Cat: IPD-X12121

Recombinant Human FGF-9 Protein(HEK293), N-hFc

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Analytical Data

  • Gene name

    FGF-9

  • 简介

    Activin AB protein is a member of the transforming growth factor-β (TGF-β) superfamily and plays a key role in various biological processes such as cell differentiation, proliferation, and apoptosis. It is involved in embryonic development, tissue repair and immune regulation. FGF-9 Protein, Human (HEK293, N-hFc) is the recombinant human-derived FGF-9 protein, expressed by HEK293 , with N-hFc labeled tag.

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Biological Activity

    Measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells. The ED50 for this effect is ≤4.765 ng/mL, corresponding to a specific activity is ≥2.099×105 units/mg. Measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells. The ED50 this effect is 3.362 ng/mL, corresponding to a specific activity is 2.974×105 units/mg.

  • Alternative Names

    Fibroblast growth factor 9; FGF-9; GAF; HBGF-9

  • Species

    Human

  • Source

    HEK293

  • Tag

    N-hFc

  • Purity

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

  • Uniprot

    NP_002001.1

  • Expression Region

    L4-S208

  • AA Sequence

    LGEVGNYFGVQDAVPFGNVPVLPVDSPVLLSDHLGQSEAGGLPRGPAVTDLDHLKGILRRRQLYCRTGFHLEIFPNGTIQGTRKDHSRFGILEFISIAVGLVSIRGVDSGLYLGMNEKGELYGSEKLTQECVFREQFEENWYNTYSSNLYKHVDTGRRYYVALNKDGTPREGTRTKRHQKFTHFLPRPVDPDKVPELYKDILSQS

  • Protein Length

    Full Length of Mature Protein

  • Molecular Weight

    55 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

Fibroblast growth factor 9 (FGF-9) is a crucial member of the FGF family, known for its significant roles in various biological processes, including embryonic development, tissue repair, and regulation of cell proliferation. Research has highlighted FGF-9’s involvement in neurogenesis, indicating its potential therapeutic implications in neurodegenerative diseases and neurological disorders. Additionally, FGF-9 is implicated in angiogenesis and the regulation of bone and cartilage development, making it a subject of interest in regenerative medicine and orthopedic research. The reconstitution of FGF-9 as a recombinant protein allows for in-depth studies of its biological activity, receptor interactions, and signaling pathways. Understanding the molecular mechanisms of FGF-9 can facilitate the development of novel therapeutic strategies for conditions such as traumatic injuries, degenerative diseases, and cancer. The exploration of FGF-9 functions has prompted investigations into its application in tissue engineering and regenerative therapies, with the aim of enhancing healing processes and improving patient outcomes. As the scientific community delves deeper into the potential of FGF-9, ongoing studies continue to unravel its multifaceted roles, providing a promising avenue for innovative treatments and interventions in various fields of medicine.

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