Cat: IPD-X12462

Recombinant Human Ephrin-B1/EFNB1 Protein(HEK293), C-hFc

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Analytical Data

  • Gene name

    Ephrin-B1/EFNB1

  • 简介

    Ephrin-B1/EFNB1 Protein, a type I membrane protein, acts as a ligand for Eph-related receptor tyrosine kinases, potentially influencing cell adhesion and contributing to nervous system development. With ubiquitous expression, it is notably present in fat, placenta, and various tissues, showcasing its broad impact on diverse cellular and physiological contexts. Ephrin-B1/EFNB1 Protein, Human (HEK293, C-hFc) is the recombinant human-derived Ephrin-B1/EFNB1 protein, expressed by HEK293 , with C-hFc labeled tag.

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Biological Activity

    Measured in a cell proliferation assay using HUVEC cells. The ED50 this effect is 2.876 ng/mL, corresponding to a specific activity is 3.4771×10^5 units/mg. Measured in a cell proliferation assay using HUVEC cells. The ED50 this effect is 2.876 ng/mL, corresponding to a specific activity is 3.4771×105 units/mg.

  • Alternative Names

    Ephrin-B1; EFL-3; ELK-L; LERK-2; Ephrin-B1 CTF; EFNB1; EFL3; EPLG2; LERK2

  • Species

    Human

  • Source

    HEK293

  • Tag

    C-hFc

  • Purity

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

  • Uniprot

    NP_004420.1

  • Expression Region

    L28-K237

  • AA Sequence

    LAKNLEPVSWSSLNPKFLSGKGLVIYPKIGDKLDIICPRAEAGRPYEYYKLYLVRPEQAAACSTVLDPNVLVTCNRPEQEIRFTIKFQEFSPNYMGLEFKKHHDYYITSTSNGSLEGLENREGGVCRTRTMKIIMKVGQDPNAVTPEQLTTSRPSKEADNTVKMATQAPGSRGSLGDSDGKHETVNQEEKSGPGASGGSSGDPDGFFNSK

  • Protein Length

    Partial

  • Molecular Weight

    58.76 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

Ephrin-B1, encoded by the EFNB1 gene, is a member of the ephrin family, which plays a critical role in various biological processes, including neuronal development, angiogenesis, and cell adhesion. Research on Ephrin-B1 has gained momentum due to its involvement in cell signaling pathways mediated by Eph receptors, particularly in the context of developmental biology and cancer. The Ephrin-B1/Eph receptor interaction is crucial for bidirectional signaling, influencing cellular responses and tissue organization. Aberrant expression or mutations in EFNB1 have been linked to several pathological conditions, including tumors and neurological disorders. The study of recombinant Ephrin-B1 proteins allows for detailed exploration of their functional roles and mechanisms. By producing these proteins in a laboratory setting, researchers aim to investigate how Ephrin-B1 mediates cellular communication and promotes various biological responses. This understanding could uncover potential therapeutic targets for diseases where Ephrin-B1 signaling is disrupted, ultimately contributing to advances in treatment strategies for related health issues. The development and characterization of Ephrin-B1 recombinant proteins offer valuable insights into their structure-function relationships, potentially paving the way for novel interventions in regenerative medicine and oncology.

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