Cat: IPD-X12577

Recombinant Mouse EphB6 Protein(HEK293), C-His

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Analytical Data

  • Gene name

    EphB6

  • 简介

    EphB6 Protein, a kinase-defective receptor, binds ephrin-B1 and ephrin-B2, influencing cell adhesion and migration with nuanced effects. Its interaction with ephrin-B2 inhibits JNK activation, T-cell receptor-induced IL-2 secretion, and CD25 expression. EphB6 also interacts with CBL, EPHB1, and ligand-independently with FYN, highlighting its intricate role in cellular signaling pathways. EphB6 Protein, Mouse (HEK293, His) is the recombinant mouse-derived EphB6 protein, expressed by HEK293 , with C-His labeled tag.

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Biological Activity

    Measured by its binding ability in a functional ELISA. Immobilized Mouse EphB6 at 10 μg/mL (100 μL/well) can bind Mouse EFNB1. The ED50 for this effect is 0.3034 μg/mL. Measured by its binding ability in a functional ELISA. Immobilized Mouse EphB6 at 10 μg/mL (100 μL/well) can bind Mouse EFNB1. The ED50 for this effect is 0.3034 μg/mL.

  • Alternative Names

    Ephrin type-B receptor 6; HEP; Tyrosine-protein kinase-defective receptor EPH-6; EPHB9

  • Species

    Mouse

  • Source

    HEK293

  • Tag

    C-His

  • Purity

    Greater than 95% as determined by reducing SDS-PAGE.

  • Uniprot

    O08644

  • Expression Region

    L33-S587

  • AA Sequence

    LEEVLLDTTGETSEIGWLTYPPGGWDEVSVLDDQRRLTRTFEACHVAGLPPGSGQDNWLQTHFVERRGAQRAHIRLHFSVRACSSLGVSGGTCRETFTLYYRQADEPDGPDSIAAWHLKRWTKVDTIAADESFPASSSSSSWAVGPHRTGQRVGLQLNVKERSFGPLTQRGFYVAFQDTGACLALVAVKLFSYTCPSVLRAFASFPETQASGAGGASLVAAVGTCVAHAEPEEDGVGGQAGGSPPRLHCNGEGRWMVAVGGCRCQPGHQPARGDKLCQACPEGSYKALAGNVPCSPCPARSHSPDPAAPVCPCLQGFYRASSDPPEAPCTGPPSAPRELWFEVQGSALMLHWRLPQELGGRGDLLFNVVCKECGGHGEPSSGGMCRRCRDEVHFDPRQRGLTESRVLVGGLRAHVPYILEVQAVNGVSELSPDPPQAAAINVSTSHEVPSAVPVMHQVSRAANSITVSWPQPEQTNGNILDYQLRYYDQAEDESHSFTMTSETNTATVTRLSPGHIYGFQVRARTAAGHGPYGGKVYFQTLPQGELSSQLPEKLS

  • Protein Length

    Extracellular Domain

  • Molecular Weight

    66 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.

Quality inspection process

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Protein Description

EphB6 is a member of the Eph receptor family, which plays a crucial role in various cellular processes, including cell migration, adhesion, and differentiation. Unlike other Eph receptors that are known to interact with ephrin ligands to mediate cellular signaling, EphB6 is considered a "decoy" receptor. It lacks a functional kinase domain and has been implicated in the negative regulation of signaling pathways initiated by other Eph receptors. The study of EphB6, particularly in the context of its recombinant protein form, has gained interest due to its potential roles in cancer biology and neurodevelopmental processes. Research has shown that altered expression of EphB6 is associated with several malignancies, suggesting its function as a tumor suppressor in some contexts. Furthermore, EphB6's interaction with various ligands and its impact on cell behavior could provide insights into mechanisms underlying diseases characterized by aberrant cell growth and motility. Investigating EphB6 recombinant proteins can also facilitate the development of therapeutic strategies aimed at modulating its signaling pathways. Understanding the structural and functional properties of EphB6 is essential for elucidating its role in health and disease, making it a promising target for future biomedical research.

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