Cat: IPD-X32676

Recombinant Mouse FAP Protein (HEK293),Avi & His

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Analytical Data

  • Gene name

    FAP

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    FAP; FAPalpha; SIMP; Seprase; APCE; DPPIV; DPPIVA; FAPA

  • Species

    Mouse

  • Source

    HEK293

  • Tag

    N-Avi;N-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P97321-1

  • Expression Region

    L26-D761

  • Molecular Weight

    92.6 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

FAP, or Fibroblast Activation Protein, is a type II transmembrane serine protease that plays a crucial role in the tumor microenvironment, particularly in cancer progression and metastasis. Initially identified for its expression in activated fibroblasts during tissue remodeling, FAP has garnered significant attention due to its preferential expression in various tumors, making it a promising target for cancer diagnostics and therapeutics. Research has demonstrated that FAP is involved in the degradation of extracellular matrix components, promoting tumor growth and invasion. Its unique expression pattern in the stroma of tumors, as opposed to normal tissues, highlights its potential as a biomarker for cancer imaging and an ideal target for antibody-drug conjugates. Recent studies have also suggested that FAP may contribute to immune modulation within the tumor microenvironment, influencing the efficacy of immunotherapies. Consequently, there is a growing interest in developing FAP-targeted therapies, including vaccines and novel targeted agents, to improve cancer treatment outcomes. As a result, the study of FAP and its associated proteins has become a vital area of research, aiming to uncover its roles in tumor biology and to devise innovative approaches for cancer diagnosis and treatment.

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