Analytical Data
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Gene name
Col26a1
- Application
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Alternative Names
Alpha-1 type XXVI collagen (EMI domain-containing protein 2) (Emilin and multimerin domain-containing protein 2) (Emu) (Col26a) (Emid2) (Emu2)
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Species
Mouse
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Source
Baculovirus
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q91VF6
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Expression Region
21-440aa
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Molecular Weight
47.7 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
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Protein Description
Collagen type XXVI alpha 1 (Col26a1) is a member of the collagen family known for its unique structure and role in various biological processes. Its importance lies mainly in its involvement in the extracellular matrix (ECM), where it contributes to tissue integrity, cellular signaling, and the modulation of mechanical properties in connective tissues. Recent studies have indicated that Col26a1 plays a critical role in developmental processes, particularly in the formation of the inner ear and in the maintenance of tissue homeostasis. Furthermore, aberrations in Col26a1 expression have been linked to several pathological conditions, including auditory dysfunction and musculoskeletal disorders. The recombinant production of Col26a1 protein offers a promising avenue for more in-depth functional studies and potential therapeutic applications. By utilizing recombinant DNA technology, researchers can produce this collagen type in sufficient quantities for biochemical characterization, structure-function analyses, and the exploration of its interactions with other matrix components. Understanding the molecular mechanisms governed by Col26a1 may shed light on its role in health and disease, paving the way for innovative strategies in regenerative medicine and tissue engineering. The study of Col26a1 recombinant proteins thus represents a significant step toward elucidating its biological functions and therapeutic potential.
