Anti-MUC1 antibody [M8C9] (HRP) (ab22751)

Overview

• Product nameAnti-MUC1 antibody [M8C9] (HRP)See all MUC1 primary antibodies ...
• Description
  Mouse monoclonal [M8C9] to MUC1 (HRP)
• ConjugationHRP
• Specificityab22751 reacts with VNTR5 and VNTR20 recombinant unglycosylated fragments of MUC1 protein and underglycosylated MUC1 prepared from tumor fluids or as a result of chemical treatment of human milk MUC1. Affinity > 1 x 10⁸. ab22751 does not recognise natural MUC1 protein isolated from human milk by affinity purification on carbohydrate epitope specific Mabs. No cross-reactivity with egg white avidin.
• Tested applicationsICC/IF, IHC-Fr, ELISA, Sandwich ELISA more details
• Species reactivity
  Reacts with: Human
  
• Immunogen

  Full length protein (Human). A high molecular weight, more than 300 kDa, glycoprotein from human milk-fat globule molecule.

• Epitopeab22751 binds with high efficiency with a region of GVTSAPDTRPAPGSTAPPAHGVTSA synthetic peptide, spanning the one repeat of VNTR extracellular portion of MUC1 molecule.

Properties

• FormLiquid
• Storage instructionsShipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.
• Storage bufferPreservative: 0.05% Proclin
  Constituents: PBS, pH 7.4
• Concentration information loading...
• PurityProtein A purified
• Clonality Monoclonal
• Clone numberM8C9
• Myelomax63-Ag8.653
• IsotypeIgG
• Research Areas
  • Cancer
  • Tumor immunology
  • Tumor-associated antigens

  • Cancer
  • Invasion/microenvironment
  • ECM
  • Extracellular matrix
  • MUC

  • Signal Transduction
  • Cytoskeleton / ECM
  • Extracellular Matrix
  • ECM Proteins
  • MUC

  • Tags & Cell Markers
  • Cell Type Markers
  • Tumor Associated

Applications

Target

• FunctionThe alpha subunit has cell adhesive properties. Can act both as an adhesion and an anti-adhesion protein. May provide a protective layer on epithelial cells against bacterial and enzyme attack.
  The beta subunit contains a C-terminal domain which is involved in cell signaling, through phosphorylations and protein-protein interactions. Modulates signaling in ERK, SRC and NF-kappa-B pathways. In activated T-cells, influences directly or indirectly the Ras/MAPK pathway. Promotes tumor progression. Regulates TP53-mediated transcription and determines cell fate in the genotoxic stress response. Binds, together with KLF4, the PE21 promoter element of TP53 and represses TP53 activity.
• Tissue specificityExpressed 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 7 is expressed in tumor cells only.
• Involvement in diseaseNote=MUC1/CA 15-3 is used as a serological clinical marker of breast cancer to monitor response to breast cancer treatment and disease recurrence (PubMed:20816948). Decreased levels over time may be indicative of a positive response to treatment. Conversely, increased levels may indicate disease progression. At an early stage disease, only 21% of patients exhibit high MUC1/CA 15-3 levels, that is why CA 15-3 is not a useful screening test. Most antibodies target the highly immunodominant core peptide domain of 20 amino acid (APDTRPAPGSTAPPAHGVTS) tandem repeats. Some antibodies recognize glycosylated epitopes.
• Sequence similaritiesContains 1 SEA domain.
• Developmental stageDuring fetal development, expressed at low levels in the colonic epithelium from 13 weeks of gestation.
• Post-translational
  modificationsHighly 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 (PubMed:11341784).
• Cellular localizationSecreted; Cell membrane. Cytoplasm. Nucleus. On EGF and PDGFRB stimulation, transported to the nucleus through interaction with CTNNB1, a process which is stimulated by phosphorylation. On HRG stimulation, colocalizes with JUP/gamma-catenin at the nucleus and Apical cell membrane. Exclusively located in the apical domain of the plasma membrane of highly polarized epithelial cells. After endocytosis, internalized and recycled to the cell membrane. Located to microvilli and to the tips of long filopodial protusions.

Target information above from: UniProt accession P15941 The UniProt Consortium
The Universal Protein Resource (UniProt) in 2010
Nucleic Acids Res. 38:D142-D148 (2010) .

Information by UniProt
• Database links
  • Entrez Gene: 4582 Human
  • Omim: 158340 Human
  • SwissProt: P15941 Human
  • SwissProt: P15941 Human
  • Unigene: 89603 Human

• Alternative names
  Breast carcinoma associated antigen DF3 antibodyBreast carcinoma-associated antigen DF3 antibodyCA 15 3 antibody

  CA 15-3 antibodyCA15 3 antibodyCA15 3 antigen antibodyCA15.3 antibodyCancer antigen 15-3 antibodyCarcinoma associated mucin antibodyCarcinoma-associated mucin antibodyCD 227 antibodyCD227 antibodyCD227 antigen antibodyDF3 antigen antibodyEMA antibodyEpisialin antibodyEpithelial membrane antigen antibodyEpithelial mucin tandem repeat sequence antibodyH23 antigen antibodyH23AG antibodyHGNC:7508 antibodyKL 6 antibodyKL-6 antibodyKL6 antibodyKrebs von den Lungen-6 antibodyMAM 6 antibodyMAM6 antibodyMUC 1 antibodyMUC 1 antibodyMUC-1 antibodyMUC-1/SEC antibodyMUC-1/X antibodyMUC1 antibodyMUC1-alpha antibodyMUC1-beta antibodyMUC1-CT antibodyMUC1-NT antibodyMUC1/ZD antibodyMUC1_HUMAN antibodyMucin 1 antibodyMucin 1 precursor antibodyMucin 1 transmembrane antibodyMucin-1 subunit beta antibodyMucin1 antibodyPeanut reactive urinary mucin antibodyPeanut-reactive urinary mucin antibodyPEM antibodyPEMT antibodyPolymorphic epithelial mucin antibodyPUM antibodyTumor associated epithelial membrane antigen antibodyTumor associated epithelial mucin antibodyTumor associated mucin antibodyTumor-associated epithelial membrane antigen antibodyTumor-associated mucin antibody

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