Analytical Data
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Gene name
EDN2
- Application
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Alternative Names
EDN2;Endothelin-2
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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
P20800
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Expression Region
25-178aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSQAAATLE QPASSSHAQG THLRLRRCSC SSWLDKECVY FCHLDIIWVN TPEQTAPYGL GNPPRRRRRS LPRRCQCSSA RDPACATFCL RRPWTEAGAV PSRKSPADVF QTGKTGATTG ELLQRLRDIS TVKSLFAKRQ QEAMREPRST HSRWRKR
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Molecular Weight
20 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
EDN2, or Endothelin-2, is a member of the endothelin family of peptides, which are known to play crucial roles in various physiological and pathological processes, including vascular tone regulation, smooth muscle contraction, and cell proliferation. The interest in EDN2 has surged due to its implications in cardiovascular diseases, pulmonary conditions, and developmental biology. Unlike the other endothelins, EDN2 exhibits distinct expression patterns and biological activities, warranting focused research to elucidate its specific roles. Advances in recombinant protein technology have allowed for the production of EDN2 in heterologous systems, providing an opportunity to study its structure-function relationship in detail. Understanding EDN2’s signaling mechanisms can unveil potential therapeutic targets for diseases where endothelin pathways are dysregulated. Furthermore, the exploration of EDN2's interactions with its receptors and other biological molecules is crucial for developing targeted interventions. Overall, the study of EDN2 recombinant protein not only enhances our understanding of endothelin biology but also holds promise for clinical applications in treating various disorders associated with endothelin signaling dysregulation.
