Cat: IPD-X38473

Recombinant Human GMFb Protein,His

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Analytical Data

  • Gene name

    GMFb

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    GMFB; GMF-B

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P60983

  • Expression Region

    Ser2~His142

  • Molecular Weight

    20kDa

  • 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

GMFb (Guanine nucleotide exchange factor for the Rho family of GTPases) is a critical protein implicated in various cellular processes, including cytoskeletal dynamics, cell migration, and signaling pathways. The research surrounding GMFb has gained considerable attention due to its potential roles in development and disease. Specifically, studies have revealed that GMFb influences Rho family GTPases, which are essential regulators of actin cytoskeleton organization. Dysregulation of GMFb has been linked to several pathological conditions, including cancer, where altered cell motility and invasion are critical features. The protein's ability to modulate cellular responses to extracellular signals underscores its significance in both normal physiology and disease progression. Recent advances in molecular biology techniques have facilitated the exploration of GMFb’s structure, function, and interaction networks, offering insights into its mechanisms of action. Furthermore, understanding GMFb's role in cellular signaling pathways presents opportunities for targeted therapeutic interventions in diseases characterized by aberrant cell behavior. As a result, ongoing research efforts aim to elucidate the precise functions of GMFb, the regulatory mechanisms governing its activity, and its potential as a biomarker or therapeutic target in cancer and other disorders. The importance of GMFb in cellular regulation makes it a compelling subject for continued investigation in both basic and applied research contexts.

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