SAB1402803
Monoclonal Anti-HEXA antibody produced in mouse
clone 3D1, purified immunoglobulin, buffered aqueous solution
Synonym(s):
MGC99608, TSD
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About This Item
UNSPSC Code:
12352203
NACRES:
NA.41
biological source
mouse
Quality Level
conjugate
unconjugated
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
3D1, monoclonal
form
buffered aqueous solution
mol wt
antigen ~84.3 kDa
species reactivity
human
technique(s)
immunofluorescence: suitable
indirect ELISA: suitable
western blot: 1-5 μg/mL
isotype
IgG1κ
NCBI accession no.
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... HEXA(3073)
General description
Hexosaminidase subunit alpha (HEXA) gene is located on the human chromosome 15q23-q24. HEXA is found to be associated with the external leaflet of plasma membrane of human fibroblasts. α and β subunits of HEXA have 57% of similarity in their amino acid sequences.
Immunogen
HEXA (AAH18927, 1 a.a. ~ 529 a.a) full-length recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.
Sequence
MTSSRLWFSLLLAAAFAGRATALWPWPQNFQTSDQRYVLYPNNFQFQYDVSSAAQPGCSVLDEAFQRYRDLLFGSGSWPRPYLTGKRHTLEKNVLVVSVVTPGCNQLPTLESVENYTLTINDDQCLLLSETVWGALRGLETFSQLVWKSAEGTFFINKTEIEDFPRFPHRGLLLDTSRHYLPLSSILDTLDVMAYNKLNVFHWHLVDDPSFPYESFTFPELMRKGSYNPVTHIYTAQDVKEVIEYARLRGIRVLAEFDTPGHTLSWGPGIPGLLTPCYSGSEPSGTFGPVNPSLNNTYEFMSTFFLEVSSVFPDFYLHLGGDEVDFTCWKSNPEIQDFMRKKGFGEDFKQLESFYIQTLLDIVSSYGKGYVVWQEVFDNKVKIQPDTIIQVWREDIPVNYMKELELVTKAGFRALLSAPWYLNRISYGPDWKDFYVVEPLAFEGTPEQKALVIGGEACMWGEYVDNTNLVPRLWPRAGAVAERLWSNKLTSDLTFAYERLSHFRCELLRRGVQAQPLNVGFCEQEFEQT
Sequence
MTSSRLWFSLLLAAAFAGRATALWPWPQNFQTSDQRYVLYPNNFQFQYDVSSAAQPGCSVLDEAFQRYRDLLFGSGSWPRPYLTGKRHTLEKNVLVVSVVTPGCNQLPTLESVENYTLTINDDQCLLLSETVWGALRGLETFSQLVWKSAEGTFFINKTEIEDFPRFPHRGLLLDTSRHYLPLSSILDTLDVMAYNKLNVFHWHLVDDPSFPYESFTFPELMRKGSYNPVTHIYTAQDVKEVIEYARLRGIRVLAEFDTPGHTLSWGPGIPGLLTPCYSGSEPSGTFGPVNPSLNNTYEFMSTFFLEVSSVFPDFYLHLGGDEVDFTCWKSNPEIQDFMRKKGFGEDFKQLESFYIQTLLDIVSSYGKGYVVWQEVFDNKVKIQPDTIIQVWREDIPVNYMKELELVTKAGFRALLSAPWYLNRISYGPDWKDFYVVEPLAFEGTPEQKALVIGGEACMWGEYVDNTNLVPRLWPRAGAVAERLWSNKLTSDLTFAYERLSHFRCELLRRGVQAQPLNVGFCEQEFEQT
Biochem/physiol Actions
Hexosaminidase subunit alpha (HEXA) degrades the carbohydrate moieties of glycoproteins, glycolipids and proteoglycans. Mutations in the α chain of HEXA impairs folding, trafficking and enzyme assembly. Lysosomal β-hexosaminidase α subunit is downregulated in prostate cancer cells due to hypermethylation of gene promoter.
Physical form
Solution in phosphate buffered saline, pH 7.4
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Storage Class Code
10 - Combustible liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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The X-ray crystal structure of human $\beta$-hexosaminidase B provides new insights into Sandhoff disease
Maier T, et al.
Journal of Molecular Biology, 328(3), 669-681 (2003)
Identification of plasma membrane associated mature beta-hexosaminidase A, active towards GM2 ganglioside, in human fibroblasts
Mencarelli S, et al.
Febs Letters, 579(25), 5501-5506 (2005)
Production of recombinant beta-hexosaminidase A, a potential enzyme for replacement therapy for Tay-Sachs and Sandhoff diseases, in the methylotrophic yeast Ogataea minuta
Akeboshi H, et al.
Applied and Environmental Microbiology, 73(15), 4805-4812 (2007)
Tay-Sachs disease mutations in HEXA target the alpha chain of hexosaminidase A to endoplasmic reticulum-associated degradation
Dersh D, et al.
Molecular Biology of the Cell, 27(24), 3813-3827 (2016)
Hypermethylation contributes to down-regulation of lysosomal beta-hexosaminidase alpha subunit in prostate cancer cells
Costanzi E, et al.
Biochimie, 101, 75-82 (2014)
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