Unconjugated Rabbit anti-Human MUC1 Polyclonal Antibody [IgG]

Breast carcinoma associated antigen DF3; Breast carcinoma associated antigen DF3; Breast carcinoma-associated antigen DF3; CA 15 3; CA 15-3; CA15 3; CA15 3 antigen; CA15.3; Cancer antigen 15-3; Carcinoma associated mucin; Carcinoma associated mucin; Carcinoma-associated mucin; CD 227; CD227; CD227; CD227 antigen; DF3 antigen; DF3 antigen; EMA; EMA; Episialin; Episialin; Epithelial membrane antigen; Epithelial membrane antigen; Epithelial mucin tandem repeat sequence; H23 antigen; H23 antigen; H23AG; H23AG; HGNC:7508; KL 6; KL-6; KL6; Krebs von den Lungen-6; MAM 6; MAM6; MUC 1; MUC 1; MUC-1; MUC-1/SEC; MUC-1/X; MUC1; MUC1-alpha; MUC1-beta; MUC1-CT; MUC1-NT; MUC1/ZD; MUC1_HUMAN; Mucin 1; Mucin 1 precursor; Mucin 1 transmembrane; Mucin-1 subunit beta; Mucin1; Mucin1; Peanut reactive urinary mucin; Peanut reactive urinary mucin; Peanut-reactive urinary mucin; PEM; PEMT; PEMT; Polymorphic epithelial mucin; Polymorphic epithelial mucin; PUM; PUM; Tumor associated epithelial membrane antigen; Tumor associated epithelial membrane antigen; Tumor associated epithelial mucin; Tumor associated mucin; Tumor associated mucin; Tumor-associated epithelial membrane antigen; Tumor-associated mucin.

MUC1 is a large cell surface mucin glycoprotein expressed by most glandular and ductal epithelial cells and some hematopoietic cell lineages. It is expressed on most secretory epithelium, including mammary gland and some hematopoietic cells. It is expressed abundantly in lactating mammary glands and overexpressed abundantly in >90% breast carcinomas and metastases. Transgenic MUC1 has been shown to associate with all four cebB receptors and localize with erbB1 (EGFR) in lactating glands. The MUC1 gene contains seven exons and produces several different alternatively spliced variants. The major expressed form of MUC1 uses all seven exons and is a type 1 transmembrane protein with a large extracellular tandem repeat domain. The tandem repeat domain is highly O glycosylated and alterations in glycosylation have been shown in epithelial cancer cells.