Analytical Data
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Gene name
Beta-galactosidase/GLB1
- Application
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Alternative Names
GL-B; b-GAL; bGAL; ELNR1; EBP; GLB1; Lactase; Elastin Receptor 1,67kDa; Elastin Receptor 1(67kD); Acid Beta-Galactosidase
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Species
Dog
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Source
E. coli
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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
Q9TRY9
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Expression Region
Gln30~Val668
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Molecular Weight
75kDa
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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
Beta-galactosidase, also known as GLB1, is an essential enzyme involved in the hydrolysis of beta-galactosides into monosaccharides, playing a critical role in various biological processes, including lactose metabolism. Its significance is underscored by its association with several diseases, most notably Morquio B syndrome, a lysosomal storage disorder caused by GLB1 mutations leading to the accumulation of glycosaminoglycans. The production of recombinant Beta-galactosidase has gained increasing attention in both research and therapeutic contexts, as it provides a means to study the enzyme's structure-function relationships and its role in cellular pathways. Moreover, recombinant GLB1 has potential therapeutic applications, including enzyme replacement therapy for affected individuals. Advances in recombinant DNA technology have facilitated the efficient expression and purification of GLB1 in various host systems, enhancing its availability for in-depth biochemical characterization. This research aims to elucidate the functional implications of different mutations and to develop strategies for the treatment of GLB1-related disorders. In addition, understanding the enzyme's kinetics and substrate specificity can pave the way for novel biotechnological applications in food and pharmaceutical industries, emphasizing the importance of continued research in this field.
