MUC1 Recombinant Rabbit Monoclonal Antibody [SN06-80] (ET1611-14)

UNIPROT #

P15941

PROTEIN NAME

MUC1

SYNONYMS

ADMCKD antibody;ADMCKD1 antibody;Breast carcinoma associated antigen DF3 antibody;Breast carcinoma-associated antigen DF3 antibody;CA 15-3 antibody;CA15 3 antibody;CA15 3 antigen antibody;CA15.3 antibody;Cancer antigen 15-3 antibody;Carcinoma associated mucin antibody;Carcinoma-associated mucin antibody;CD 227 antibody;CD227 antibody;DF3 antigen antibody;EMA antibody;Episialin antibody;H23 antigen antibody;H23AG antibody;KL 6 antibody;KL-6 antibody;KL6 antibody;Krebs von den Lungen-6 antibody;MAM 6 antibody;MAM6 antibody;MCD antibody;MCKD antibody;MCKD1 antibody;Medullary cystic kidney disease 1 (autosomal dominant) antibody;Medullary cystic kidney disease, autosomal dominant antibody;MUC 1 antibody;MUC-1 antibody;MUC-1/SEC antibody;MUC-1/X antibody;MUC1 antibody;MUC1-alpha antibody;MUC1-beta antibody;MUC1-CT antibody;MUC1-NT antibody;MUC1/ZD antibody;MUC1_HUMAN antibody;Mucin 1 antibody;Mucin 1 transmembrane antibody;Mucin 1, cell surface associated antibody;Mucin-1 subunit beta antibody;Peanut reactive urinary mucin antibody;Peanut-reactive urinary mucin antibody;PEM antibody;PEMT antibody;Polymorphic epithelial mucin antibody;PUM antibody;Tumor associated epithelial membrane antigen antibody;Tumor associated epithelial mucin antibody;Tumor associated mucin antibody;Tumor-associated epithelial membrane antigen antibody;Tumor-associated mucin antibody

TISSUE SPECIFICITY

Expressed on the apical surface of epithelial cells, especially of airway passages, breast and uterus. Also expressed in activated and unactivated T-cells. Overexpressed in epithelial tumors, such as breast or ovarian cancer and also in non-epithelial tumor cells. Isoform Y is expressed in tumor cells only.

DEVELOPMENTAL STAGE

During fetal development, expressed at low levels in the colonic epithelium from 13 weeks of gestation.

POST-TRANSLATIONAL MODIFICATION

Highly glycosylated (N- and O-linked carbohydrates and sialic acid). O-glycosylated to a varying degree on serine and threonine residues within each tandem repeat, ranging from mono- to penta-glycosylation. The average density ranges from about 50% in human milk to over 90% in T47D breast cancer cells. Further sialylation occurs during recycling. Membrane-shed glycoproteins from kidney and breast cancer cells have preferentially sialyated core 1 structures, while secreted forms from the same tissues display mainly core 2 structures. The O-glycosylated content is overlapping in both these tissues with terminal fucose and galactose, 2- and 3-linked galactose, 3- and 3,6-linked GalNAc-ol and 4-linked GlcNAc predominating. Differentially O-glycosylated in breast carcinomas with 3,4-linked GlcNAc. N-glycosylation consists of high-mannose, acidic complex-type and hybrid glycans in the secreted form MUC1/SEC, and neutral complex-type in the transmembrane form, MUC1/TM.; Proteolytic cleavage in the SEA domain occurs in the endoplasmic reticulum by an autoproteolytic mechanism and requires the full-length SEA domain as well as requiring a Ser, Thr or Cys residue at the P + 1 site. Cleavage at this site also occurs on isoform MUC1/X but not on isoform MUC1/Y. Ectodomain shedding is mediated by ADAM17.; Dual palmitoylation on cysteine residues in the CQC motif is required for recycling from endosomes back to the plasma membrane.; Phosphorylated on tyrosines and serine residues in the C-terminal. Phosphorylation on tyrosines in the C-terminal increases the nuclear location of MUC1 and beta-catenin. Phosphorylation by PKC delta induces binding of MUC1 to beta-catenin/CTNNB1 and thus decreases the formation of the beta-catenin/E-cadherin complex. Src-mediated phosphorylation inhibits interaction with GSK3B. Src- and EGFR-mediated phosphorylation on Tyr-1229 increases binding to beta-catenin/CTNNB1. GSK3B-mediated phosphorylation on Ser-1227 decreases this interaction but restores the formation of the beta-cadherin/E-cadherin complex. On T-cell receptor activation, phosphorylated by LCK. PDGFR-mediated phosphorylation increases nuclear colocalization of MUC1CT and CTNNB1.; The N-terminal sequence has been shown to begin at position 24 or 28.

SUBCELLULAR LOCATION

Apical cell membrane, Secreted, Cell membrane, Cytoplasm, Nucleus.

FUNCTION

Mucin 1, cell surface associated (MUC1), also called polymorphic epithelial mucin (PEM) or epithelial membrane antigen or EMA, is a mucin encoded by the MUC1 gene in humans. MUC1 is a glycoprotein with extensive O-linked glycosylation of its extracellular domain. Mucins line the apical surface of epithelial cells in the lungs, stomach, intestines, eyes and several other organs. Mucins protect the body from infection by pathogen binding to oligosaccharides in the extracellular domain, preventing the pathogen from reaching the cell surface. Overexpression of MUC1 is often associated with colon, breast, ovarian, lung and pancreatic cancers.