Analytical Data
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Gene name
EDIL3
- Application
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Alternative Names
EDIL3；DEL1；EGF-like repeat and discoidin I-like domain-containing 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
O43854-2
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Expression Region
16-470aa
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AA Sequence
GVPQFGKGDI CDPNPCENGG ICLPGLADGS FSCECPDGFT DPNCSSVVEV GPCTPNPCHN GGTCEISEAY RGDTFIGYVC KCPRGFNGIH CQHNINECEV EPCKNGGICT DLVANYSCEC PGEFMGRNCQ YKCSGPLGIE GGIISNQQIT ASSTHRALFG LQKWYPYYAR LNKKGLINAW TAAENDRWPW IQINLQRKMR VTGVITQGAK RIGSPEYIKS YKIAYSNDGK TWAMYKVKGT NEDMVFRGNI DNNTPYANSF TPPIKAQYVR LYPQVCRRHC TLRMELLGCE LSGCSEPLGM KSGHIQDYQI TASSIFRTLN MDMFTWEPRK ARLDKQGKVN AWTSGHNDQS QWLQVDLLVP TKVTGIITQG AKDFGHVQFV GSYKLAYSND GEHWTVYQDE KQRKDKVFQG NFDNDTHRKN VIDPPIYARH IRILPWSWYG RITLRSELLG CTEEE
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Molecular Weight
52 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
EDIL3 (Egf-like-domain 3) is a protein that belongs to the EGF-like domain-containing protein family, which plays a significant role in various biological processes, including cell adhesion, migration, and proliferation. It has been implicated in several physiological and pathological conditions, such as tumorigenesis, angiogenesis, and wound healing. The interest in EDIL3 has grown due to its potential as a biomarker for certain cancers and its involvement in the regulation of the inflammatory response. In recent years, studies have focused on the recombinant production of EDIL3 to elucidate its structure-function relationship and to investigate its biological activities in vitro and in vivo. This recombinant protein can provide a valuable tool for understanding the molecular mechanisms underlying its role in disease, as well as for assessing its therapeutic potential. Researchers are employing various expression systems, including bacteria, yeast, and mammalian cells, to produce functional EDIL3, which allows for detailed studies into its interaction with specific receptors and other cellular components. Such investigations may pave the way for novel therapeutic strategies that target EDIL3's pathways in disease contexts, ultimately contributing to improved patient outcomes in cancer and other related conditions.
