Code | CSB-MP023072HU2 |
Abbreviation | Recombinant Human TACSTD2 protein, partial (Active) |
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Size | $174 |
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The recombinant human TACSTD2 protein is produced through mammalian cell expression of a plasmid containing the target gene for amino acids 31-274 of the human TACSTD2. The target gene fragment is co-expressed with the C-terminal 10xHis-tag gene. SDS-PAGE analysis reveals a purity of this TACSTD2 protein greater than 95%, and endotoxin levels measured by the LAL method are less than 1.0 EU/μg. ELISA confirms the TACSTD2 protein's biological activity with specific TACSTD2 recombinant antibody (CSB-RA023072MA1HU) binding, achieving an EC50 range of 0.9108 to 1.640 ng/mL.
Human TACSTD2 (TROP2) is a type I transmembrane glycoprotein that plays a significant role in various cellular processes, particularly in the context of cancer biology. It is widely expressed in various epithelial tumors, including breast, prostate, lung, and colorectal cancers [1][2][3].
TACSTD2 functions primarily as a calcium signal transducer and is involved in the regulation of intracellular calcium levels. This calcium signaling is crucial for various cellular functions, including proliferation, migration, and invasion of cancer cells [6][7]. TACSTD2 has been shown to activate several intracellular signaling pathways, notably the MAPK and PI3K/AKT pathways, which are essential for tumor growth and metastasis [6][7]. Studies have demonstrated that TACSTD2 can enhance the invasion of cancer cells by modulating matrix metalloproteinase activity through ERK and JNK signaling pathways [8][7].
Moreover, TACSTD2 is associated with the epithelial-mesenchymal transition (EMT), a process that enables epithelial cells to acquire migratory and invasive properties, which is a hallmark of cancer progression [9]. The expression of TACSTD2 is often upregulated in various cancers, correlating with poor prognosis and increased metastatic potential [2][3][10]. In prostate cancer, TACSTD2 has been identified as a marker that distinguishes a subpopulation of cells with stem cell-like characteristics, further implicating its role in tumorigenesis [11].
References:
[1] K. Nakashima, H. Shimada, T. Ochiai, M. Kuboshima, N. Kuroiwa, S. Okazumi, et al. Serological identification of trop2 by recombinant cdna expression cloning using sera of patients with esophageal squamous cell carcinoma, International Journal of Cancer, vol. 112, no. 6, p. 1029-1035, 2004. https://doi.org/10.1002/ijc.20517
[2] B. Wu, C. Yu, B. Zhou, T. Huang, L. Gao, T. Liu, et al. Overexpression of trop2 promotes proliferation and invasion of ovarian cancer cells, Experimental and Therapeutic Medicine, vol. 14, no. 3, p. 1947-1952, 2017. https://doi.org/10.3892/etm.2017.4788
[3] S. Zaman, H. Jadid, A. Denson, & J. Gray. Targeting Trop-2 in solid tumors: future prospects, Oncotargets and Therapy, vol. Volume 12, p. 1781-1790, 2019. https://doi.org/10.2147/ott.s162447
[4] M. Pak, D. Shin, C. Lee, & M. Lee. Significance of epcam and trop2 expression in non-small cell lung cancer, World Journal of Surgical Oncology, vol. 10, no. 1, 2012. https://doi.org/10.1186/1477-7819-10-53
[5] E. Guerra. Targeting trop-2 as a cancer driver, Journal of Clinical Oncology, vol. 41, no. 29, p. 4688-4692, 2023. https://doi.org/10.1200/jco.23.01207
[6] D. Okajima, S. Yasuda, T. Maejima, T. Karibe, K. Sakurai, T. Aida, et al. Datopotamab deruxtecan, a novel trop2-directed antibody–drug conjugate, demonstrates potent antitumor activity by efficient drug delivery to tumor cells, Molecular Cancer Therapeutics, vol. 20, no. 12, p. 2329-2340, 2021. https://doi.org/10.1158/1535-7163.mct-21-0206
[7] X. Guo, X. Zhu, L. Zhao, L. Xiao, D. Cheng, & K. Feng. Tumor-associated calcium signal transducer 2 regulates neovascularization of non-small-cell lung cancer via activating erk1/2 signaling pathway, Tumor Biology, vol. 39, no. 3, p. 101042831769432, 2017. https://doi.org/10.1177/1010428317694324
[8] H. Guan, Z. Guo, W. Liang, H. Li, G. Wei, L. Xu, et al. Trop2 enhances invasion of thyroid cancer by inducing mmp2 through erk and jnk pathways, BMC Cancer, vol. 17, no. 1, 2017. https://doi.org/10.1186/s12885-017-3475-2
[9] F. Davis, I. Azimi, R. Faville, A. Peters, K. Jalink, J. Putney, et al. Induction of epithelial–mesenchymal transition (emt) in breast cancer cells is calcium signal dependent, Oncogene, vol. 33, no. 18, p. 2307-2316, 2013. https://doi.org/10.1038/onc.2013.187
[10] E. Bignotti, L. Zanotti, S. Calza, M. Falchetti, S. Lonardi, A. Ravaggi, et al. Trop-2 protein overexpression is an independent marker for predicting disease recurrence in endometrioid endometrial carcinoma, BMC Clinical Pathology, vol. 12, no. 1, 2012. https://doi.org/10.1186/1472-6890-12-22
[11] A. Goldstein, D. Lawson, D. Cheng, W. Sun, I. Garraway, & O. Witte. Trop2 identifies a subpopulation of murine and human prostate basal cells with stem cell characteristics, Proceedings of the National Academy of Sciences, vol. 105, no. 52, p. 20882-20887, 2008. https://doi.org/10.1073/pnas.0811411106
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