Cat: IPD-X32993

Recombinant Mouse EphB1 Protein (HEK293),His

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Analytical Data

  • Gene name

    EphB1

  • 简介

    EphB1 protein is a receptor tyrosine kinase that participates in bidirectional signaling with ephrin B ligands (including EFNB1, EFNB2, and EFNB3). It plays a crucial role in retinal axon guidance, neural progenitor cell regulation, dendritic spine maturation, synapse formation, angiogenesis, targeted cell migration, and muscle stem cell maintenance. EphB1 Protein, Mouse (HEK293, His) is the recombinant mouse-derived EphB1 protein, expressed by HEK293 , with C-His labeled tag.

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Biological Activity

    Immobilized mouse EPHB1 10 μg/mL (100 μL/well) can bind mouse EFNB1, The ED50 for this effect is 128.3 ng/mL. Immobilized mouse EPHB1 10 μg/mL (100 μL/well) can bind mouse EFNB1, The ED50 for this effect is 128.3 ng/mL.

  • Alternative Names

    Ephrin type-B receptor 1; ELK; EK6; NET; EPHB1; EPHT2; HEK6

  • Species

    Mouse

  • Source

    HEK293

  • Tag

    C-His

  • Purity

    Greater than 95% as determined by SDS-PAGE.

  • Uniprot

    Q8CBF3-1

  • Expression Region

    M18-L539

  • AA Sequence

    MEETLMDTRTATAELGWTANPASGWEEVSGYDENLNTIRTYQVCNVFEPNQNNWLLTTFINRRGAHRIYTEMRFTVRDCSSLPNVPGSCKETFNLYYYETDSVIATKKSAFWSEAPYLKVDTIAADESFSQVDFGGRLMKVNTEVRSFGPLTRNGFYLAFQDYGACMSLLSVRVFFKKCPSIVQNFAVFPETMTGAESTSLVIARGTCIPNAEEVDVPIKLYCNGDGEWMVPIGRCTCKPGYEPENSVACKACPAGTFKASQEAEGCSHCPSNSRSPSEASPICTCRTGYYRADFDPPEVACTSVPSGPRNVISIVNETSIILEWHPPRETGGRDDVTYNIICKKCRADRRSCSRCDDNVEFVPRQLGLTECRVSISSLWAHTPYTFDIQAINGVSSKSPFPPQHVSVNITTNQAAPSTVPIMHQVSATMRSITLSWPQPEQPNGIILDYEIRYYEKEHNEFNSSMARSQTNTARIDGLRPGMVYVVQVRARTVAGYGKFSGKMCFQTLTDDDYKSELREQL

  • Protein Length

    Extracellular Domain

  • Molecular Weight

    65-75 kDa

  • Endotoxin

    < 1.0 EU per μg protein as determined by the LAL method.

  • Form

    Freeze-dried powder

  • Buffer formulation

    PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.

  • Reconstitution

    Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.

  • Customization

    Site-directed mutagenesis Custom tag design Custom buffer formulation Custom full-length protein production

  • 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.

  • 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.

  • 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.

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Protein Description

EphB1 is a member of the Eph receptor family, which encompasses a subclass of receptor tyrosine kinases known for their roles in mediating cell-cell interactions during developmental processes and tissue homeostasis. This receptor is particularly involved in pathways related to neuronal development, angiogenesis, and immune responses. Its interacting ephrin ligands, particularly ephrin-Bs, facilitate bidirectional signaling essential for various physiological functions. Aberrant EphB1 signaling has been implicated in multiple diseases, including cancer, where it may contribute to processes such as tumor progression and metastasis. Thus, understanding the structure and function of EphB1 has significant implications for therapeutic strategies. Research involving EphB1 recombinant protein has gained traction as it allows for the elucidation of its biological activities and molecular mechanisms. The production of EphB1 in a recombinant form enables detailed studies of its ligand interactions, signaling pathways, and potential as a target for drug development. Furthermore, the characterization of EphB1 through recombinant protein studies can shed light on its role in pathological conditions, opening avenues for innovative treatments based on modulation of EphB1 signaling. Given the complexity of its functions and the critical nature of its signaling in developmental and pathological contexts, continuous research on EphB1 remains vital for advancing our understanding of its contributions to health and disease.

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