TGFB1 (113 a.a.) Human
Description
Functional Activity
The recombinant protein retains biological activity comparable to native TGF-β1:
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Bioassay: Inhibits IL-4-induced proliferation of HT-2 cells with an ED<sub>50</sub> of 0.0149 ng/mL (specific activity: 6.7 × 10<sup>7</sup> units/mg) .
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Receptor Binding: Binds TGF-β receptor II (TGFBR2) with high affinity (K<sub>D</sub> = 99.2 nM for TGFBR1) .
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Signaling: Activates SMAD-dependent pathways, influencing immune regulation, apoptosis, and extracellular matrix remodeling .
Immune Regulation and Cancer
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Hematological Malignancies: TGFB1 overexpression correlates with immune dysregulation in myeloid cancers (e.g., AML, CML) and modulates macrophage, monocyte, and CD8<sup>+</sup> T-cell infiltration .
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Therapeutic Targeting: Inhibiting TGFB1 enhances immunotherapy efficacy by counteracting its immunosuppressive effects in tumors .
Tissue Engineering and Disease Modeling
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Fibrosis and Wound Healing: Promotes collagen synthesis and fibroblast activation, making it valuable for studying fibrotic diseases .
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Neurological Studies: Linked to schizophrenia susceptibility via TGFB1 +869T>C polymorphism, which increases TGF-β1 production .
Comparative Analysis of Recombinant TGF-β1 Variants
Clinical and Industrial Relevance
Product Specs
Product Science Overview
Transforming Growth Factor-Beta 1 (TGF-β1) is a multifunctional cytokine that plays a crucial role in various cellular processes, including cell growth, differentiation, and immune modulation. The development of TGF-β1 human recombinant proteins has provided valuable tools for studying its biological functions and therapeutic applications .
TGF-β1 is a pivotal cytokine involved in numerous physiological and pathological processes, such as embryonic development, tissue repair, and immune regulation . It is synthesized as a precursor protein that is cleaved to yield a 112 amino acid polypeptide, which remains associated with the latent portion of the molecule . The recombinant form of TGF-β1 (113 a.a.) is produced using recombinant DNA technology, enabling the production of large quantities of biologically active protein for research purposes .
The human recombinant TGF-β1 (113 a.a.) is typically produced in Escherichia coli (E. coli) as a single, non-glycosylated polypeptide chain containing 113 amino acids (279-390 a.a.) with a total molecular mass of 12.9 kDa . The protein is purified using proprietary chromatographic techniques to ensure high purity and biological activity .
- Source: Escherichia coli (E. coli)
- Physical Appearance: Sterile filtered colorless solution
- Formulation: Contains 10mM Sodium Citrate (pH 3.5) and 10% glycerol
- Stability: Store at 4°C if used within 2-4 weeks; for longer periods, store frozen at -20°C. For long-term storage, it is recommended to add a carrier protein (0.1% HSA or BSA) and avoid multiple freeze-thaw cycles .
- Purity: Greater than 95.0% as determined by SDS-PAGE .
TGF-β1 is involved in a wide range of cellular processes, including:
