Analytical Data
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Gene name
Collagen alpha-1(VIII) chain/COL8A1
- Application
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Alternative Names
COL8-A1; Collagen Alpha-1(VIII)chain; Endothelial collagen; Vastatin
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Species
Human
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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
P27658
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Expression Region
Pro575~Pro743
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Molecular Weight
20kDa
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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
The collagen alpha-1(VIII) chain, also known as COL8A1, is a crucial component of the extracellular matrix, particularly in the structure of various tissues, including the vascular system and the cornea. Its primary role involves providing structural support and maintaining the integrity of these tissues. Abnormalities in COL8A1 have been linked to various pathologies, such as glaucoma and corneal dystrophies, highlighting its significance in ocular health and disease. The study of COL8A1 is vital for understanding tissue development, repair mechanisms, and the underlying causes of related disorders. Recombinant COL8A1 protein production allows for in-depth investigation of its functional properties, interactions, and potential therapeutic applications. By utilizing advanced molecular biology techniques, researchers aim to elucidate the structural and biological characteristics of this collagen type, ultimately paving the way for novel treatments targeting COL8A1-related diseases. Furthermore, understanding the mechanisms behind COL8A1 function may contribute to advancements in tissue engineering and regenerative medicine, enhancing therapeutic strategies for conditions involving collagen deficiencies. Overall, the exploration of COL8A1 is not only critical for scientific understanding but also holds promise for clinical applications.
