Analytical Data
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Gene name
colA
- Application
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Alternative Names
120 kDa collagenase Microbial collagenase
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Species
Clostridium perfringens
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Source
E. coli
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Tag
N- His & C- Myc
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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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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
Related Products
Protein Description
ColA, short for collagenase A, is a type of proteolytic enzyme that primarily targets collagen, a crucial structural protein found in connective tissues. The study of ColA recombinant proteins has gained significant attention due to their potential applications in various fields, including medicine, biotechnology, and tissue engineering. Research on ColA focuses on its ability to effectively degrade collagen, which can facilitate wound healing, enhance tissue regeneration, and assist in the development of therapeutic strategies for fibrotic diseases. The recombinant production of ColA allows for the generation of large quantities of the enzyme with controlled activity and specificity, overcoming the limitations associated with traditional extraction methods from animal tissues. Moreover, understanding the molecular mechanisms underlying ColA's activity could inform the design of inhibitors for therapeutic interventions in pathological conditions characterized by excessive collagen deposition. Advances in genetic engineering techniques have enabled the optimization of ColA for specific applications, such as targeted drug delivery systems or as a tool for tissue scaffolding in regenerative medicine. The ongoing research into ColA not only highlights its biochemical significance but also its versatility in addressing challenges in modern healthcare and biotechnology.
