Analytical Data
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Gene name
EphA1
- Application
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Alternative Names
EPH; EPHT; EPHT1; EPH Receptor A1; EPH tyrosine kinase 1; Erythropoietin-producing hepatoma receptor; Tyrosine-protein kinase receptor EPH
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Species
Mouse
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
Q60750
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Expression Region
Lys716~Thr960
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Molecular Weight
31kDa
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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
EphA1, a member of the Eph receptor tyrosine kinase family, plays a crucial role in various biological processes, including cellular signaling, development, and tissue organization. Its involvement in axon guidance and angiogenesis highlights its importance in the nervous system and vascular development. Recently, research has shown that EphA1 is implicated in several pathological conditions, including cancer and neurodegenerative diseases, where it may contribute to tumor progression and neuronal degeneration. The study of recombinant EphA1 proteins has gained momentum as scientists seek to understand the molecular mechanisms underlying its functions and interactions. By producing EphA1 in a recombinant form, researchers can investigate its receptor-ligand interactions, signaling pathways, and potential as a therapeutic target. Additionally, recombinant EphA1 proteins facilitate the exploration of its structural biology, aiding in the identification of binding domains and functional sites critical for its activity. Through these investigations, insights into the specific roles of EphA1 in health and disease can be gained, potentially leading to novel therapeutic strategies and the development of EphA1-targeted interventions in cancer and other disorders.
