Analytical Data
-
Gene name
COL8A1
- Application
-
Alternative Names
COL8A1；C3orf7；Collagen alpha-1(VIII) chain
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P27658
-
Expression Region
572-744aa
-
AA Sequence
AVMPPTPPPQGEYLPDMGLGIDGVKPPHAYGAKKGKNGGPAYEMPAFTAELTAPFPPVGAPVKFNKLLYNGRQNYNPQTGIFTCEVPGVYYFAYHVHCKGGNVWVALFKNNEPVMYTYDEYKKGFLDQASGSAVLLLRPGDRVFLQMPSEQAAGLYAGQYVHSSFSGYLLYPM
-
Molecular Weight
31.9 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
Collagen type VIII alpha 1 (COL8A1) is a significant component of the extracellular matrix, primarily found in the corneal endothelium and other tissues where it plays a crucial role in maintaining tissue structure and integrity. Research on COL8A1 has gained attention due to its implications in various ocular diseases, including Fuchs' endothelial corneal dystrophy and other conditions affecting corneal and retinal health. Mutations in the COL8A1 gene have been linked to these disorders, highlighting its importance in maintaining cellular function and tissue homeostasis. The production of recombinant COL8A1 protein has become a focal point in biomedical research, as it allows for detailed studies of its biochemical properties and its interactions with other matrix components. Understanding the functional dynamics of COL8A1 can provide valuable insights into its role in disease mechanisms and may lead to potential therapeutic strategies. Furthermore, recombinant COL8A1 can serve as a valuable tool for tissue engineering applications, offering opportunities for the development of biomaterials that mimic the native extracellular matrix environment. Overall, the investigation of COL8A1 and its recombinant forms enriches our understanding of collagen biology and opens avenues for innovative treatments for degenerative diseases involving the extracellular matrix.
