Analytical Data
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Gene name
GLA
- Application
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Alternative Names
Alpha-D-galactosidase AAlpha-D-galactoside galactohydrolase;MelibiaseINN: Agalsidase
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Species
Human
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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
P06280
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Expression Region
32-429aa
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Molecular Weight
49.4 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
GLA, or galactosylceramidase, is an essential enzyme involved in the metabolism of complex lipids, specifically sphingolipids. Deficiencies in GLA lead to a rare lysosomal storage disorder known as Krabbe disease, which is characterized by severe neurological impairment and early mortality. The need for effective therapeutic interventions has spurred extensive research into the recombinant production of GLA, which can potentially provide a viable treatment option through enzyme replacement therapy (ERT). Advances in recombinant DNA technology have facilitated the expression of human GLA in various systems, enabling the generation of biologically active enzyme for clinical application. Moreover, understanding the structure and function of GLA at the molecular level has been crucial for developing strategies to enhance its stability and efficacy. Additionally, studies focusing on the localization and delivery methods of GLA within the body aim to optimize its therapeutic potential. The ongoing exploration of GLA reconstitution not only holds promise for patients with Krabbe disease but also paves the way for novel approaches in treating other lysosomal storage disorders. As research progresses, the insights gained from GLA studies could lead to advancements in gene therapy and personalized medicine, offering hope for better management of these debilitating conditions.
