Analytical Data
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基因名
colA
- Application
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别名
colA;COL1AL;Collagen alpha-1(XXI) chain
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种属
Clostridium
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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
P43153
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表达区间
90-370aa
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氨基酸序列
NKIYTFDELNRMNYSDLVELIKTISYENVPDLFNFNDGSYTFFSNRDRVQAIIYGLEDSGRTYTADDDKGIPTLVEFLRAGYYLGFYNKQLSYLNTPQLKNECLPAMKAIQYNSNFRLGTKAQDGVVEALGRLIGNASADPEVINNCIYVLSDFKDNIDKYGSNYSKGNAVFNLMKGIDYYTNSVIYNTKGYDAKNTEFYNRIDPYMERLESLCTIGDKLNNDNAWLVNNALYYTGRMGKFREDPSISQRALERAMKEYPYLSYQYIEAANDLDLNFGGKN
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分子量
39.7 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
ColA, a collagenase enzyme derived from specific bacterial sources, has garnered significant attention in biomedical research due to its unique ability to selectively degrade collagen, a major structural protein in connective tissues. This characteristic positions ColA as a valuable tool in various applications, including tissue engineering, wound healing, and reconstructive surgery, where the precise modulation of collagen is essential for promoting tissue regeneration and repair. Understanding the biochemical properties and mechanisms of action of ColA is crucial for optimizing its use in therapeutic contexts. Recent studies have explored its structural characteristics, enzyme kinetics, and potential effects on cellular behavior in order to harness its capabilities effectively. Furthermore, the recombinant production of ColA facilitates its large-scale availability and allows for the exploration of modified versions with enhanced activity or specificity. As a result, ongoing research into ColA continues to unveil promising biomedical applications, ranging from enhanced surgical outcomes to innovative strategies for treating fibrotic diseases and other collagen-related conditions. By dissecting its molecular functions and establishing effective methods for its application, scientists aim to translate ColA's biological properties into clinical solutions, thereby revolutionizing treatment approaches in regenerative medicine.












