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Mouse Anti-MUC1 Recombinant Antibody (IHC566) (CBMAB-MA171-YC)


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Summary

Host Animal
Mouse
Specificity
Human
Clone
IHC566
Application
IHC (1:100 - 1:200)

Basic Information

Specificity
Human
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Buffer
Tris buffer pH 7.3 - 7.7, 1% BSA, < 0.1% Sodium Azide
Storage
Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C long term. Avoid freeze / thaw cycle.

Target

Full Name
Mucin 1, Cell Surface Associated
Introduction
MUC1 is a membrane-bound protein that is a member of the mucin family. Mucins are O-glycosylated proteins that play an essential role in forming protective mucous barriers on epithelial surfaces. These proteins also play a role in intracellular signaling. This protein is expressed on the apical surface of epithelial cells that line the mucosal surfaces of many different tissues including lung, breast stomach and pancreas. This protein is proteolytically cleaved into alpha and beta subunits that form a heterodimeric complex. The N-terminal alpha subunit functions in cell-adhesion and the C-terminal beta subunit is involved in cell signaling. Overexpression, aberrant intracellular localization, and changes in glycosylation of this protein have been associated with carcinomas. This gene is known to contain a highly polymorphic variable number tandem repeats (VNTR) domain.
Entrez Gene ID
4582
UniProt ID
P15941
Alternative Names
Mucin 1, Cell Surface Associated; Tumor-Associated Epithelial Membrane Antigen; Breast Carcinoma-Associated Antigen DF3; Peanut-Reactive Urinary Mucin; Polymorphic Epithelial Mucin; Carcinoma-Associated Mucin; Mucin 1, Transmembrane; Krebs Von Den Lungen-6; Cancer Antigen 15-3; Episialin; CA 15-3; H23AG; MUC-1; KL-6; PEMT; EMA; PUM; PEM;
Function
The 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.
Biological Process
DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: BHF-UCL
DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator Source: BHF-UCL
Negative regulation of cell adhesion mediated by integrin Source: CACAO
Negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: BHF-UCL
Negative regulation of transcription by competitive promoter binding Source: BHF-UCL
Positive regulation of histone H4 acetylation Source: BHF-UCL
Positive regulation of transcription from RNA polymerase II promoter in response to stress Source: BHF-UCL
Regulation of transcription from RNA polymerase II promoter in response to stress Source: BHF-UCL
Cellular Location
Plasma membrane
Apical cell membrane
Note: 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.
Isoform 5:
Secreted
Isoform Y:
Secreted
Isoform 9:
Secreted
Mucin-1 subunit beta:
Nucleus
Plasma membrane
Cell membrane
Cytoplasm
Note: 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.
Involvement in disease
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.
Tubulointerstitial kidney disease, autosomal dominant, 2 (ADTKD2):
A form of autosomal dominant tubulointerstitial kidney disease, a genetically heterogeneous disorder characterized by slowly progressive loss of kidney function, bland urinary sediment, hyperuricemia, absent or mildly increased albuminuria, lack of severe hypertension during the early stages, and normal or small kidneys on ultrasound. Renal histology shows variable abnormalities including interstitial fibrosis with tubular atrophy, microcystic dilatation of the tubules, thickening of tubular basement membranes, medullary cysts, and secondary glomerulosclerotic or glomerulocystic changes with abnormal glomerular tufting. There is significant variability, as well as incomplete penetrance.
Topology
Extracellular: 24-1158
Helical: 1159-1181
Cytoplasmic: 1182-1255
PTM
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.
More Infomation

Iverson, E., Griswold, K., Song, D., Gagliardi, T. B., Hamidzadeh, K., Kesimer, M., ... & Scull, M. A. (2022). Membrane-tethered mucin 1 is stimulated by interferon and virus infection in multiple cell types and inhibits influenza a virus infection in human airway epithelium. Mbio, 13(4), e01055-22.

Supimon, K., Sangsuwannukul, T., Sujjitjoon, J., Phanthaphol, N., Chieochansin, T., Poungvarin, N., ... & Yenchitsomanus, P. T. (2021). Anti-mucin 1 chimeric antigen receptor T cells for adoptive T cell therapy of cholangiocarcinoma. Scientific reports, 11(1), 6276.

Ballester, B., Milara, J., & Cortijo, J. (2021). The role of mucin 1 in respiratory diseases. European Respiratory Review, 30(159).

Chen, W., Zhang, Z., Zhang, S., Zhu, P., Ko, J. K. S., & Yung, K. K. L. (2021). MUC1: structure, function, and clinic application in epithelial cancers. International Journal of Molecular Sciences, 22(12), 6567.

Kashyap, B., & Kullaa, A. M. (2020). Regulation of mucin 1 expression and its relationship with oral diseases. Archives of Oral Biology, 117, 104791.

Bose, M., & Mukherjee, P. (2020). Microbe–MUC1 crosstalk in cancer-associated infections. Trends in molecular medicine, 26(3), 324-336.

Gao, T., Cen, Q., & Lei, H. (2020). A review on development of MUC1-based cancer vaccine. Biomedicine & Pharmacotherapy, 132, 110888.

Dhar, P., & McAuley, J. (2019). The role of the cell surface mucin MUC1 as a barrier to infection and regulator of inflammation. Frontiers in cellular and infection microbiology, 9, 117.

Yousefi, M., Dehghani, S., Nosrati, R., Zare, H., Evazalipour, M., Mosafer, J., ... & Ramezani, M. (2019). Aptasensors as a new sensing technology developed for the detection of MUC1 mucin: A review. Biosensors and Bioelectronics, 130, 1-19.

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For research use only. Not intended for any clinical use.

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