This IgG1 kappa antibody was generated against recombinant human MUC1-C cytoplasmic domain (MUC1-CD) and recognizes an epitope (NYGQLDIFP) between amino acids 7 and 15.
Anti-MUC1 (CD-1) is ideal for Western Blot (WB) and Immunoprecipitation (IP) experiments.
Mucin 1 (MUC1) is aberrantly overexpressed in diverse human carcinomas and certain hematologic malignancies, and is an attractive target for drug development. MUC1 consists of two subunits; the MUC1 C-terminal (MUC1-C) subunit is an oncoprotein and cancer target. The MUC1-C subunit contains an extracellular domain, a transmembrane region, and a cytoplasmic domain. The MUC1-C cytoplasmic domain (CD) has been shown to interact with effectors such as PI3K, NF-kappaB, and Beta-Catenin which have all been linked to transformation. The MUC1-C cytoplasmic domain also contains a CQC motif necessary for dimerization, interaction with effectors, and nuclear localization. Cell-penetrating peptides and small molecules have been designed to block this site, one of which is currently in Phase I clinical evaluation. As vaccines and drugs are well under development against MUC1, antibodies will serve as useful biomarkers to define those patients who express MUC1-C and are thus likely to respond.
From the laboratory of Donald W. Kufe, MD, Dana-Farber Cancer Institute.
Part of The Investigator's Annexe program.
|Antigen:||Muc1-Cytoplasmic Domain (MUC1-CD)|
|Purification Method:||Affinity chromatograpy|
|Method Used to Determine Concentration:||Nanodrop|
|Tested Applications:||WB, IP|
|Storage:||4C (working) -20C or -80C (stock)|
Immunoblot and immunoprecipitation analyses with anti-MUC1-CD.
(A) Schematic of oncogenic MUC1-Csubunit with the 58 aa extracellular domain (ED), the 28 aatransmembrane region (TM), and the 72 aa cytoplasmic domain(CD). Highlighted are the sites for N-glycosylation inthe ED and for anti-MUC1-CD binding in the CD. (B) Lysatesfrom the indicated cell lines were immunoblotted withanti-MUC1-CD and anti-b-actin. (C) Lysates from MCF-7cells were immunoprecipitated with anti-MUC1-CD or, as acontrol, IgG. The precipitates were immunoblotted with anti-MUC1-CD.
Adapted from: Panchamoorthy G, Rehan H, Kharbanda A, Ahmad R, Kufe, D. A monoclonal antiboyd against the oncogenic mucin 1 cytoplasmic domain. Hybridoma, 30(6):531-535 (2011).
The extracellular domain is subject to glycosylation at the third asparagine residue. As such, MUC1-C in cell lysates is detectable as a broad 20-25 kDa glycosylated form.
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