Analytical Data
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基因名
Alpha-Galactosidase A
- Application
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别名
/
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种属
Rhesus Macaque
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表达系统
E. coli
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标签
N- His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
H9EZY5
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表达区间
32-426aa
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分子量
48.6 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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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
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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.
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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.
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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
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Protein Description
Alpha-Galactosidase A (α-Gal A) is an enzyme crucial for the degradation of glycosphingolipids, particularly those containing galactose residues, and is linked to the rare genetic disorder Fabry disease. Patients with Fabry disease experience severe symptoms due to the accumulation of these lipid substrates, leading to vascular, renal, and cardiac complications. The research on recombinant α-Gal A has surged in recent years as a therapeutic approach to replace the deficient enzyme in affected individuals. Advancements in biotechnological methods have enabled the production of recombinant α-Gal A in various expression systems, such as yeast, bacteria, and mammalian cells, enhancing its efficacy and stability. Studies are focused on optimizing these production methods and improving the enzyme's pharmacokinetics and bioavailability. Additionally, understanding the enzyme's structure and function through techniques like X-ray crystallography and mutational analysis has aided in the development of enzyme replacement therapies. As a result, recombinant α-Gal A has proven effective in clinical trials, leading to its approval as a treatment option. Ongoing research aims to refine these therapies further and explore potential gene therapies to address the underlying genetic defect, ultimately improving the quality of life for Fabry disease patients.












