Analytical Data
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Gene name
COL12A1
- Application
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Alternative Names
COL12A1；COL12A1L；Collagen alpha-1(XII) 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
Q99715
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Expression Region
140-316aa
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AA Sequence
DLVFLVDGSWSVGRNNFKYILDFIAALVSAFDIGEEKTRVGVVQYSSDTRTEFNLNQYYQRDELLAAIKKIPYKGGNTMTGDAIDYLVKNTFTESAGARVGFPKVAIIITDGKSQDEVEIPARELRNVGVEVFSLGIKAADAKELKQIASTPSLNHVFNVANFDAIVDIQNEIISQV
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Molecular Weight
23.5 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
COL12A1, a member of the collagen family, encodes a protein that plays a crucial role in the structural integrity of various tissues, particularly in the extracellular matrix. Research has shown that COL12A1 is involved in tissue repair and regeneration, making it a significant focus in studies related to fibrosis, wound healing, and musculoskeletal disorders. Its unique structure, characterized by the presence of multiple collagenous domains, allows it to interact with other matrix components, influencing cellular behaviors such as adhesion, migration, and differentiation. Abnormal expression or mutations in COL12A1 have been linked to various pathological conditions, including skeletal dysplasia and other connective tissue disorders. Consequently, the recombinant production of COL12A1 protein has garnered attention for potential therapeutic applications, including its use in tissue engineering and regenerative medicine. Understanding the functional characteristics and molecular mechanisms of COL12A1 through recombinant techniques could pave the way for novel treatments and enhance our knowledge of collagen-related diseases. This research aims to elucidate the biological roles of COL12A1 and explore its potential in clinical applications, thereby contributing to advancements in regenerative therapies and improving patient outcomes.
