Analytical Data
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Gene name
Col26a1
- Application
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Alternative Names
Col26a1；EMID2；EMU2；Collagen alpha-1(XXVI) 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
Q96A83
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Expression Region
21-441aa
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AA Sequence
TGFLYPFSAA ALQQHGYPEP GAGSPGSGYA SRRHWCHHTV TRTVSCQVQN GSETVVQRVY QSCRWPGPCA NLVSYRTLIR PTYRVSYRTV TVLEWRCCPG FTGSNCDEEC MNCTRLSDMS ERLTTLEAKV LLLEAAERPS SPDNDLPAPE STPPTWNEDF LPDAIPLAHP VPRQRRPTGP AGPPGQTGPP GPAGPPGSKG DRGQTGEKGP AGPPGLLGPP GPRGLPGEMG RPGPPGPPGP AGNPGPSPNS PQGALYSLQP PTDKDNGDSR LASAIVDTVL AGVPGPRGPP GPPGPPGPRG PPGPPGTPGS QGLAGERGTV GPSGEPGVKG EEGEKAATAE GEGVQQLREA LKILAERVLI LEHMIGIHDP LASPEGGSGQ DAALRANLKM KRGGAQPDGV LAALLGPDPG QKSVDQASSR K
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Molecular Weight
45.3 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
Col26a1, or collagen type XXVI α1, is a novel member of the collagen family, which plays a crucial role in the extracellular matrix (ECM), particularly in connective tissues. Recent studies have highlighted its significance in various biological processes, including tissue development, repair, and maintenance. Unlike other collagens, Col26a1 exhibits unique structural properties and expression patterns, making it a potential biomarker for certain pathologies and a candidate for therapeutic applications. Research has indicated that Col26a1 may be involved in modulating cell behavior, influencing inflammation, and contributing to the mechanical properties of tissues. Understanding the molecular mechanisms governing Col26a1's function could provide insights into its role in diseases such as osteoarthritis, fibrosis, and certain genetic disorders. Therefore, the recombinant production of Col26a1 protein is critical for detailed biochemical and biophysical characterization, enabling the exploration of its functional roles. By leveraging advances in recombinant DNA technology, researchers aim to produce functional Col26a1 proteins for further investigation, paving the way for potential applications in regenerative medicine and therapeutic interventions. Overall, the study of Col26a1 and its recombinant form represents a promising avenue for understanding extracellular matrix dynamics and developing novel strategies for treating related diseases.
