Analytical Data
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Gene name
GBA/glucocerebrosidase
- Application
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Alternative Names
Acid beta-glucosidase; Beta-glucocerebrosidase; SGTase; Cholesteryl-beta-glucosidase
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Species
Human
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Source
HEK293
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Tag
C-8*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
NP_000148
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Expression Region
A40-Q536
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Protein Length
Full Length of Mature Protein
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Molecular Weight
60-70 kDa
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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
Related Products
Protein Description
Glucocerebrosidase (GBA) is an essential lysosomal enzyme that catalyzes the hydrolysis of glucocerebrosides into glucose and ceramide. Mutations in the GBA gene are associated with Gaucher disease, a lysosomal storage disorder characterized by the accumulation of glucocerebrosides in various tissues, leading to significant morbidity and, in severe cases, mortality. The therapeutic interest in GBA has surged due to its association not only with Gaucher disease but also with increasing evidence linking GBA mutations to Parkinson's disease. As a result, recombinant GBA proteins have been developed to provide enzyme replacement therapy (ERT) for patients with Gaucher disease and to explore potential therapeutic avenues for neurodegenerative disorders. Recent advances in protein engineering and expression systems have enabled the production of highly active and stable recombinant GBA, facilitating biological studies and therapeutic applications. Understanding the structure-function relationship of GBA is critical for optimizing its activity and stability, as well as for designing targeted therapies for associated conditions. The ongoing research aims to elucidate the biochemical pathways influenced by GBA, explore novel delivery methods for enzyme therapies, and assess the impact of GBA modulation on neurodegenerative processes, making it a pivotal focus in both genetic and neurobiological research.
