United Kingdom (UK)
Recombinant monoclonal antibody to MUC1. Manufactured using AbAb’s Recombinant Platform with variable regions (i.e. specificity) from the hybridoma 12D10.
UniProt Accession Number of Target Protein: P15941
Alternative Name(s) of Target: Mucin-1; Breast carcinoma-associated antigen DF3; Cancer antigen 15-3; CA 15-3; Carcinoma-associated mucin; Episialin; H23AG; Krebs von den Lungen-6; KL-6; PEMT; Peanut-reactive urinary mucin; PUM; Polymorphic epithelial mucin; PEM; Tumor-associated epithelial membrane antigen; EMA; Tumor-associated mucin; CD227
Immunogen: This antibody was raised by immunizing female Balb/c mice with MUC1 antigen.
Specificity: This antibody is specific for the unsubstituted O-6 position of the Neu5Ac residue of MUC1. The alpha subunit of MUC1 has cell adhesive properties. Can act both as an adhesion and an anti-adhesion protein. May provide a protective layer on epithelial cells against bacterial and enzyme attack. The beta subunit of MUC-1 contains a C-terminal domain which is involved in cell signaling, through phosphorylations and protein-protein interactions. Modulates signaling in ERK, SRC and NF-kappa-B pathways. In activated T-cells, influences directly or indirectly the Ras/MAPK pathway. Promotes tumor progression. Regulates TP53-mediated transcription and determines cell fate in the genotoxic stress response. Binds, together with KLF4, the PE21 promoter element of TP53 and represses TP53 activity.
Application Notes: To characterize this antibody an ELISA was preformed on MUC1 glycorproteins. Furthermore, the binding constant of this antibody was determined by surface plasmon resonance on MUC1 glycoprotein using the mouse version of this antibody. Finally, human breast cancer cells (T-47D), human lung adenocarcinoma cells (Calu-3), human mucoepidermoid carcinoma cells (H292), and human lung adenocarcinoma epithelial cells were used for flow cytometry with the murine version of this antibody (Naito et al, 2017; pmid:30023556).
Antibody first published in:
Naito et al. Generation of Novel Anti-MUC1 Monoclonal Antibodies with Designed Carbohydrate Specificities Using MUC1 Glycopeptide Library. ACS Omega. 2017 Nov 30;2(11):7493-7505. PMID:30023556
Note on publication:
. In this study, using an MUC1 glycopeptide library, we established two novel anti-MUC1 monoclonal antibodies (1B2 and 12D10) with designed carbohydrate specificities.
Western blot using anti-MUC1 antibody 12D10 (Ab02843). A431 (A) (0.1µg/ml), HeLa (B) (0.1µg/ml), MCF7 (C) (0.001µg/ml), and human breast cancer (D) (0.0003µg/ml) tissue lysate (35µg protein in RIPA buffer) were resolved via SDS-PAGE, and the subsequent blots were probed with the chimeric rabbit version of 12D10 (Ab02843-23.0) at the mentioned respective concentrations before detection using an anti-rabbit secondary antibody. A primary incubation of 1 hour was used, and proteins were detected by chemiluminescence.
Immunofluorescence staining of MCF7 cells with anti-MUC1 antibody 12D10 (Ab02843). Immunofluorescence analysis of paraformaldehyde fixed MCF7 cells on Shi-fix™ coverslips stained with the chimeric rabbit IgG version of 12D10 (Ab02843-23.0) (1:100 dilution) for 1h followed by Alexa Fluor® 488 secondary antibody (1:1000 dilution), showing cytoplasmic staining. The nuclear stain is DAPI (blue). Panels show, from left-right, top-bottom, Ab02843-23.0, DAPI, merged channels, and an isotype control. The isotype control was an unknown specificity antibody (Ab00178-23.0) followed by staining with Alexa Fluor® 488 secondary antibody.