TGFBR1 Antibodies

Structure of TGFBR1

The TGFBR1 gene encodes a transforming growth factor β receptor 1, which is a transmembrane serine/threonine kinase protein with a molecular weight of approximately 53 kDa. The molecular weight varies slightly among different species, mainly due to the conservative amino acid sequence variations in the extracellular region and the kinase domain.

This protein is composed of approximately 503 amino acid residues. Its primary structure includes a signal peptide, an extracellular ligand-binding domain rich in cysteines, a transmembrane region, and an intracellular kinase domain. In terms of secondary structure, its extracellular region is mainly composed of β-sheet, responsible for specifically recognizing and binding to the TGF-β ligand; while the intracellular kinase domain is mainly composed of α-helix, forming an ATP-binding pocket. The key to the spatial conformation lies in a conformational change transmitted by the transmembrane region: when the ligand binds, the two receptors (TGFBR1 and TGFBR2) form an heterodimer, and TGFBR2 phosphorylates a specific glycine-serine-rich region (GS domain) of the kinase structure domain of TGFBR1, thereby relieving autorepression and activating the downstream SMAD protein signaling pathway.

Fig. 1 Schematic depiction of the TGFBR1 protein.¹

Key structural properties of TGFBR1:

• Extracellular ligand-binding domains are rich in conserved cysteine
• Intracellular GS domain (Glycine-Serine rich region)
• The serine/threonine kinase domain contains a typical ATP-binding pocket and a catalytic loop

Functions of TGFBR1

The TGFBR1 gene encodes the transforming growth factor β receptor 1. Its core function is to serve as a key hub for cell signal transduction, by mediating the regulation of cell fate and tissue homeostasis through the TGF-β superfamily signaling. Its main functions are as follows:

The signal output of this receptor is highly context-dependent: in normal epithelial cells, it mainly exerts a **tumor suppressor** function; however, in advanced tumors or stromal cells, its signaling pathway is often **hijacked**, and it instead promotes tumor invasion, metastasis, and immune evasion. The precise regulation of its kinase activity is crucial for maintaining tissue balance.

Applications of TGFBR1 and TGFBR1 Antibody in Literature

1. Alaamery, Manal, et al. "TGFBR1 variants can associate with non-syndromic congenital heart disease without Aortopathy." Journal of Cardiovascular Development and Disease 10.11 (2023): 455. https://doi.org/10.3390/jcdd10110455

The study found that rare variations in the TGFBR1 gene (p.R398C/p.R398H) can cause hereditary non-syndromic congenital heart disease without aortic involvement. The mechanism is related to abnormal TGF-β signaling pathway. This expands the understanding of the pathogenicity of this gene.

2. Wang, Xinyue, et al. "Rescue RM/CS-AKI by blocking strategy with one-dose anti-myoglobin RabMAb." Nature Communications 16.1 (2025): 1044. https://doi.org/10.1038/s41467-024-55788-5

The study found that the NPC1 protein binds to TGFBR1 through its transmembrane domain (aa 692-854), inhibiting the ubiquitination and degradation of TGFBR1 mediated by SMAD7/SMURF, thereby promoting the progression of hepatocellular carcinoma independently of its cholesterol transport function.

3. Wang, Yong-qiang, et al. "Association between TGFBR1 polymorphisms and cancer risk: a meta-analysis of 35 case-control studies." PLOS One (2012): e42899. https://doi.org/10.1371/journal.pone.0042899

This meta-analysis confirmed that the *6A variant of the TGFBR1 gene and the IVS7+24G>A polymorphism are associated with the risk of cancer, especially having a significant impact on ovarian cancer, breast cancer, etc. This suggests that the genetic polymorphism of this gene is a potential genetic marker for cancer susceptibility.

4. Qiu, Jiehua, et al. "Identification of TGFBR1 Gene Variants in Two Chinese Pedigrees with Loeys-Dietz Syndrome." Brazilian Journal of Cardiovascular Surgery 40.1 (2025): e20230495. https://doi.org/10.21470/1678-9741-2023-0495

In this study, new mutations in the TGFBR1 gene (p.Ala202Val and p.Glu227Lys) were identified in two patients with LDS. These mutations were confirmed to be the main genetic cause of the disease. Case two recovered well after endovascular surgery, suggesting that this surgical method can provide a feasible option for patients.

5. Wu, Weidong, et al. "ANRIL upregulates TGFBR1 to promote idiopathic pulmonary fibrosis in TGF-β1-treated lung fibroblasts via sequestering let-7d-5p." Epigenetics 19.1 (2024): 2435682. https://doi.org/10.1080/15592294.2024.2435682

This study reveals that the long non-coding RNA ANRIL is highly expressed in pulmonary fibrosis. It upregulates TGFBR1 by adsorbing let-7d-5p, thereby promoting fibroblast activation and fibrosis. Targeting ANRIL may represent a new therapeutic strategy.

Creative Biolabs: TGFBR1 Antibodies for Research

Creative Biolabs specializes in the production of high-quality TGFBR1 antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

• Custom TGFBR1 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 TGFBR1 antibodies, custom preparations, or technical support, contact us at email.