Analytical Data
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Gene name
GBA1
- Application
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Alternative Names
GBA1；GBA；GC；GLUC；Lysosomal acid glucosylceramidase
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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
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Expression Region
40-536aa
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AA Sequence
ARPCIPKSFGYSSVVCVCNATYCDSFDPPTFPALGTFSRYESTRSGRRMELSMGPIQANHTGTGLLLTLQPEQKFQKVKGFGGAMTDAAALNILALSPPAQNLLLKSYFSEEGIGYNIIRVPMASCDFSIRTYTYADTPDDFQLHNFSLPEEDTKLKIPLIHRALQLAQRPVSLLASPWTSPTWLKTNGAVNGKGSLKGQPGDIYHQTWARYFVKFLDAYAEHKLQFWAVTAENEPSAGLLSGYPFQCLGFTPEHQRDFIARDLGPTLANSTHHNVRLLMLDDQRLLLPHWAKVVLTDPEAAKYVHGIAVHWYLDFLAPAKATLGETHRLFPNTMLFASEACVGSKFWEQSVRLGSWDRGMQYSHSIITNLLYHVVGWTDWNLALNPEGGPNWVRNFVDSPIIVDITKDTFYKQPMFYHLGHFSKFIPEGSQRVGLVASQKNDLDAVALMHPDGSAVVVVLNRSSKDVPLTIKDPAVGFLETISPGYSIHTYLWRRQ
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Molecular Weight
61.2 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
GBA1, the gene encoding the enzyme glucocerebrosidase, is crucial for the metabolism of glycosphingolipids, and its mutations are known to cause Gaucher disease, a lysosomal storage disorder characterized by the accumulation of glucocerebroside in various tissues. This condition has significant clinical implications, including organomegaly, skeletal abnormalities, and increased risk of Parkinson's disease due to shared pathological pathways. Recent advances in recombinant protein technology have enabled the production of active GBA1, which has garnered attention for potential therapeutic applications. Researchers are exploring enzyme replacement therapy (ERT) utilizing recombinant GBA1 to effectively manage Gaucher disease symptoms and potentially mitigate neurodegenerative risks. Furthermore, studying GBA1 recombinant protein helps elucidate the enzyme's structure-function relationship, providing insights that could lead to the development of small molecule chaperones or gene therapies, thus expanding treatment options for patients with various GBA1-related disorders. This research not only addresses a pressing clinical need but also contributes to a broader understanding of lysosomal biology and its implications in diseases beyond Gaucher, highlighting the significance of GBA1 in both heredity and neurodegenerative conditions.
