Analytical Data
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Gene name
ECF
- Application
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Alternative Names
ECF；Chi3l3；Ym1；Chitinase-like Protein 3
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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
Q9BZP6
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Expression Region
1-368aa
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AA Sequence
MVSTPENRQTFITSVIKFLRQYEFDGLDFDWEYPGSRGSPPQDKHLFTVLVQEMREAFEQEAKQINKPRLMVTAAVAAGISNIQSGYEIPQLSQYLDYIHVMTYDLHGSWEGYTGENSPLYKYPTDTGSNAYLNVDYVMNYWKDNGAPAEKLIVGFPTYGHNFILSNPSNTGIGAPTSGAGPAGPYAKESGIWAYYEICTFLKNGATQGWDAPQEVPYAYQGNVWVGYDNIKSFDIKAQWLKHNKFGGAMVWAIDLDDFTGTFCNQGKFPLISTLKKALGLQSASCTAPAQPIEPITAAPSGSGNGSGSSSSGGSSGGSGFCAVRANGLYPVANNRNAFWHCVNGVTYQQNCQAGLVFDTSCDCCNWA
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Molecular Weight
67.1kDa
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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
The study of ECF (Epsilon-Crystallin-Fibrinogen) recombinant proteins has gained significant attention in the field of molecular biology and biotechnology due to their unique structural and functional properties. ECF proteins are derived from a variety of sources, including bacteria and eukaryotic organisms, and exhibit a range of applications in therapeutics and diagnostics. The recombinant expression of ECF proteins allows for the production of large quantities of these proteins with high purity, facilitating comprehensive studies on their biochemical properties and potential medical applications. Research has shown that ECF proteins possess distinct characteristics, such as stability and specificity, making them ideal candidates for use in drug development and as biomolecular tools in research. The ability to engineer these proteins through recombinant DNA technology enhances their functionality and improves their interaction with other biomolecules. As scientists continue to explore the potential of ECF recombinant proteins, the implications for understanding disease mechanisms and developing novel therapeutic strategies become increasingly promising, positioning ECF proteins at the forefront of biotechnological innovations.
