Cat: IPD-X33022

Recombinant Human EphB4 Protein (Baculovirus),His & GST

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Analytical Data

  • Gene name

    EphB4

  • 简介

    EphB4 protein is a receptor tyrosine kinase that binds to ephrin B ligand and initiates bidirectional signaling. Positive signaling regulates the rejection and separation of cells from EFNB2-expressing cells. EphB4 Protein, Human (sf9, His-GST) is the recombinant human-derived EphB4 protein, expressed by Sf9 insect cells , with N-His, N-GST labeled tag.

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Ephrin type-B receptor 4; EPHB4; HTK; MYK1; TYRO11

  • Species

    Human

  • Source

    Baculovirus

  • Tag

    N-His;N-GST

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P54760-1

  • Expression Region

    L563-Y987

  • AA Sequence

    LRKQSNGREAEYSDKHGQYLIGHGTKVYIDPFTYEDPNEAVREFAKEIDVSYVKIEEVIGAGEFGEVCRGRLKAPGKKESCVAIKTLKGGYTERQRREFLSEASIMGQFEHPNIIRLEGVVTNSMPVMILTEFMENGALDSFLRLNDGQFTVIQLVGMLRGIASGMRYLAEMSYVHRDLAARNILVNSNLVCKVSDFGLSRFLEENSSDPTYTSSLGGKIPIRWTAPEAIAFRKFTSASDAWSYGIVMWEVMSFGERPYWDMSNQDVINAIEQDYRLPPPPDCPTSLHQLMLDCWQKDRNARPRFPQVVSALDKMIRNPASLKIVARENGGASHPLLDQRQPHYSAFGSVGEWLRAIKMGRYEESFAAAGFGSFELVSQISAEDLLRIGVTLAGHQKKILASVQHMKSQAKPGTPGGTGGPAPQY

  • Protein Length

    Cytoplasmic 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

EphB4 is a member of the Eph receptor tyrosine kinase family, which plays a critical role in developmental processes, cell migration, and the formation of various tissues. It interacts with its ligands, ephrin-B1 and ephrin-B2, to mediate bidirectional signaling pathways that influence cell positioning and communication during embryogenesis and in mature tissues. Research has indicated that EphB4 is implicated in several pathological conditions, including cancer metastasis, vascular formation, and neurological disorders. The overexpression or dysregulation of EphB4 in various cancers has drawn attention to its potential as a therapeutic target. Consequently, recombinant EphB4 protein has become a focus of study for understanding its functional mechanisms and interactions. By producing EphB4 in a recombinant form, researchers are able to investigate its role in cell signaling, elucidate its implications in disease, and explore its utility in therapeutic interventions. Studies utilizing the recombinant protein have provided insights into the modulation of tumor growth and angiogenesis, suggesting that targeting EphB4 signaling pathways may offer novel strategies for cancer treatment and tissue regeneration. As such, the investigation of EphB4 and its recombinant counterparts is significant for both fundamental biological research and the development of future therapeutic approaches.

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