Cat: IPD-X38232

Recombinant Human TGFb1 Protein,His

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Analytical Data

  • Gene name

    TGFb1

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    TGF-B1; CED; DPD1; LAP; Camurati-Engelmann Disease; Latency-associated peptide

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P01137

  • Expression Region

    Ala279~Ser390

  • Molecular Weight

    15kDa

  • 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

Transforming Growth Factor Beta 1 (TGF-β1) is a multifaceted cytokine that plays crucial roles in various biological processes, including cell proliferation, differentiation, immune responses, and tissue repair. Its dysregulation is implicated in numerous pathologies, such as fibrosis, cancer, and autoimmune disorders. The ability to produce recombinant TGF-β1 has significantly advanced research into its functional mechanisms and therapeutic applications. Recombinant TGF-β1 is generated through recombinant DNA technology, allowing for the synthesis of large quantities of the protein with high purity. This enables detailed studies on its role in cell signaling pathways and the complex interactions within the tumor microenvironment. Additionally, it provides a valuable tool for investigating TGF-β1's effects on different cell types, including fibroblasts, epithelial cells, and immune cells. Understanding these interactions is critical for developing strategies to modulate TGF-β1 activity in disease contexts, potentially leading to novel therapeutic interventions. Furthermore, the availability of recombinant TGF-β1 has facilitated the exploration of its role in stem cell biology, tissue engineering, and regenerative medicine, highlighting its importance as a therapeutic target. Overall, the study of recombinant TGF-β1 not only deepens our understanding of its biological functions but also paves the way for innovative treatments for diseases associated with its dysregulation.

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