TGF-β Antibodies

Structure of TGF-β

TGF-β form of mature activity is composed of 112 amino acid monomers, and formed through disulfide bond homologous dimers, present the stability of the beta folding barrel structure. Its core function relies on the highly conserved cystine knot domain, which is cross-linked and stabilized by multiple pairs of disulfide bonds, endowing the protein with extremely strong structural rigidity.

TGF-β is a homologous dimer protein linked by disulfide bonds. Each monomer contains 112 amino acids and has a characteristic cystine binding domain. This protein is secreted in the form of a latent complex, containing a latent associated peptide (LAP) and a mature TGF-β dimer. When LAP is cleaved by protease, the exposed receptor binding sites can successively bind to TβRII and TβRI receptors, regulating processes such as cell proliferation, differentiation and immune response through the Smad signaling pathway.

Fig. 1 TGF-β drives the multidimensional mechanism of TME immunosuppression and treatment resistance.¹

Key structural properties of TGF-β:

• Cystine knot structural motifs stabilized by disulfide bonds
• Latent complexes are formed through non-covalently bound LAP
• β -fold interface with receptor binding ("wrist" region)
• Dimer conformation is the foundation of its biological activity
• Protein hydrolysis activation is required to release the function

Functions of TGF-β

TGF-β (Transforming growth factor-β) is a multifunctional cytokine, mainly involved in physiological processes such as cell growth, differentiation and immune regulation. Its core functions include:

The signal transduction of TGF-β has typical biphasic characteristics: at low concentrations, it mainly shows growth inhibitory effects, while at high concentrations, it exhibits pro-fibrotic and pro-metastatic activities. This characteristic makes it play a complex and crucial role in maintaining tissue homeostasis and disease development.

Applications of TGF-β and TGF-β Antibody in Literature

1. Hülper, Petra, et al. "Tumor localization of an anti-TGF-β antibody and its effects on gliomas." International journal of oncology 38.1 (2011): 51-59.https://doi.org/10.3892/ijo_00000823

Studies have shown that intravenous injection of TGF-β neutralizing antibody 1D11 can be targeted and enriched in glioma tissues. In immune-healthy mice, 1D11 completely regressed subcutaneous GL261 tumors, but in situ tumors only inhibited invasion. Tumor growth accelerated in immunodeficient mice, indicating that the anti-tumor effect of TGF-β depends on the microenvironment and immune status.

2. Lee, Jung-Shun, et al. "Anti-IL-20 antibody improved motor function and reduced glial scar formation after traumatic spinal cord injury in rats." Journal of Neuroinflammation 17 (2020): 1-12. https://link.springer.com/article/10.1186/s12974-020-01814-4

Studies have shown that during the secondary injury process after spinal cord injury, the pro-inflammatory factor IL-20 may play a key role by regulating the expression of TGF-β1. In pathological processes such as renal fibrosis and liver cirrhosis, IL-20, as a pro-inflammatory factor, can up-regulate the expression of TGF-β1, thereby promoting the fibrosis process.

3. Yi, Ming, et al. "The construction, expression, and enhanced anti-tumor activity of YM101: a bispecific antibody simultaneously targeting TGF-β and PD-L1." Journal of hematology & oncology 14 (2021): 1-22. https://link.springer.com/article/10.1186/s13045-021-01045-x

Studies have shown that although anti-PD-1 /PD-L1 therapy can stimulate a persistent anti-tumor response, the clinical response rate is limited. Studies have found that the immune negative regulatory factor TGF-β can significantly weaken the efficacy of PD-1/PD-L1 inhibitors and lead to drug resistance. At present, the combined treatment regimen targeting both PD-1/PD-L1 and TGF-β simultaneously shows breakthrough potential and is expected to significantly improve the therapeutic effect and solve the problem of drug resistance.

4. Gulley, James L., et al. "Dual inhibition of TGF‐β and PD‐L1: a novel approach to cancer treatment." Molecular oncology 16.11 (2022): 2117-2134. https://doi.org/10.1002/1878-0261.13146

This article explains that TGF-β and PD-L1 cooperatively suppress immunity through complementary pathways in the tumor microenvironment (TME): TGF-β promotes fibrosis and immunosuppression, while PD-L1 inhibits T cell function. Anti-pd-l1 therapy is vulnerable to TGF-β -mediated drug resistance. Currently, dual-target drugs can simultaneously block both pathways, which is expected to improve the therapeutic effect and reduce toxicity.

5. Niu, Mengke, et al. "Synergistic efficacy of simultaneous anti-TGF-β/VEGF bispecific antibody and PD-1 blockade in cancer therapy." Journal of hematology & oncology 16.1 (2023): 94. https://link.springer.com/article/10.1186/s13045-023-01487-5

This article indicates that the efficacy of PD-1/PD-L1 antibodies is limited, and TGF-β is the key drug resistance factor. It significantly reduces the therapeutic effect by inhibiting the function of immune cells, promoting tumor fibrosis and immune escape. Targeting TGF-β combined with PD-1/PD-L1 blockade is expected to overcome the problem of drug resistance.

Creative Biolabs: TGF-β Antibodies for Research

Creative Biolabs specializes in the production of high-quality TGF-β antibodies for research and industrial applications. Our portfolio features monoclonal antibodies specifically optimized for ELISA, Flow Cytometry, Western Blot, Immunohistochemistry, and other advanced diagnostic applications.

• Custom TGF-β Antibody Development: Tailor-made solutions to meet specific research requirements.
• Bulk Production: Large-scale antibody manufacturing for industry partners.
• Technical Support: Expert consultation for protocol optimization and troubleshooting.
• Aliquoting Services: Conveniently sized aliquots for long-term storage and consistent experimental outcomes.

For more details on our TGF-β antibodies, custom preparations, or technical support, contact us at info@creative-biolabs.com.