Cat: IPD-X32013

Recombinant Rat Coagulation Factor XII/F12 Protein,His & SUMO

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Analytical Data

  • Gene name

    Coagulation Factor XII/F12

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    FXII; HAF; Contact Factor; Hageman Factor

  • Species

    Rat

  • Source

    E. coli

  • Tag

    Two N- s, His- & SUMO-

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    A0A0H2UI19

  • Expression Region

    Val354~Phe595

  • Molecular Weight

    40kDa

  • 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

Coagulation Factor XII (F12) is a crucial protein in the blood coagulation cascade, playing a significant role in initiating both the intrinsic pathway of coagulation and the fibrinolytic system. Its activation can lead to thrombosis; however, it also has implications in inflammation, wound healing, and host defense. Research into recombinant forms of Factor XII has gained traction due to the potential for therapeutic applications in managing bleeding disorders and thrombotic diseases. Recombinant Factor XII could offer advantages over plasma-derived products, such as reduced risk of pathogen transmission, consistent quality, and the ability to modify its properties for enhanced efficacy. Studies have also demonstrated that modulating Factor XII activity might offer a novel approach for treating hypercoagulable states without affecting hemostasis, thereby presenting an opportunity to develop targeted therapies. Understanding the structure-function relationship of Factor XII through recombinant protein studies can provide insights into its mechanisms of action and pave the way for innovative treatments in coagulation disorders. As research advances, the therapeutic potential of recombinant Factor XII continues to be explored, highlighting the importance of this protein in both basic and applied biomedical research.


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