Cat: IPD-X32985

Recombinant Rat EphA7 Protein (HEK293),His

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Analytical Data

  • Gene name

    EphA7

  • 简介

    The EphA7 protein is a receptor tyrosine kinase that participates in bidirectional signaling with GPI-anchored ephrin A ligands (such as EFNA5). It affects brain development by regulating cell-cell adhesion and repulsion. EphA7 Protein, Rat (HEK293, His) is the recombinant rat-derived EphA7 protein, expressed by HEK293 , with C-His labeled tag.

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Biological Activity

    Measured by its binding ability in a functional ELISA. When Recombinant Rat EphA7 is immobilized at 10 µg/mL (100 µL/well) can bind Biotinylated Recombinant mouse Ephrin-A4. The ED50 for this effect is 212.3 ng/mL. Measured by its binding ability in a functional ELISA. When Recombinant Rat EphA7 is immobilized at 10 µg/mL (100 µL/well) can bind Biotinylated Recombinant mouse Ephrin-A4. The ED50 for this effect is 212.3ng/mL.

  • Alternative Names

    Ephrin Type-A Receptor 7; EPH Homology Kinase 3; EHK-3; EPH-Like Kinase 11; EK11; EPHA7; HEK11

  • Species

    Rat

  • Source

    HEK293

  • Tag

    C-His

  • Purity

    Greater than 95% as determined by SDS-PAGE.

  • Uniprot

    P54759-1

  • Expression Region

    Q28-S539

  • AA Sequence

    QAAKEVLLLDSKAQQTELEWISSPPSGWEEISGLDENYTPIRTYQVCQVMEPNQNNWLRTNWISKGNAQRIFVELKFTLRDCNSLPGVLGTCKETFNLYYYETDYDTGRNIRENLYVKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSKKGFYLAFQDVGACIALVSVKVYYKKCWSIIENLAVFPDTVTGSEFSSLVEVRGTCVSSAEEEAENSPRMHCSAEGEWLVPIGKCICKAGYQQKGDTCEPCGRRFYKSSSQDLQCSRCPTHSFSDREGSSRCECEDGYYRAPSDPPYVACTRPPSAPQNLIFNINQTTVSLEWSPPADNGGRNDVTYRILCKRCSWEQGECVPCGSNIGYMPQQTGLEDNYVTVMDLLAHANYTFEVEAVNGVSDLSRSQRLFAAVSITTGQAAPSQVSGVMKERVLQRSVELSWQEPEHPNGVITEYEIKYYEKDQRERTYSTLKTKSTSASINNLKPGTVYVFQIRAFTAAGYGNYSPRLDVATLEEAS

  • Protein Length

    Partial

  • Molecular Weight

    65-72 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

EphA7 is a member of the Eph receptor tyrosine kinase family, which plays a crucial role in various biological processes, including cell adhesion, migration, and tissue development. This receptor is particularly important in the nervous system, where it mediates axon guidance and neuronal patterning. Aberrant EphA7 signaling has been implicated in several neurological disorders and cancers, making it a potential therapeutic target. The study of recombinant EphA7 proteins allows researchers to investigate their structural and functional properties, providing insights into receptor activation mechanisms and interactions with ligands, specifically ephrin-A family members. By producing EphA7 as a recombinant protein, researchers can explore its binding affinity and signaling pathways in a controlled environment, enhancing our understanding of its role in cellular processes and disease states. These studies have significant implications for developing targeted therapies that modulate EphA7 activity, offering new avenues for treating conditions linked to its dysregulation. Overall, the research on EphA7 recombinant proteins is vital for elucidating the complexities of cell signaling and for advancing therapeutic strategies in regenerative medicine and oncology.

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