Analytical Data
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Gene name
EDF1
- Application
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Alternative Names
EDF1;Endothelial differentiation-related factor 1
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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
O60869
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Expression Region
2-148aa
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AA Sequence
AESDWDTVT VLRKKGPTAA QAKSKQAILA AQRRGEDVET SKKWAAGQNK QHSITKNTAK LDRETEELHH DRVTLEVGKV IQQGRQSKGL TQKDLATKIN EKPQVIADYE SGRAIPNNQV LGKIERAIGL KLRGKDIGKP IEKGPRAK
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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
EDF1, or Endothelial Differentiation Gene 1, is a critical protein involved in the regulation of endothelial cell function and vascular development. It plays a pivotal role in the differentiation and maintenance of endothelial cells, which line blood vessels and are essential for maintaining vascular homeostasis. Research has highlighted EDF1's involvement in various biological processes, including angiogenesis, inflammation, and the response to hypoxia. Aberrant expression or dysfunction of EDF1 has been linked to several diseases, including cardiovascular disorders and tumorigenesis. Consequently, understanding the structural and functional characteristics of EDF1 through recombinant protein studies is crucial for elucidating its role in endothelial biology and its potential as a therapeutic target. Advances in protein engineering and expression systems have enabled the production of significant quantities of recombinant EDF1, facilitating in-depth studies of its molecular pathways and interactions. This research not only contributes to our understanding of vascular biology but also opens avenues for innovative therapeutic strategies aimed at addressing disorders linked to endothelial dysfunction.
