Analytical Data
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Gene name
EphB3
- Application
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Alternative Names
ETK2; HEK2; TYRO6; EPH-like tyrosine kinase 2; Embryonic kinase 2; Tyrosine-protein kinase TYRO6
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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
P54754
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Expression Region
Val628~Ile891
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Molecular Weight
34kDa
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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
EphB3, a member of the Eph receptor tyrosine kinase family, plays a crucial role in various physiological and pathological processes, particularly in cell-cell interactions and neuronal development. It is involved in the regulation of cell migration, axon guidance, and synaptic plasticity, making it essential for normal brain function and development. Research has shown that EphB3 is implicated in several diseases, including cancer, where its expression can influence tumor progression and metastasis. The interest in recombinant EphB3 proteins has surged, as they serve as valuable tools for understanding the receptor's signaling pathways and interactions. By studying EphB3 in a recombinant form, researchers can elucidate its structure-function relationships, identify potential binding partners, and uncover its role in disease mechanisms. Additionally, recombinant EphB3 can be utilized in therapeutic applications, including targeted cancer therapies, by modulating its activity or blocking its interactions. This research is critical in paving the way for novel treatment strategies aimed at conditions linked to EphB3 dysregulation. Overall, the investigation of EphB3 recombinant proteins is a rapidly evolving field that promises to enhance our understanding of cell signaling and open new avenues for therapeutic intervention.
