Analytical Data
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Gene name
COL1A1
- Application
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Alternative Names
COL1A1；Collagen alpha-1(I) 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
P02452
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Expression Region
334-389aa
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AA Sequence
PGPTGPAGPPGFPGAVGAKGEAGPQGPRGSEGPQGVRGEPGPPGPAGAAGPAGNPG
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Molecular Weight
33.8 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
Collagen type I alpha 1 (COL1A1) is a crucial gene that encodes the alpha-1 chain of type I collagen, which is the most abundant collagen in the human body and a major component of the extracellular matrix. Research on COL1A1 has gained significant attention due to its pivotal role in various physiological and pathological processes, including bone formation, wound healing, and tissue repair. Mutations or dysregulation of COL1A1 can lead to several genetic disorders, such as osteogenesis imperfecta, characterized by brittle bones, and other connective tissue diseases. The study of recombinant COL1A1 protein has emerged as a powerful tool in understanding collagen's structure-function relationships, developing therapeutics, and engineering biomaterials for tissue regeneration. By producing recombinant COL1A1 in various expression systems, researchers can investigate the protein's functional properties, interactions with other matrix components, and its role in cellular behavior. This research is not only critical for advancing our knowledge of collagen biology but also for developing innovative strategies for treating collagen-related disorders and improving regenerative medicine approaches. Therefore, COL1A1 protein research is integral to both basic science and clinical applications, making it a focal point in biomedical research.
