Analytical Data
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Gene name
EphA4
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简介
The EphA4 protein is a receptor tyrosine kinase that participates in contact-dependent bidirectional signaling with ephrin A and ephrin B ligands. EphA4 is activated by GPI-anchored EFNA and transmembrane EFNB and regulates cell morphology, integrin-dependent adhesion, and GTPase activity. EphA4 Protein, Mouse (HEK293, His) is the recombinant mouse-derived EphA4 protein, expressed by HEK293 , with C-His labeled tag.
- Application
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Alternative Names
Sek; Sek1; EphA4; HEK8; SEK; TYRO1; EK8
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Species
Mouse
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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
Q03137-1
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Expression Region
V20-T547
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Protein Length
Extracellular Domain
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Molecular Weight
65-80 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
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Protein Description
EphA4, a member of the Eph receptor tyrosine kinase family, plays a critical role in various physiological and pathological processes, including neuronal development, tissue morphogenesis, and cancer progression. Its function is primarily mediated through interactions with ephrin ligands, which guide cell signaling pathways that influence cell movement, adhesion, and shape. Dysregulation of EphA4 has been implicated in several diseases, particularly in the context of tumors and neurodegenerative disorders. Research on EphA4 recombinant proteins has gained momentum due to the potential therapeutic applications, including targeting cancers and modulating neurodevelopmental processes. By generating and characterizing EphA4 recombinant proteins, researchers aim to elucidate its precise mechanisms of action and explore its interactions with ephrin ligands and downstream signaling molecules. This understanding could lead to novel strategies for treating diseases associated with EphA4 dysregulation, highlighting the importance of these proteins in the development of targeted therapies. Overall, the study of EphA4 recombinant proteins is essential for advancing our knowledge of cell signaling and developing innovative treatments for various medical conditions.
