Analytical Data
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Gene name
COL4A2
- Application
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Species
Human
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Source
Baculovirus
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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
P08572
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Expression Region
1261-1712aa
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Molecular Weight
48.6 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 gene encoding collagen type IV alpha 2 chain, is pivotal in the formation of basement membranes, contributing to the structural integrity of various tissues, including the kidney, skin, and blood vessels. Mutations in COL4A2 are linked to several connective tissue disorders, such as Alport syndrome and Ehlers-Danlos syndrome, resulting in renal dysfunction, vascular abnormalities, and other systemic complications. The study of COL4A2 recombinant proteins has gained traction due to their potential in elucidating the molecular mechanisms underlying these conditions and developing therapeutic interventions. Recombinant COL4A2 can be produced in various expression systems, allowing researchers to investigate its biochemical properties, interactions with other matrix components, and the impact of specific mutations. Moreover, the use of recombinant COL4A2 helps in the exploration of its role in cell adhesion, migration, and differentiation, which are crucial processes in wound healing and tissue regeneration. As research progresses, understanding the functional implications of COL4A2 through recombinant protein studies may lead to advancements in regenerative medicine and targeted therapies for related disorders, providing hope for improved clinical outcomes.
