Cat: IPD-X27652

Recombinant Human Thymopoietin Protein,His

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Analytical Data

  • Gene name

    Thymopoietin

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    TP; LAP2; CMD1T; LEMD4; TP5; Splenin; Lamina-Associated Polypeptide 2,Isoforms Beta/Gamma; LEM Domain Containing 4; Thymopoietin-related peptide isoforms beta/gamma

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 95% as determined by SDS-PAGE.

  • Uniprot

    P42167

  • Expression Region

    Met1~Leu243

  • Molecular Weight

    35kDa

  • 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

Thymopoietin (TP) is a thymus-derived peptide that plays a crucial role in T-cell differentiation and immune regulation. Initially identified in the 1970s, TP has been found to influence various physiological processes, including the maturation of T lymphocytes, which are essential for adaptive immunity. Research has shown that TP can enhance T-cell proliferation and cytokine production, making it a potential candidate for therapeutic applications, particularly in immune deficiency and autoimmune diseases. The recombinant form of thymopoietin has been utilized in various studies to better understand its biological functions and mechanism of action. Advances in recombinant DNA technology have facilitated the production of TP, allowing researchers to generate sufficient quantities for both in vitro and in vivo experiments. By exploring its structural properties and interactions with immune cells, scientists aim to develop TP-based therapies that could enhance immune responses or serve as immunomodulators. The growing interest in TP and its recombinant forms reflects its potential as a novel therapeutic agent to improve immune function in clinical settings, suggesting that further research could lead to significant advancements in immunotherapy and regenerative medicine.

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