Analytical Data
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Gene name
GBA
- Application
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Alternative Names
GBA；CBG；CBGL1;Cytosolic beta-glucosidase
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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
P04062-1
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Expression Region
40-536aa
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AA Sequence
ARPCIPKSFGYSSVVCVCNATYCDSFDPPTFPALGTFSRYESTRSGRRME LSMGPIQANHTGTGLLLTLQPEQKFQKVKGFGGAMTDAAALNILALSPPA QNLLLKSYFSEEGIGYNIIRVPMASCDFSIRTYTYADTPDDFQLHNFSLP EEDTKLKIPLIHRALQLAQRPVSLLASPWTSPTWLKTNGAVNGKGSLKGQ PGDIYHQTWARYFVKFLDAYAEHKLQFWAVTAENEPSAGLLSGYPFQCLG FTPEHQRDFIARDLGPTLANSTHHNVRLLMLDDQRLLLPHWAKVVLTDPE AAKYVHGIAVHWYLDFLAPAKATLGETHRLFPNTMLFASEACVGSKFWEQ SVRLGSWDRGMQYSHSIITSLLYHVVGWTDWNLALNPEGGPNWVRNFVDS PIIVDITKDTFYKQPMFYHLGHFSKFIPEGSQRVGLVASQKNDLDAVALM HPDGSAVVVVLNRSSKDVPLTIKDPAVGFLETISPGYSIHTYLWRRQ
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Molecular Weight
56 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
The study of GBA (Glucosylceramidase) recombinant proteins has gained significant importance due to their association with Gaucher disease, a genetic disorder caused by mutations in the GBA gene leading to a deficiency in the enzyme responsible for glucocerebroside degradation. This deficiency results in the accumulation of glucocerebrosides in cells, causing various clinical manifestations, including anemia, bone pain, and organomegaly. Research has increasingly focused on the production of recombinant GBA proteins as therapeutic agents, especially for enzyme replacement therapy (ERT), which aims to restore the enzyme's activity in affected individuals. Advances in biotechnological methods, such as the use of mammalian cell systems and yeast expression systems, have enabled the efficient production and purification of these proteins, allowing for better characterization and optimization. Moreover, understanding the structure-function relationships of GBA proteins through recombinant engineering can facilitate the development of more effective ERT formulations and other novel therapeutic approaches, including substrate reduction therapy and gene therapy. The ongoing research into GBA recombinant proteins not only provides insights into the molecular mechanisms underlying Gaucher disease but also holds promise for improving treatment strategies and patient outcomes for this and related lysosomal storage disorders.
