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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Protein Length
Partial
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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 pivotal role in mediating cell adhesion, communication, and migration during developmental processes and tissue homeostasis. Its functions are primarily dictated by interactions with ephrin ligands, which are membrane-bound proteins expressing bidirectional signaling capabilities. Dysregulation of EphA1 has been implicated in various pathological conditions, including cancer metastasis, neurodegenerative diseases, and cardiovascular disorders, underscoring its potential as a therapeutic target. The study of EphA1 recombinant proteins allows for a detailed exploration of its molecular mechanisms, interactions, and signaling pathways. Moreover, recombinant EphA1 can facilitate the development of assays for screening small molecules or antibodies that modulate its function. This research holds significant promise in understanding how EphA1 contributes to cellular dynamics and establishing strategies for the design of targeted therapies to combat diseases associated with its dysfunction. As such, investigating EphA1 through recombinant protein approaches could lead to innovative insights in both basic and clinical research, paving the way for advancements in precision medicine.
