Analytical Data
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Gene name
COL8a1
- Application
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Alternative Names
COL8-A1; Collagen Alpha-1(VIII)chain; Endothelial collagen; Vastatin
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Species
Rat
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
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Expression Region
Leu591~Met744
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Molecular Weight
18kDa
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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
COL8A1, or Collagen Type VIII Alpha 1, is a crucial component of the extracellular matrix, primarily found in various tissues, including the cornea, blood vessels, and skin. Research on COL8A1 has gained significant attention due to its potential role in both normal physiological processes and pathological conditions. Studies have shown that mutations in the COL8A1 gene are associated with corneal dystrophies, leading to vision impairment and other ocular disorders. Understanding the structure and function of COL8A1 is essential for unraveling its contributions to collagen formation and tissue integrity. The recombinant protein variant of COL8A1 allows for detailed investigations into its biochemical properties and interactions with other matrix components. This research is pivotal not only for elucidating the molecular mechanisms underlying connective tissue diseases but also for developing new therapeutic strategies, including tissue engineering and regenerative medicine applications. By studying the recombinant COL8A1 protein, researchers aim to establish a foundational knowledge that could inform clinical interventions for conditions linked to collagen deficiencies and promote advancements in ocular health. Overall, the exploration of COL8A1 and its recombinant forms highlights the intricate role of collagens in maintaining tissue structure and function, paving the way for future innovations in medical science.
