Analytical Data
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Gene name
Gbal
- Application
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Alternative Names
GbaLysosomal acid glucosylceramidase; Lysosomal acid GCase; EC 3.2.1.45; Acid beta-glucosidase; Beta-glucocerebrosidase; Cholesterol glucosyltransferase; SGTase; EC 2.4.1.-; Cholesteryl-beta-glucosidase; EC 3.2.1.104; D-glucosyl-N-acylsphingosine glucohydrolase
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Species
Mouse
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Source
Yeast
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P17439
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Expression Region
20-515aa
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Molecular Weight
57.5 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
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Protein Description
The Gbal protein, a member of the glycosyltransferase family, has garnered significant attention in recent years due to its pivotal role in various biological processes, including cell signaling, immune response, and metabolic regulation. Research has shown that Gbal is involved in glycosylation, a post-translational modification essential for protein stability and function. Its dysregulation is linked to several diseases, such as cancer and autoimmune disorders. The study of Gbal's structure and function is critical for understanding its mechanism of action. Advanced techniques like X-ray crystallography and cryo-electron microscopy have facilitated insights into its three-dimensional structure, revealing potential active sites for enzymatic activity. Moreover, the exploration of Gbal as a therapeutic target has gained momentum, with ongoing research aimed at developing inhibitors or modulators that can effectively interact with its active sites. Understanding Gbal's interactions with other biomolecules is also vital, as it may unveil novel pathways that could be exploited for drug development. Consequently, the research on Gbal not only enriches our comprehension of glycosylation processes but also holds promise for innovative therapeutic strategies in treating Gbal-related diseases.
