Analytical Data
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Gene name
GLA
- Application
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Alternative Names
GLA；Alpha-galactosidase A
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P06280
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Expression Region
1-429aa
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AA Sequence
MQLRNPELHLGCALALRFLALVSWDIPGARALDNGLARTPTMGWLHWERF MCNLDCQEEPDSCISEKLFMEMAELMVSEGWKDAGYEYLCIDDCWMAPQR DSEGRLQADPQRFPHGIRQLANYVHSKGLKLGIYADVGNKTCAGFPGSFG YYDIDAQTFADWGVDLLKFDGCYCDSLENLADGYKHMSLALNRTGRSIVY SCEWPLYMWPFQKPNYTEIRQYCNHWRNFADIDDSWKSIKSILDWTSFNQ ERIVDVAGPGGWNDPDMLVIGNFGLSWNQQVTQMALWAIMAAPLFMSNDL RHISPQAKALLQDKDVIAINQDPLGKQGYQLRQGDNFEVWERPLSGLAWA VAMINRQEIGGPRSYTIAVASLGKGVACNPACFITQLLPVKRKLGFYEWT SRLRSHINPTGTVLLQLENTMQMSLKDLL
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Molecular Weight
73 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
GLA, or glucocerebrosidase, is an essential enzyme that plays a crucial role in the metabolism of glucocerebrosides, sphingolipids found in cell membranes. Mutations in the GBA gene, which encodes the enzyme GLA, lead to Gaucher's disease, a genetic disorder characterized by the accumulation of glucocerebrosides, resulting in various symptoms such as organ enlargement, anemia, and bone complications. This condition has garnered significant attention due to its prevalence and the severity of its impact on patients' quality of life. The development of recombinant GLA proteins has emerged as a promising therapeutic approach to manage Gaucher's disease. These recombinant proteins aim to provide enzyme replacement therapy, restoring the function of the deficient enzyme. Research has focused on optimizing the production and purification of GLA, enhancing its stability and activity, and evaluating its safety and efficacy in clinical settings. Advances in biotechnological techniques, such as plant-based expression systems and microbial fermentation, have facilitated the generation of high-yield, fully functional GLA variants. Furthermore, studies have investigated the structural and functional aspects of GLA, enabling a better understanding of its enzymatic mechanisms and the effects of various mutations. Overall, the research on GLA recombinant protein continues to evolve, aiming not only to improve existing therapies for Gaucher's disease but also to explore potential applications for related lipid storage disorders.
