Analytical Data
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Gene name
GBA/Glucosylceramidase
- Application
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Alternative Names
GBA1; GCB; GLUC; Imiglucerase; Alglucerase; Beta-glucocerebrosidase; Glucosidase Beta, Acid; β-Glucosidase; D-Glucosyl-N-Acylsphingosine Glucohydrolase
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Species
Rat
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
B2RYC9
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Expression Region
Ala248~His508
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Molecular Weight
59kDa
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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
Glucosylceramidase (GBA) is an important lysosomal enzyme responsible for the hydrolysis of glucocerebrosides into glucose and ceramide, playing a crucial role in lipid metabolism. Deficiency in GBA activity leads to the accumulation of glucocerebrosides, a condition prominently associated with Gaucher's disease, the most common lysosomal storage disorder. The importance of GBA has gained attention not only due to its relevance in Gaucher's disease but also for its potential links to other neurodegenerative diseases, such as Parkinson's disease, where mutations in the GBA gene have been identified as significant risk factors. The advancement of molecular biology techniques has facilitated the generation of recombinant GBA proteins, enabling detailed studies of enzyme function, regulation, and interaction with small molecule therapeutics. These recombinant proteins serve as valuable tools for developing enzyme replacement therapies, which aim to restore the deficient enzymatic activity in patients. Furthermore, characterizing the structural and functional properties of GBA is essential for understanding its role in disease pathology and for designing novel therapeutic strategies that can address the underlying molecular defects. The ongoing research into recombinant GBA not only contributes to therapeutic advances for Gaucher's disease but also provides insights into broader implications for lysosomal function and neurodegeneration.
