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Deglycosylated Mucin

Catalog# Product Description Host Species Nature Cross reactivity Quantity Volume Price
MUC-101AP Mucin antibodies Rabbit AP r, m, h 100.0 ug 150-500 ul $245.00
FITC-MUC FITC-conjugated antibodies Rabbit FITC-AP r, m, h 100.0 ug 150-500 ul $350.00
P-MUC Antigenic blocking peptide n/a Synthetic peptide n/a 250.0 ug 100 ul $125.00
PC-MUC WB positive control for MUC n/a Protein in ready-to-use buffer n/a 0.0 ug 150 ul $185.00
Mucin 1 (Muc1) is a large transmembrane glycoprotein that is overexpressed by a majority of carcinomas. High expression of MUC1 is associated with aggressive tumors, and MUC1 antigen is used as a marker to monitor disease progression in breast cancer patients. Mucin is a mucopolysaccharidic matrix, its expression is widely varied during cell differentitiaon and inflammation. The extent of Glycosylation determines essential biological functions of epithelial mucins in conditions of health and disease. The mucin MUC1 is a candidate for use in specific immunotherapy against breast cancer. Mucin also protects the covering of gut epithelium where it is protected from proteolytic digestion by extensive glycosylation on the mucin molecule (1). The quantity and quality of mucins are also affected in inflammatory bowel disease (IBD) both because of a reduction in the number of goblet cells and a decrease in the number of sugar residues per oligosaccharide side chain (2). There are several mucin phenotypes examined in the gut (mucin 1-mucin 6), the expression of these mucin in various type of minute well-differentiated type adenocarcinoma has been examined for diagnostic purposes (3). The mucin knockout mice showed significant decrease in cholesterol uptake with no effect on fatty acif absorption (4). 
In breast cancer, overexpression of MUC1 suggest to contributes to cancer progression and metastasis. It has been shown that naturally occurring cancer preventative, indole-3-carbinol (I3C), inhibits the expression of MUC1 in breast cancer estrogen responsive and non-responsive cells (5). Unlike normal tissue where MUC exists as heavily glycosylated form, the disease- or tumor-associated MUC molecules are underglycosylated. Such underglycosylation of the core protein in cancer tissues exposes new epitopes on the cell surface that are unique to cancer tissues (6). 
 
Mucins are large glycoproteins characterized by mucin domains that show little sequence conservation and that are rich in the amino acids Ser, Thr and Pro. The sequentially-repeating nature of the core protein 20 a.a. polypeptide chain on the surface of malignant cells makes it a potential target for immunotherapy.   We have used the 20 a.a repeat sequence from the mucin protein to generate Mucin1 antibodies. This antibody was generated using a 60 mer peptide representing a repeat sequence of 20 mino acids. The antibody to this peptide recognize the mucin core protein, it is expected that this antibody eill recognize only the core protein when it is exposed due to under glyclosylation as seen in various carcinomas. FabGennix Inc. has generated epitope specific rabbit antibodies against many targets for cancer detection. These antibodies have been fully characterized for use in imminohistochemistry and western blotting applications. Limited quantities of the antigenic blocking peptide for BMP2 antibodies is also available.

For research use only, not for diagnostic or therapeutic use.

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Deglycosylated Mucin

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