Analytical Data
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基因名
COL1
- Application
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种属
Horse
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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
XP_023508478.1
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表达区间
Arg1226~Phe1462
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分子量
30kDa
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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
Collagen type I (COL1) is the most abundant collagen in the human body, playing a crucial role in maintaining the structural integrity and mechanical properties of various tissues, including skin, bones, tendons, and ligaments. The study of COL1 recombinant proteins has gained significant attention in recent years due to their potential applications in regenerative medicine, tissue engineering, and biomaterials development. Advances in molecular cloning and recombinant DNA technology have enabled the production of COL1 in various expression systems, facilitating the study of its structural properties and biological functions. The ability to generate COL1 proteins allows for the investigation of their interactions with cells and other extracellular matrix components, contributing to our understanding of tissue repair and development. Moreover, recombinant COL1 can be engineered to possess specific properties, enhancing its usability in therapeutic contexts. Researchers are exploring its use in wound healing, bone regeneration, and even as a scaffold in 3D cell cultures and organoid development. Overall, the continued exploration of COL1 recombinant proteins holds promise for innovative treatments and the advancement of tissue engineering strategies.
