The recombinant human TSPAN8 protein is a mammalian cell-expressed virus-like particle (VLP) presenting the full-length human TSPAN8 sequence spanning amino acids 1 to 237, with a C-terminal 10xHis tag facilitating purification. This lyophilized protein preparation exhibits functional activity as demonstrated by its ability to specifically bind the anti-TSPAN8 recombinant antibody (CSB-RA025166MA1HU) in ELISA assays, with an EC50 ranging from 2.261 to 2.623 ng/mL when immobilized at 5 μg/mL. The VLPs without TSPAN8 serve as negative controls. The VLP format preserves native-like conformation and membrane topology, enhancing the presentation of conformational epitopes for antibody recognition and functional studies. This recombinant TSPAN8 protein is valuable for investigating tetraspanin-mediated cellular processes and developing therapeutic antibodies targeting tumor-associated antigens.
Human TSPAN8, also known as TM4SF3, belongs to the tetraspanin superfamily, characterized by its four highly-conserved transmembrane domains and its involvement in various cellular processes, including cell proliferation, adhesion, and motility [1]. TSPAN8 is particularly noted for its role in cancer, having been identified as a tumor-associated antigen with elevated expression in multiple malignancies such as melanoma, pancreatic cancer, and colorectal cancer [2][3][4]. The overexpression of TSPAN8 has been correlated with increased metastatic potential and cancer progression [3][4].
TSPAN8 forms microdomains in the cell membrane, facilitating the lateral organization of proteins and interaction with various partners, including integrins [5][6]. This dynamic organization is critical for regulating multiple signaling pathways related to cell movement and growth [6][2]. For instance, TSPAN8 promotes invasive characteristics in melanoma cells by activating certain extracellular matrix-degrading enzymes, contributing to the protein's role in facilitating tumor invasion and metastasis [7][8].
Moreover, research has highlighted TSPAN8's potential as a prognostic marker in cancer. High expression levels of TSPAN8 have been linked to poor outcomes in various types of cancers, making it a candidate for targeted immunotherapy [9][10]. Studies indicate that TSPAN8 is instrumental in the recruitment of proteins into extracellular vesicles, which further influences intercellular communication and may play a role in the tumor microenvironment [11][12]. TSPAN8 also appears to cross-regulate with other signaling molecules, influencing cancer cell behavior under various physiological conditions [6][2][9].
References:
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[11] J. Zhu, J. Zhang, X. Ji, Z. Tan, & D. Lubman. Column-based technology for cd9-hplc immunoaffinity isolation of serum extracellular vesicles. Journal of Proteome Research, vol. 20, no. 10, p. 4901-4911, 2021. https://doi.org/10.1021/acs.jproteome.1c00549
[12] Y. Liu, J. Fan, et al. Extracellular vesicle tetraspanin-8 level predicts distant metastasis in non–small cell lung cancer after concurrent chemoradiation. Science Advances, vol. 6, no. 11, 2020. https://doi.org/10.1126/sciadv.aaz6162
