Analytical Data
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Gene name
EGFL6
- Application
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Alternative Names
MAEG; MAM And EGF Domain Containing; Epidermal growth factor-like protein 6
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8IUX8
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Expression Region
Asn22~Asp553
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Molecular Weight
63kDa
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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.
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Protein Description
EGFL6 (Epidermal Growth Factor-Like 6) is a protein that plays a critical role in various biological processes, including cell proliferation, differentiation, and tissue repair. It belongs to the epidermal growth factor (EGF) family and is characterized by the presence of EGF-like domains, which are known to interact with multiple receptors and signaling pathways. Research indicates that EGFL6 is involved in embryonic development and has been implicated in cancer biology, where its expression levels can influence tumor growth and metastasis. The study of recombinant EGFL6 protein has gained attention due to its potential therapeutic applications, particularly in regenerative medicine and oncology. By understanding the structure-function relationship of EGFL6, researchers aim to develop novel strategies for targeting EGFL6-mediated pathways, potentially leading to new treatments for cancer and degenerative diseases. Furthermore, the production of recombinant EGFL6 allows for functional assays and the exploration of its interactions with specific receptors, contributing to the broader knowledge of EGF-like proteins in health and disease. The ongoing studies on EGFL6 not only expand our understanding of its biological significance but also open avenues for innovative therapeutic interventions.











