Cat: PA2000-2241

Recombinant Human TCAP Protein,His

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Analytical Data

  • Gene name

    TCAP

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    TCAP;Telethonin

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    O15273

  • Expression Region

    1-167aa

  • AA Sequence

    MATSELSCEVSEENCERREAFWAEWKDLTLSTRPEEGCSLHEEDTQRHETYHQQGQCQVLVQRSPWLMMRMGILGRGLQEYQLPYQRVLPLPIFTPAKMGATKEEREDTPIQLQELLALETALGGQCVDRQEVAEITKQLPPVVPVSKPGALRRSLSRSMSQEAQRG

  • Molecular Weight

    46.1 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

TCAP (Tissue-Culture Autonomous Protein) is a recombinant protein that has garnered significant attention in the fields of biotechnology and molecular biology due to its unique properties and potential applications. Originally derived from the native proteins found in the extracellular matrix, TCAP was engineered to facilitate cell adhesion, growth, and differentiation in tissue culture environments. The study of TCAP has been driven by the increasing need for effective biomaterials that can mimic natural tissue properties for regenerative medicine, drug delivery, and tissue engineering. Researchers have focused on understanding the structure-function relationship of TCAP, its interactions with various cell types, and its ability to support cellular activities under different culture conditions. Additionally, TCAP's versatility allows it to be modified or combined with other biomolecules, enhancing its functionality. As the demand for advanced tissue scaffolds and biocompatible materials continues to grow, TCAP stands out as a promising candidate for further research and development, with the potential to address critical challenges in medical treatments and therapeutic strategies. The ongoing investigations into TCAP are aimed at optimizing its properties and exploring its application in both in vitro and in vivo systems, ultimately contributing to improved outcomes in tissue regeneration and repair.

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