Analytical Data
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Gene name
EPHB3
- Application
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Alternative Names
EPHB3；ETK2；HEK2；TYRO6；Ephrin type-B receptor 3
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P54753
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Expression Region
585-998aa
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AA Sequence
QRHGSDSEYTEKLQQYIAPGMKVYIDPFTYEDPNEAVREFAKEIDVSCVKIEEVIGAGEFGEVCRGRLKQPGRREVFVAIKTLKVGYTERQRRDFLSEASIMGQFDHPNIIRLEGVVTKSRPVMILTEFMENCALDSFLRLNDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRFLEDDPSDPTYTSSLGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDVINAVEQDYRLPPPMDCPTALHQLMLDCWVRDRNLRPKFSQIVNTLDKLIRNAASLKVIASAQSGMSQPLLDRTVPDYTTFTTVGDWLDAIKMGRYKESFVSAGFASFDLVAQMTAEDLLRIGVTLAGHQKKILSSIQDMRLQMNQTLPVQV
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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, or Ephrin type-B receptor 3, is a member of the Eph receptor tyrosine kinase family, known for its critical roles in developmental processes, cell migration, and axon guidance. Research on EPHB3 has gained momentum due to its implications in various physiological and pathological contexts, including neural development, angiogenesis, and cancer. Dysregulation of EPHB3 has been associated with several types of cancer, where it may influence tumor progression and metastasis. The study of recombinant EPHB3 proteins is crucial for understanding its structure-function relationship and the molecular mechanisms underlying its interactions with ephrin ligands. By producing and characterizing EPHB3 recombinant proteins, researchers aim to investigate its binding affinities, downstream signaling pathways, and potential as a therapeutic target. These studies can unveil how EPHB3 alters cellular behavior and contribute to the development of innovative strategies for cancer treatment and regenerative medicine. Overall, the exploration of EPHB3 recombinant protein promises to provide significant insights into its biological roles and therapeutic potentials.
