Analytical Data
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Gene name
Collagenase
- Application
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Alternative Names
Hypodermin C (HC)
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Species
Hypoderma lineatum
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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
P08897
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Expression Region
31-260aa
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Molecular Weight
32.7 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
Collagenase is an important enzyme that catalyzes the breakdown of collagen, a key structural protein found in connective tissues. Its role in the degradation of collagen makes it valuable in various biomedical applications, including wound healing, tissue engineering, and cancer research. The production of recombinant collagenase has gained attention due to the limitations associated with traditional extraction methods from animal tissues, including inconsistencies in enzyme activity, potential contamination, and ethical concerns. Advances in recombinant DNA technology have enabled the expression of collagenase in host systems such as bacteria, yeast, or mammalian cells, allowing for a more controlled and scalable production process. Research into recombinant collagenase focuses on optimizing its expression, purification, and characterization, as well as understanding its structure-function relationships to enhance its activity and specificity. Such studies are crucial for developing collagenase-based therapeutics that can improve outcomes in clinical applications, particularly in regenerative medicine and surgery. By harnessing the advantages of recombinant technologies, researchers aim to provide more reliable and efficient sources of collagenase that can meet the growing demand in various scientific and medical fields.
