Cat: IPD-X22568

Recombinant Mouse Vitronectin Protein (HEK293),His

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Analytical Data

  • Gene name

    Vitronectin

  • 简介

    Vitronectin is a key cell adhesion factor in serum and tissues and plays a crucial role in cell interactions by binding to glycosaminoglycans and proteoglycans.It is recognized by specific integrins and serves as an important adhesion molecule, facilitating cell-matrix interactions.Vitronectin Protein, Mouse (HEK293, His) is the recombinant mouse-derived Vitronectin protein, expressed by HEK293 , with C-His labeled tag.

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Biological Activity

    1.Measured by the ability of the immobilized protein to support the adhesion of DU145 human prostate carcinoma cells. When cells are added to mouse Vitronectin coated plates (10 μg/mL and 100 μL/well), > 60% cells will adhere specifically after 30 minutes at 37°C. 2.Measured by the ability of the immobilized protein to support the adhesion of DU145 human prostate carcinoma cells. When cells are added to mouse Vitronectin coated plates (5 μg/mL and 100 μL/well), approximately is 79.89% adhered specifically after 30 minutes at 37°C.

  • Alternative Names

    Vitronectin; VN; S-Protein; Serum-Spreading Factor; V75; VTN

  • Species

    Mouse

  • Source

    HEK293

  • Tag

    C-10*His

  • Purity

    Greater than 95% as determined by SDS-PAGE.

  • Uniprot

    P29788

  • Expression Region

    D20-K478

  • AA Sequence

    DQESCKGRCTQGFMASKKCQCDELCTYYQSCCADYMEQCKPQVTRGDVFTMPEDDYWSYDYVEEPKNNTNTGVQPENTSPPGDLNPRTDGTLKPTAFLDPEEQPSTPAPKVEQQEEILRPDTTDQGTPEFPEEELCSGKPFDAFTDLKNGSLFAFRGQYCYELDETAVRPGYPKLIQDVWGIEGPIDAAFTRINCQGKTYLFKGSQYWRFEDGVLDPGYPRNISEGFSGIPDNVDAAFALPAHRYSGRERVYFFKGKQYWEYEFQQQPSQEECEGSSLSAVFEHFALLQRDSWENIFELLFWGRSSDGAREPQFISRNWHGVPGKVDAAMAGRIYVTGSLSHSAQAKKQKSKRRSRKRYRSRRGRGHRRSQSSNSRRSSRSIWFSLFSSEESGLGTYNNYDYDMDWLVPATCEPIQSVYFFSGDKYYRVNLRTRRVDSVNPPYPRSIAQYWLGCPTSEK

  • Protein Length

    Full Length of Mature Protein

  • Molecular Weight

    75-85 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

Vitronectin is a multifunctional glycoprotein found in the extracellular matrix and body fluids, playing a vital role in various biological processes, including cell adhesion, migration, and wound healing. It serves as a substrate for cell attachment and interacts with several integrin receptors, influencing cellular responses to the microenvironment. Due to its significant involvement in pathophysiological conditions such as cancer metastasis and cardiovascular diseases, vitronectin has garnered attention in biomedical research and therapeutic applications. The production of recombinant vitronectin protein has become essential for elucidating its structural and functional properties, enabling researchers to better understand the molecular mechanisms underlying its diverse biological activities. Advances in protein engineering techniques, such as recombinant DNA technology and expression systems, have facilitated the generation of high-purity vitronectin, which can be utilized in cell culture studies and in vitro assays. By systematically investigating the interactions between vitronectin and its binding partners, researchers aim to develop targeted therapies that manipulate these interactions to control cell behavior in disease contexts. Overall, the study of recombinant vitronectin not only deepens our understanding of its fundamental biological roles but also paves the way for innovative therapeutic strategies in regenerative medicine and cancer treatment.

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