Analytical Data
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Gene name
COL4a2
- Application
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Alternative Names
COL4a2;Collagen alpha-2(IV) chain
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P08572
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Expression Region
1493-1712aa
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AA Sequence
VKHSQTDQEPMCPVGMNKLWSGYSLLYFEGQEKAHNQDLGLAGSCLARFS TMPFLYCNPGDVCYYASRNDKSYWLSTTAPLPMMPVAEDEIKPYISRCSV CEAPAIAIAVHSQDVSIPHCPAGWRSLWIGYSFLMHTAAGDEGGGQSLVS PGSCLEDFRATPFIECNGGRGTCHYYANKYSFWLTTIPEQSFQGSPSADT LKAGLIRTHISRCQVCMKNL
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Molecular Weight
168 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
Related Products
Protein Description
COL4A2, a member of the collagen family, encodes alpha-2 chain of type IV collagen, which is crucial for the structural integrity of basement membranes. Abnormalities in the COL4A2 gene have been linked to various human diseases, including nephropathy, Alport syndrome, and connective tissue disorders. Research on COL4A2 recombinant proteins is essential for understanding the molecular mechanisms underlying these diseases and developing potential therapeutic strategies. The production of COL4A2 recombinant proteins allows for detailed studies of its structural properties, interactions with other extracellular matrix components, and its role in cell signaling pathways. Moreover, COL4A2 recombinant proteins can be utilized in tissue engineering and regenerative medicine, offering insights into their potential applications in repairing or regenerating damaged tissues. As a result, the study of COL4A2 and its recombinant forms contributes significantly to the knowledge of collagen-related pathologies and advances in biomedical research.











