Analytical Data
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Gene name
colA
- Application
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Alternative Names
colA；COL1AL；Collagen alpha-1(XXI) chain
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Species
Clostridium
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P43153
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Expression Region
90-370aa
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AA Sequence
NKIYTFDELNRMNYSDLVELIKTISYENVPDLFNFNDGSYTFFSNRDRVQAIIYGLEDSGRTYTADDDKGIPTLVEFLRAGYYLGFYNKQLSYLNTPQLKNECLPAMKAIQYNSNFRLGTKAQDGVVEALGRLIGNASADPEVINNCIYVLSDFKDNIDKYGSNYSKGNAVFNLMKGIDYYTNSVIYNTKGYDAKNTEFYNRIDPYMERLESLCTIGDKLNNDNAWLVNNALYYTGRMGKFREDPSISQRALERAMKEYPYLSYQYIEAANDLDLNFGGKN
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Molecular Weight
39.7 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
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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Storage & Shelf Life
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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Shipping
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.
