The recombinant human MUC13 protein is an active form produced in a yeast expression system, which supports proper folding and glycosylation for functional integrity. It comprises amino acids 19 to 421 of the native MUC13 sequence and features an N-terminal 6xHis tag to facilitate purification and assay compatibility. Supplied as a lyophilized powder, the recombinant MUC13 protein demonstrates high purity, exceeding 95% as confirmed by SDS-PAGE. Endotoxin content is tightly controlled and remains below 1.0 EU/µg, as measured by the LAL assay. Functional activity is verified through ELISA, where immobilized MUC13 at 2 μg/mL binds specifically to the anti-MUC13 recombinant antibody (CSB-RA887973MA1HU), with an EC50 in the range of 2.592 to 2.923 ng/mL. These attributes confirm its suitability for applications in antibody screening, biomarker research, and mucin-related studies.
Human MUC13 protein is a member of the mucin family of glycoproteins primarily expressed on the cell surfaces of epithelial tissues. The MUC13 gene encodes a high-molecular-weight transmembrane glycoprotein characterized by its significant role in cellular processes such as signaling, adhesion, and modulation of tumor microenvironments. It plays a crucial role in various cancers, including colorectal, gastric, ovarian, and pancreatic cancers.
MUC13 expression is notably increased in various carcinomas, suggesting its involvement in tumorigenesis and progression. Various studies have established that its overexpression correlates with cancer aggressiveness and poor prognosis. For instance, overexpression of MUC13 is linked to increased nuclear localization of β-catenin, which has been found to correlate with decreased overall survival rates in liver cancer patients [1]. Research shows that MUC13 promotes malignant growth and metastasis by upregulating key oncogenic pathways and proteins, including the NF-κB pathway, which has been shown to enhance cell survival and proliferation [2].
In colorectal cancer, the knockdown of MUC13 has been observed to sensitize cancer cells to anti-cancer therapies and apoptosis-inducing treatments, suggesting its role in chemoresistance [3]. Furthermore, MUC13's interaction with receptor tyrosine kinases like HER2 has been linked to signal transduction mechanisms that drive pancreatic ductal adenocarcinoma progression [4]. This has opened avenues for monoclonal antibody development targeting MUC13, which holds promising implications for cancer immunotherapy [5].
The functional properties of MUC13 extend beyond tumor biology. It also participates in inflammatory responses. This dual role implicates MUC13 in cancer biology and normal physiological processes such as mucosal immunity and epithelial barrier functions [6]. For example, MUC13 can modulate gastrointestinal inflammation, indicating its significance in treating gastrointestinal tract diseases [7].
References:
[1] K. Doxtater, M. Tripathi, et al. Muc13 drives cancer aggressiveness and metastasis through the yap1-dependent pathway. Life Science Alliance, vol. 6, no. 12, p. e202301975, 2023. https://doi.org/10.26508/lsa.202301975
[2] Y. Sheng, Y. He, et al. Muc13 protects colorectal cancer cells from death by activating the nf-κb pathway and is a potential therapeutic target. Oncogene, vol. 36, no. 5, p. 700-713, 2016. https://doi.org/10.1038/onc.2016.241
[3] B. Gupta, D. Maher, et al. Increased expression and aberrant localization of mucin 13 in metastatic colon cancer. Journal of Histochemistry & Cytochemistry, vol. 60, no. 11, p. 822-831, 2012. https://doi.org/10.1369/0022155412460678
[4] S. Khan, M. Sikander, et al. Muc13 interaction with receptor tyrosine kinase her2 drives pancreatic ductal adenocarcinoma progression. Oncogene, vol. 36, no. 4, p. 491-500, 2016. https://doi.org/10.1038/onc.2016.218
[5] Y. Nishii, M. Yamaguchi, et al. A newly developed anti-mucin 13 monoclonal antibody targets pancreatic ductal adenocarcinoma cells. International Journal of Oncology, vol. 46, no. 4, p. 1781-1787, 2015. https://doi.org/10.3892/ijo.2015.2880
[6] Y. Sheng, S. Triyana, et al. Muc1 and muc13 differentially regulate epithelial inflammation in response to inflammatory and infectious stimuli. Mucosal Immunology, vol. 6, no. 3, p. 557-568, 2013. https://doi.org/10.1038/mi.2012.98
[7] C. Liu, A. Smet, et al. Gastric de novo muc13 expression and spasmolytic polypeptide-expressing metaplasia during helicobacter heilmannii infection. Infection and Immunity, vol. 82, no. 8, p. 3227-3239, 2014. https://doi.org/10.1128/iai.01867-14
