Analytical Data
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Gene name
COL4a5
- Application
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Alternative Names
COL4-A5; ASLN; ATS; CA54; Collagen Alpha-5(IV)chain; Alport Syndrome
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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
P29400
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Expression Region
Gly1461~Thr1685
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Molecular Weight
31kDa
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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
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Protein Description
COL4A5 is a gene that encodes the alpha-5 chain of type IV collagen, a crucial structural component of the basement membrane in various tissues, including the kidneys, eyes, and skin. Mutations in COL4A5 are mainly associated with Alport syndrome, a genetic disorder characterized by progressive nephritis, sensorineural hearing loss, and ocular abnormalities. Research on the recombinant protein of COL4A5 has become increasingly important as scientists seek to understand its role in tissue integrity and disease progression. Recombinant COL4A5 protein can be used to explore the molecular mechanisms underlying Alport syndrome, investigate the effects of specific mutations, and develop potential therapeutic strategies. By producing the protein in a laboratory setting, researchers can study its interactions with other extracellular matrix components, elucidate its functional properties, and assess the impact of altered collagen structures on cellular behavior. Furthermore, this research has implications not only for understanding Alport syndrome but also for broader applications in tissue engineering and regenerative medicine, where collagen-based scaffolds are utilized to facilitate tissue repair and regeneration. Understanding COL4A5 and its recombinant form aids in identifying biomarkers for diagnosis and prognosis, paving the way for innovative therapeutic approaches to manage and treat associated disorders. This work underscores the significance of collagen biology in health and disease, contributing to the development of effective strategies for tackling collagen-related pathologies.











