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Summary This MAb recognizes full-length MUC1 in a glycosylation-independent manner and can bind to the fully glycosylated protein.The dominant epitope of this MAb is APDTR in the VNTR region. It reacts with the core peptide of the MUC1 protein, which is a member of a family of mucin glycoproteins that are characterized by high carbohydrate content, O-linked oligosaccharides, high molecular weight (200kDa) and an amino acid composition rich in serine, threonine, proline and glycine. The core protein contains a domain of 20 amino-acid tandem repeats that functions as multiple epitopes for the MAb. Incomplete glycosylation of some tumor-associated mucins may lead to variable unmasking of the multiple peptide epitopes leading to the observed differences in staining intensity between normal and malignant tissues. This MAb reacts with both normal and malignant epithelia of various tissues including breast and colon.

Summary Recognizes a 53kDa protein, which is identified as p53 suppressor gene product. It reacts with the mutant as well as the wild form of p53 under denaturing and non-denaturing conditions.

Summary In Western blotting, it reacts with two bands of ~MW of 210kDa and 300kDa, identified as two isoforms of Tenascin C. Specificity of this MAb is validated by sequential immunoprecipitation with a PAb against Tenascin C.
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Summary Recognizes a 47-55kDa-tumor suppressor protein, identified as Wilm's Tumor (WT1) protein. The antibody reacts with all isoforms of the full-length WT1 and also identifies WT1 lacking exon 2-encoded amino acids, frequently found in subsets of sporadic Wilm's tumors.