Analytical Data
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Gene name
EPHA5
- Application
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Alternative Names
EHK-1; EK7; BSK; EHK1; HEK7; TYRO4; EphA5; Rek7; TYRO4HEK7CEK7
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Species
Cynomolgus
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Source
HEK293
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Tag
C-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
XP_005555256.1
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Expression Region
S56-P573
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Protein Length
Partial
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Molecular Weight
76 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
EPHA5, a member of the Eph receptor tyrosine kinase family, plays a crucial role in various biological processes, including cell adhesion, migration, and tissue development. Its involvement in neural development and synaptic plasticity has garnered significant interest in understanding neurodegenerative diseases and cancers. Abnormal expression of EPHA5 has been associated with various pathological conditions, including Alzheimer's disease and certain types of tumors, indicating its potential as a therapeutic target. The study of EPHA5 recombinant proteins allows researchers to investigate its structural and functional properties, providing insights into its signaling mechanisms and interactions with ephrin ligands. Additionally, reconstituting EPHA5 in vitro can facilitate the development of therapeutic strategies, such as monoclonal antibodies or small molecules aimed at modulating its activity. As the field of targeted therapies continues to evolve, exploring EPHA5's pathway could lead to breakthroughs in personalized medicine, paving the way for novel strategies in treating diseases linked to its dysfunction. Understanding EPHA5 through recombinant protein studies thus represents a pivotal step in elucidating its roles in health and disease.
