Anti-Human MUC1 (CD227) [Clone C595 (NCRC48)] — Purified in vivo GOLD™ Functional Grade

Purified human MUC1

This monoclonal antibody is aseptically packaged and formulated in 0.01 M phosphate buffered saline (150 mM NaCl) PBS pH 7.2 - 7.4 with no carrier protein, potassium, calcium or preservatives added. Due to inherent biochemical properties of antibodies, certain products may be prone to precipitation over time. Precipitation may be removed by aseptic centrifugation and/or filtration.

Functional grade preclinical antibodies are manufactured in an animal free facility using only in vitro protein free cell culture techniques and are purified by a multi-step process including the use of protein A or G to assure extremely low levels of endotoxins, leachable protein A or aggregates.

anti-human MUC1 (CD227)

Mucin 1 (MUC1) is a 120-225 kDa heterodimeric transmembrane protein in the mucin family (1,3). A growing body of evidence suggests a role for aberrantly-expressed MUC1 in oncogenesis (1-3), immune regulation (2,3), and kidney disease (4). MUC1 is primarily expressed on the epithelial cells lining the respiratory and GI tracts, as well as ducts in the mammary gland, liver, and pancreas (3). The extracellular domain of MUC1 can be shed through auto-proteolysis, and these soluble fragments are elevated in biofluids of cancer patients (3). Signaling through MUC1 involves a variety of common pathways/receptors, including ICAM-1, EGFR, HER2, PI3K-AKT, MAPK, to name a few (3). The hybridoma C595 was developed as a ‘second-generation’ antibody against mucin, using a previously developed anti-mucin antibody (NCRC-11, developed using breast carcinoma cells) to isolate urinary mucin antigens (5). C595 was created using spleen cells of a mouse immunized with these NCRC-11-defined antigens and has a very similar epitope to NCRC-11 (5). C595 has been used in IHC, WB, IF, ELISA, and in-vivo applications (6-8).

ICAM-1, E-selectin

P15941

1. Horm, T. M., & Schroeder, J. A. (2013). MUC1 and metastatic cancer: Expression, function and therapeutic targeting. Cell Adhesion & Migration, 7(2), 187–198.

2. Grewal, U.S., Kurzrock, R. (2025). Mucin-1: a promising pan-cancer therapeutic target. npj Precis. Onc. 9, 218.

3. Palollathil, A., Dagamajalu, S., Ahmed, M., Vijayakumar, M., Prasad, T. S. K., & Raju, R. (2025). The network map of mucin 1 mediated signaling in cancer progression and immune modulation. Discover oncology, 16(1), 1404.

4. Al-Bataineh, M. M., Sutton, T. A., & Hughey, R. P. (2017). Novel roles for mucin 1 in the kidney. Current opinion in nephrology and hypertension, 26(5), 384–391.

5. Price, M. R., Pugh, J. A., Hudecz, F., Griffiths, W., Jacobs, E., Symonds, I. M., Clarke, A. J., Chan, W. C., & Baldwin, R. W. (1990). C595--a monoclonal antibody against the protein core of human urinary epithelial mucin commonly expressed in breast carcinomas. British journal of cancer, 61(5), 681–686.

6. Rabassa, M. E., Croce, M. V., Pereyra, A., & Segal-Eiras, A. (2006). MUC1 expression and anti-MUC1 serum immune response in head and neck squamous cell carcinoma (HNSCC): a multivariate analysis. BMC cancer, 6, 253.

7. Mao, W., Zhang, H., Wang, K. et al. (2024). Research progress of MUC1 in genitourinary cancers. Cell Mol Biol Lett 29, 135.

8. Spencer, D. I., Missailidis, S., Denton, G., Murray, A., Brady, K., Matteis, C. I., Searle, M. S., Tendler, S. J., & Price, M. R. (1999). Structure/activity studies of the anti-MUC1 monoclonal antibody C595 and synthetic MUC1 mucin-core-related peptides and glycopeptides. Biospectroscopy, 5(2), 79–91.