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Hexosaminidase B is the beta subunit of the lysosomal enzyme beta-hexosaminidase that, together with the cofactor GM2 activator protein, catalyzes the degradation of the ganglioside GM2, and other molecules containing terminal N-acetyl hexosamines. Additionally we are shipping HEXB Antibodies (47) and HEXB Kits (20) and many more products for this protein.
Showing 10 out of 15 products:
mast cell granule beta-hexosaminidase (show HEXA Proteins) is crucial for defense against bacterial invasion, but is not involved in the allergic response. the bactericidal mechanism of beta-hexosaminidase (show HEXA Proteins) involves degradation of bacterial cell wall peptidoglycan.
transgenic inducible strains of Sandhoff disease mice provide a dynamic platform with which to explore the pathophysiological sequelae immediately after loss of neuronal lysosomal beta-hexosaminidase (show HEXA Proteins) activity.
Data suggest that pathogenesis of Sandhoff disease (heritable beta-hexosaminidase (show HEXA Proteins) deficiency) involves an increase in macrophage-inflammatory protein 1alpha (show CCL3 Proteins) that induces monocytes to infiltrate the CNS and trigger neuronal apoptosis.
The bicistronic beta-hexosaminidase (show HEXA Proteins) vector can reverse the biochemical defects and down-stream consequences in Sandhoff neurons, reinforcing its potential for Sandhoff disease in vivo gene therapy.
Beta-hexosaminidase (show HEXA Proteins) is a peptidoglycan hydrolase that surprisingly exerts its mycobactericidal effect at the macrophage plasma membrane during mycobacteria-induced secretion of lysosomes
There was no change in the level of GM2 (show CYB5D2 Proteins) storage and pro-apoptotic activity or astrocyte activation in HexB-/- knockout mice
Mannose receptor (-/-) liver sinusoidal endothelial cells had markedly and significantly reduced enzyme activities for four out of five lysosomal enzymes tested, i.e., cathepsin-D, alpha-mannosidase, beta-hexosaminidase and arylsulfatase.
The absence of beta-N-acetyl-hexosaminidase activity does not alter the differentiation of i-DCs from HSCs, but it is critical for the activation of CD4 (show CD4 Proteins)(+)T cells because knock-down of HEXA (show HEXA Proteins) or HEXB gene causes a loss of function of i-DCs.
A total of 19 HEXB variants were found in the 1092 genomes of which 5 are suspected of having a deleterious effect on hexosaminidase activity.
DNA from Iranian Tay-Sachs patients reveals a novel mutation in HEXB predicting a termination codon or nonsense mutation.
A patient with Sandhoff disease also is found to have a compound macro-deletion in HEXB.
GM2 (show CYB5D2 Proteins) gangliosidosis is caused by the gene mutation. (review)
A highly significant correlation of HEX (show HHEX Proteins)-7 and %CDT has been found. Because of exclusion of the P isoform, HEX (show HHEX Proteins)-7 could be a useful supplementary marker for detecting chronic alcohol abuse.
Expression of beta-hexosaminidase (show HEXA Proteins) in the neurons of Sandhoff disease patients rescues transgenic mice from neurodegeneration.
minigene studies revealed the presence of a novel alternative spliced HEXB mRNA variant also present in normal cells
Characterization of seven novel mutations on the HEXB gene in French Sandhoff patients.
identified 27 different mutations, 14 of which were novel, in the HEXA (show HEXA Proteins) gene and 14 different mutations, 8 of which unreported until now, in the HEXB gene, and attempted to correlate these mutations with the clinical presentation of the patients
Hexosaminidase B is the beta subunit of the lysosomal enzyme beta-hexosaminidase that, together with the cofactor GM2 activator protein, catalyzes the degradation of the ganglioside GM2, and other molecules containing terminal N-acetyl hexosamines. Beta-hexosaminidase is composed of two subunits, alpha and beta, which are encoded by separate genes. Both beta-hexosaminidase alpha and beta subunits are members of family 20 of glycosyl hydrolases. Mutations in the alpha or beta subunit genes lead to an accumulation of GM2 ganglioside in neurons and neurodegenerative disorders termed the GM2 gangliosidoses. Beta subunit gene mutations lead to Sandhoff disease (GM2-gangliosidosis type II).
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