Cat: IPD-X40012

Recombinant Human TBCC Protein ,His

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Analytical Data

  • Gene name

    TBCC

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Tubulin-folding cofactor C ;CFC

  • Species

    Human

  • Source

    E. coli

  • Tag

    N- His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q15814

  • Expression Region

    2-345aa

  • Molecular Weight

    43 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.

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Protein Description

The study of TBCC (tubulin-specific chaperone C) recombinant protein has garnered significant attention in recent years due to its crucial role in the assembly and regulation of tubulin, a key structural component of the cytoskeleton in eukaryotic cells. Tubulin polymerization into microtubules is essential for various cellular processes, including cell division, intracellular transport, and maintenance of cell shape. TBCC, as a chaperone, assists in the proper folding and assembly of tubulin, ensuring the formation of functional microtubules. Dysfunction in tubulin dynamics is associated with several diseases, including cancer and neurodegenerative disorders, highlighting the importance of understanding TBCC's mechanisms. Research on TBCC recombinant protein aims to elucidate its structure-function relationship, to explore its interactions with tubulin, and to investigate its potential as a therapeutic target. By producing TBCC in recombinant systems, researchers can study its biochemical properties in detail, facilitating the development of strategies to modulate its activity in pathological conditions. Ultimately, this research could pave the way for novel treatments that leverage the manipulation of microtubule dynamics to address various diseases linked to cytoskeletal dysfunction.

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