Cat: IPD-X38750

Recombinant Human TPSd1 Protein,His

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Analytical Data

  • Gene name

    TPSd1

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    MCP7L1; MMCP-7L; mMCP-7-like II; mMCP-7-like I; MMCP-7-LIKE-2; HmMCP-3-like tryptase III; Mast cell mMCP-7-like; Tryptase-3

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q9BZJ3

  • Expression Region

    Glu99~Glu191

  • Molecular Weight

    14kDa

  • 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

TPSd1 (Trehalose-6-phosphate synthase 1) is a crucial enzyme involved in trehalose biosynthesis, an essential sugar that serves as an energy source and plays a significant role in stress responses in various organisms, including plants, fungi, and bacteria. The increasing interest in trehalose has stemmed from its potential applications in agriculture, biotechnology, and medicine, particularly due to its protective effects against abiotic stresses such as drought, salinity, and extreme temperatures. Research on TPSd1 and its recombinant protein has garnered attention as it provides insights into the regulatory mechanisms of trehalose metabolism. Understanding the structure and function of TPSd1 at a molecular level can lead to advancements in crop engineering to enhance stress tolerance, improve yield, and augment food security amidst climate change challenges. Furthermore, TPSd1 presents opportunities for biotechnological innovations, including the development of trehalose-based therapies in medicine, exploiting its roles in cellular protection and anti-apoptotic pathways. Overall, the study of TPSd1 recombinant protein represents a vital frontier in the intersection of molecular biology, agriculture, and biomedicine, with promising implications for enhancing resilience in both plants and human health.

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