Analytical Data
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Gene name
EDIL3
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简介
EDIL3 Protein enhances endothelial cell adhesion by interacting with the alpha-v/beta-3 integrin receptor, while also inhibiting the formation of vascular-like structures. Its role suggests involvement in the regulation of vascular morphogenesis during embryonic development. EDIL3 Protein, Human (HEK293, Fc) is the recombinant human-derived EDIL3 protein, expressed by HEK293, with C-hFc labeled tag.
- Application
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Alternative Names
EGF-Like Repeats and Discoidin I-Like Domains 3; EDIL3
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Species
Human
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Source
HEK293
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Tag
C-hFc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O43854-1
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Expression Region
D24-E480
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Molecular Weight
80-90 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
RIIB/ACVR2B, a dual receptor for activin and bone morphogenetic proteins, has garnered significant attention in recent years due to its pivotal role in muscle wasting and other degenerative conditions. Research has demonstrated that the inhibition of the RIIB/ACVR2B signaling pathway can lead to increased muscle mass and strength, making it a potential therapeutic target for conditions such as cachexia, muscular dystrophy, and age-related muscle loss. The development of recombinant proteins that modulate this pathway could revolutionize treatment strategies by promoting muscle regeneration and enhancing physical function in affected individuals. Several studies have focused on engineering these recombinant proteins to enhance their efficacy and specificity, aiming to develop biologics that can effectively block the action of RIIB/ACVR2B. This research is particularly timely as the global population ages and the prevalence of muscle-wasting diseases rises, highlighting the urgent need for innovative therapies. Understanding the structure and function of RIIB/ACVR2B and its role in muscle biology is critical for advancing clinical applications. In summary, RIIB/ACVR2B recombinant protein research represents a promising frontier in regenerative medicine, targeting muscle atrophy and improving the quality of life for patients suffering from debilitating muscular disorders.
