKNVLVVSVVTPGCNQLPTLESVENYTLTINDDQCLLLSETVWGALRGLETFSQLVWKSAEGTFFINKTEIEDFPRFPHRGLLLDTSRHYLPLSSILDTLDVMAYNKLNVFHWHLVDDPSFPYESFTFPELMRKGSYNPVTHIYTAQDVKEVIEYARLRGIRVLAEFDTPGHTLSWGPGIPGLLTPCYSGSEPSGTFGPVNPSLNNTYEFMSTFFLEVSSVFPDFYLHLGGDEVDFTCWKSNPEIQDFMRKKGFGEDFKQLESFYIQTLLDIVSSYGKGYVVWQEVFDNKVKIQPDTIIQVWREDIPVNYMKELELVTKAGFRALLSAPWYLNRISYGPDWKDFYIVEPLAFEGTPEQKALVIGGEACMWGEYVDNTNLVPRLWPRAGAVAERLWSNKLTSDLTFAYERLSHFRCELLRRGVQAQPLNVGFCEQEFEQT

Approximately 64 kDa

Greater than 95% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.