Analytical Data
-
基因名
GBA/glucocerebrosidase
- Application
-
别名
Acid beta-glucosidase; Beta-glucocerebrosidase; SGTase; Cholesteryl-beta-glucosidase
-
种属
Human
-
表达系统
HEK293
-
标签
C-8*His
-
纯度
Greater than 90% as determined by SDS-PAGE.
-
蛋白编号
NP_000148
-
表达区间
A40-Q536
-
蛋白长度
Full Length of Mature Protein
-
分子量
60-70 kDa
-
内毒素
< 1.0 EU per μg protein as determined by the LAL method.
-
性状
Freeze-dried powder
-
缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
-
稳定性测试
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.
-
保存条件 & 期限
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.
-
运输条件
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
Glucocerebrosidase (GBA) is an essential lysosomal enzyme that catalyzes the hydrolysis of glucocerebrosides into glucose and ceramide. Mutations in the GBA gene are associated with Gaucher disease, a lysosomal storage disorder characterized by the accumulation of glucocerebrosides in various tissues, leading to significant morbidity and, in severe cases, mortality. The therapeutic interest in GBA has surged due to its association not only with Gaucher disease but also with increasing evidence linking GBA mutations to Parkinson's disease. As a result, recombinant GBA proteins have been developed to provide enzyme replacement therapy (ERT) for patients with Gaucher disease and to explore potential therapeutic avenues for neurodegenerative disorders. Recent advances in protein engineering and expression systems have enabled the production of highly active and stable recombinant GBA, facilitating biological studies and therapeutic applications. Understanding the structure-function relationship of GBA is critical for optimizing its activity and stability, as well as for designing targeted therapies for associated conditions. The ongoing research aims to elucidate the biochemical pathways influenced by GBA, explore novel delivery methods for enzyme therapies, and assess the impact of GBA modulation on neurodegenerative processes, making it a pivotal focus in both genetic and neurobiological research.
