Analytical Data
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Gene name
EphB2
- Application
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Alternative Names
CAPB; DRT; EPHT3; ERK; Hek5; PCBC; Tyro5; Developmentally-regulated Eph-related tyrosine kinase; ELK-related tyrosine kinase; EPH-like kinase 5; EPH tyrosine kinase 3
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Species
Human
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Source
E. coli
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Tag
Two N- s, His- & SUMO-
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P29323
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Expression Region
Val19~Leu543
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Protein Length
Partial
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Molecular Weight
70kDa
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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
EphB2 is a member of the Eph receptor tyrosine kinase family, which plays a crucial role in various biological processes, including cell signaling, tissue development, and neural network formation. Dysregulation of EphB2 has been implicated in several pathological conditions, particularly in cancer, where it can influence tumor growth, metastasis, and the tumor microenvironment. This makes EphB2 a compelling target for therapeutic interventions. Research on recombinant EphB2 proteins has gained traction as a means of understanding the precise mechanisms by which EphB2 interacts with its ligands, primarily ephrins, and mediates cellular responses. By studying the structure and functional characteristics of EphB2 in a recombinant form, scientists can elucidate the signaling pathways involved and identify potential biomarkers for cancer diagnosis and prognosis. Furthermore, the production of recombinant EphB2 offers opportunities for drug design and targeted therapies that could modulate its activity, providing avenues for innovative cancer treatments. Understanding the EPHB2-ephrins interaction at the molecular level may also lead to insights into more complex physiological processes, including angiogenesis and neurogenesis, thereby expanding the significance of this receptor beyond oncology. Overall, the ongoing research on recombinant EphB2 proteins not only enhances our foundational knowledge of cellular communication but also holds promise for the development of novel therapeutic strategies against cancer and other diseases associated with EphB2 dysfunction.
