Analytical Data
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Gene name
HEXB/Hexosaminidase B
- Application
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Alternative Names
Hex-B; ENC-1AS; HCC-7; Beta-N-acetylhexosaminidase subunit beta; Cervical cancer proto-oncogene 7 protein; N-acetyl-beta-glucosaminidase subunit beta
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Species
Rat
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
Q6AXR4
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Expression Region
Pro100~Ile216
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Molecular Weight
17kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
Hexosaminidase B (HEXB) is a critical lysosomal enzyme involved in the degradation of gangliosides, particularly GM2 gangliosides, which are complex glycosphingolipids. Deficiency in HEXB activity leads to the accumulation of GM2 gangliosides and is associated with Tay-Sachs disease and Sandhoff disease, neurodegenerative disorders characterized by severe neurological symptoms and early death. The study of recombinant HEXB protein is paramount for understanding the enzyme's structure-function relationship and developing potential therapeutic strategies, such as enzyme replacement therapy. Advances in recombinant DNA technology have facilitated the production of HEXB proteins in model systems, allowing researchers to explore enzyme kinetics, substrate specificity, and the effects of mutations linked to genetic disorders. Moreover, the ability to produce functional HEXB protein enables the assessment of potential inhibitors or activators, providing insights into the modulation of its activity. As research continues to unravel the molecular mechanisms underlying HEXB function, there is significant potential for developing targeted therapies for related metabolic disorders, thereby alleviating the impact of these debilitating conditions on patients and their families.
