Analytical Data
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Gene name
EphB1
- Application
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Alternative Names
Ephrin Type-B Receptor 1; ELK; EPH Tyrosine Kinase 2; EPH-Like Kinase 6; EK6; hEK6; Neuronally-Expressed EPH; Related Tyrosine Kinase; NET; Tyrosine-Protein Kinase Receptor EPH-2; EPHB1; ELK; EPHT2; HEK6
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Species
Human
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Source
HEK293
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Tag
C- His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P54762
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Expression Region
564-984aa
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Protein Length
Partial
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Molecular Weight
48.8 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
EphB1, a member of the Eph receptor family, plays a crucial role in cell signaling, influencing numerous biological processes such as neuronal development, angiogenesis, and tissue organization. Its interactions with ephrin-B ligands are essential for mediating bidirectional signaling, promoting both normal physiological functions and potential pathophysiological conditions. Research on recombinantly expressed EphB1 protein has gained traction owing to its significance in various diseases, including cancer and neurological disorders. By producing EphB1 in a recombinant system, scientists can study its structure, function, and interactions in detail. This is vital for elucidating the specific signaling pathways and mechanisms underlying its role in cellular communication. Furthermore, understanding the functional characteristics of EphB1 can pave the way for the development of targeted therapeutics aimed at modulating EphB1 signaling in disease contexts. As ongoing studies refine our grasp of EphB1's biological functions, they also highlight its potential as a biomarker for disease progression and therapeutic targets, underscoring the importance of continued research into its recombinant expression and application in biomedical sciences.
