MUC1 Antibody [F23K8] | Primary Antibodies

Application: Reactivity: Mouse, Rat, Human

Lane 1: T47-D, Lane 2: Mouse lung, Lane 3: Rat lung

Usage Information

Dilution
WB1:1000 - 1:5000 IP1:20 IHC1:250 - 1:500 IF1:1000 FCM1:30

Application
WB, IP, IHC, IF, FCM

Reactivity
Mouse, Rat, Human

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
122 kDa 17-25 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight.

Positive Control	Mouse lung tissue; Human colon cancer; Rat lung tissue; Normal stomach tissue; Human endometrium; Breast ductal infiltrating carcinoma tissue; Rat kidney; Mouse lung; A431 cells; MCF7 cells; T47-D cells; HeLa cells
Negative Control	Mouse liver tissue; Rat liver tissue

Datasheet & SDS

Biological Description

Specificity
MUC1 Antibody [F23K8] detects endogenous levels of total MUC1 protein.

Clone
F23K8

Synonym(s)
CD227; PUM; MUC1; Mucin-1; MUC-1; Breast carcinoma-associated antigen DF3; Cancer antigen 15-3; Carcinoma-associated mucin; Episialin; H23AG; PEMT; Polymorphic epithelial mucin; CA 15-3; KL-6; PEM; EMA

Background
MUC1 is a transmembrane mucin glycoprotein that is overexpressed in the majority of epithelial carcinomas, functioning both as a protective barrier and a central oncogenic signaling hub. It undergoes autocatalytic cleavage at its SEA module, producing two non-covalently associated subunits: the extracellular, heavily O-glycosylated N-terminal (MUC1-N), which features extensive 20-amino-acid tandem repeats and extends hundreds of nanometers from the cell surface, and the membrane-anchored C-terminal (MUC1-C), which includes a short 72-amino-acid cytoplasmic tail rich in phosphorylation sites within the TFAHY motif. These phospho-acceptor sites are targeted by kinases such as Src, GSK3β, and PKCδ, enabling recruitment of β-catenin, EGFR, and Src, and supporting the nuclear translocation of MUC1-C. MUC1-C forms complexes that transactivate ErbB, Wnt, and inflammatory pathways, promoting cell proliferation, survival, epithelial-mesenchymal transition (EMT), invasion, and angiogenesis by upregulating genes like cyclin D1, c-Myc, Bcl-xL, vimentin, and VEGF. In tumors, hypoglycosylated MUC1 exposes peptide epitopes such as PDTRPAPGSTAPPAHGVT, which are recognized by immune T-cells but can also shield the tumor from immune surveillance. Truncation variants and mutations within the SEA module can impair MUC1 cleavage and signaling, contributing to the progression of cancers such as those of the breast, prostate, and pancreas.

Background

MUC1 is a transmembrane mucin glycoprotein that is overexpressed in the majority of epithelial carcinomas, functioning both as a protective barrier and a central oncogenic signaling hub. It undergoes autocatalytic cleavage at its SEA module, producing two non-covalently associated subunits: the extracellular, heavily O-glycosylated N-terminal (MUC1-N), which features extensive 20-amino-acid tandem repeats and extends hundreds of nanometers from the cell surface, and the membrane-anchored C-terminal (MUC1-C), which includes a short 72-amino-acid cytoplasmic tail rich in phosphorylation sites within the TFAHY motif. These phospho-acceptor sites are targeted by kinases such as Src, GSK3β, and PKCδ, enabling recruitment of β-catenin, EGFR, and Src, and supporting the nuclear translocation of MUC1-C. MUC1-C forms complexes that transactivate ErbB, Wnt, and inflammatory pathways, promoting cell proliferation, survival, epithelial-mesenchymal transition (EMT), invasion, and angiogenesis by upregulating genes like cyclin D1, c-Myc, Bcl-xL, vimentin, and VEGF. In tumors, hypoglycosylated MUC1 exposes peptide epitopes such as PDTRPAPGSTAPPAHGVT, which are recognized by immune T-cells but can also shield the tumor from immune surveillance. Truncation variants and mutations within the SEA module can impair MUC1 cleavage and signaling, contributing to the progression of cancers such as those of the breast, prostate, and pancreas.

References
https://pubmed.ncbi.nlm.nih.gov/34207342/ https://pubmed.ncbi.nlm.nih.gov/15987679/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%