Recombinant human TGF-beta receptor type-1 (TGFBR1) is a high-purity protein with a purity exceeding 90%, as confirmed by SDS-PAGE. Derived from human species and expressed in E. coli, this protein includes the expression region 34-126aa, representing a partial length version. It contains an N-terminal 10xHis-tag and a C-terminal Myc-tag for easy detection and purification. It comes in liquid or lyophilized powder form.
The human TGFBR1 forms a heterocomplex with TGFBR2 upon binding with TGF-β, leading to the phosphorylation of downstream signaling proteins, particularly the SMAD family of proteins, which transduce the signal to the nucleus to regulate gene expression [1][2]. This receptor is integral to physiological and pathological processes, including cell growth, differentiation, migration, development, immune response, and cancer progression [3][4].
Evidence has shown that miR-769-5p inhibits the proliferation and invasion of NSCLC cells by targeting TGFBR1, highlighting the TGFBR1's role in cancer biology [5][6]. TGFBR1 is implicated in other diseases, including fibrosis and cardiovascular conditions. The receptor's signaling can promote fibrogenesis in tissues such as the liver and heart, enhancing the activation and survival of fibroblasts and myofibroblasts [7][8]. Moreover, dysregulation of TGFBR1 signaling has been associated with aortic aneurysm formation, indicating its involvement in vascular diseases [9].
References:
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[2] M. Boutet, L. Gauthier, M. Leclerc, G. Gros, V. Montpréville, N. Théretet al., Tgfβ signaling intersects with cd103 integrin signaling to promote t-lymphocyte accumulation and antitumor activity in the lung tumor microenvironment, Cancer Research, vol. 76, no. 7, p. 1757-1769, 2016. https://doi.org/10.1158/0008-5472.can-15-1545
[3] Y. Li, D. Deng, C. Höfer, J. Kim, W. Heo, Q. Xuet al., Liebig’s law of the minimum in the tgf-β/smad pathway,, 2023. https://doi.org/10.1101/2023.07.10.548398
[4] R. Liu, Y. Zhang, Y. Ding, S. Zhang, & L. Pan, Characteristics of tgfbr1–egfr–ctnnb1–cdh1 signaling axis in wnt-regulated invasion and migration in lung cancer, Cell Transplantation, vol. 29, p. 096368972096916, 2020. https://doi.org/10.1177/0963689720969167
[5] H. Guo, Z. Bao, J. Li, S. Lian, S. Wang, Y. Heet al., Correction: molecular characterization of tgf-β type i receptor gene (tgfbr1) in chlamys farreri, and the association of allelic variants with growth traits, Plos One, vol. 8, no. 7, 2013. https://doi.org/10.1371/annotation/75437eff-feb9-4592-baeb-ec7b98d1d212
[6] Y. Zhao, J. He, P. Gao, Y. Niu, J. Zhang, L. Wanget al., Mir-769-5p suppressed cell proliferation, migration and invasion by targeting tgfbr1 in non-small cell lung carcinoma, Oncotarget, vol. 8, no. 69, p. 113558-113570, 2017. https://doi.org/10.18632/oncotarget.23060
[7] F. Jiang, Q. Yu, Y. Chu, X. Zhu, W. Lu, Q. Liuet al., Microrna-98-5p inhibits proliferation and metastasis in non-small cell lung cancer by targeting tgfbr1, International Journal of Oncology, 2018. https://doi.org/10.3892/ijo.2018.4610
[8] W. Liao, P. Liang, B. Liu, Z. Xu, L. Zhang, M. Fenget al., Microrna-140-5p mediates renal fibrosis through tgf-β1/smad signaling pathway by directly targeting tgfbr1, Frontiers in Physiology, vol. 11, 2020. https://doi.org/10.3389/fphys.2020.01093
[9] Y. Wang, J. Du, X. Niu, N. Fu, R. Wang, Y. Zhanget al., Mir-130a-3p attenuates activation and induces apoptosis of hepatic stellate cells in nonalcoholic fibrosing steatohepatitis by directly targeting tgfbr1 and tgfbr2, Cell Death and Disease, vol. 8, no. 5, p. e2792-e2792, 2017. https://doi.org/10.1038/cddis.2017.10
