Analytical Data
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Gene name
Collagen alpha-1(IX) chain/COL9A1
- Application
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Alternative Names
COL9-A1; MED; Collagen Alpha-1(IX)chain
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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 95% as determined by SDS-PAGE.
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Uniprot
F1LQ93
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Expression Region
Phe24~Leu268
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Molecular Weight
32kDa
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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
Collagen alpha-1(IX) chain, or COL9A1, is a vital component of the extracellular matrix, primarily found in cartilage and intervertebral discs. This protein plays a crucial role in maintaining the structural integrity and function of these tissues, contributing to the mechanical properties essential for load-bearing and support. Abnormalities in COL9A1 expression or function are linked to various skeletal disorders, such as osteoarthritis and intervertebral disc degeneration, highlighting its significance in both developmental and pathological contexts. The study of COL9A1 recombinant protein has gained attention due to its potential applications in regenerative medicine and tissue engineering. By producing and characterizing this protein, researchers aim to gain insights into its structural properties and interactions with other matrix components. Furthermore, understanding the post-translational modifications and functional mechanisms of COL9A1 may aid in developing therapeutic strategies for conditions associated with cartilage and disc degeneration. The creation of recombinant COL9A1 not only provides a model for studying its biological roles but also offers opportunities for drug delivery systems and biomaterials that can mimic the natural extracellular matrix environment. In summary, COL9A1 is significant for its contributions to cartilage health, and its recombinant form serves as a valuable tool for advancing research in both basic biology and clinical applications.
