Analytical Data
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基因名
COL4a5
- Application
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别名
COL4a5；Collagen alpha-5(IV) chain
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P02462
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表达区间
30-167aa
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氨基酸序列
GCAGSGCGKCDCHGVKGQKGERGLPGLQGVIGFPGMQGPEGPQGPPGQKGDTGEPGLPGTKGTRGPPGASGYPGNPGLPGIPGQDGPPGPPGIPGCNGTKGERGPLGPPGLPGFAGNPGPPGLPGMKGDPGEILGHVP
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分子量
39.9kDa
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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
COL4A5 is a gene that encodes a crucial component of type IV collagen, which is a key structural protein in the basement membranes of various tissues, including kidneys, eyes, and ears. Mutations in COL4A5 are primarily implicated in Alport syndrome, a genetic disorder characterized by progressive kidney disease, hearing loss, and eye abnormalities due to defects in the basement membranes. Research on recombinant COL4A5 proteins is essential for understanding the functional role of this collagen type in health and disease. Recombinant proteins can be used to investigate the molecular mechanisms underlying Alport syndrome, develop diagnostic tools, and evaluate potential therapeutic approaches. Moreover, understanding the structure-function relationship of COL4A5 can aid in the design of gene therapy strategies aimed at correcting the underlying genetic defects. Advances in recombinant protein technology also facilitate the creation of animal models, which are vital for studying the pathophysiology of Alport syndrome. Overall, the investigation of COL4A5 recombinant proteins holds significant promise for enhancing our understanding of collagen-related diseases and developing innovative treatment interventions.
