MUC1 (D9O8K) XP® Rabbit mAb #14161
- WB
- IP
- IF
- F
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 230, 400 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
- IF-Immunofluorescence
- F-Flow Cytometry
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:50 |
| Immunofluorescence (Immunocytochemistry) | 1:400 |
| Flow Cytometry (Fixed/Permeabilized) | 1:200 |
| Flow Cytometry (Live) | 1:200 |
Storage
For a carrier free (BSA and azide free) version of this product see product #20246.
Protocol
Specificity / Sensitivity
MUC1 (D9O8K) XP® Rabbit mAb detects endogenous levels of total MUC1 protein. Because this protein is heavily glycosylated, multiple bands or a smear may result from western blot analysis using this antibody.
Species Reactivity:
Human
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the amino terminus of human MUC1 protein.
Background
Mucins represent a family of glycoproteins characterized by repeat domains and dense O-glycosylation (1). MUC1 (or mucin 1) is aberrantly overexpressed in most human carcinomas. Increased expression of MUC1 in carcinomas reduces cell-cell and cell-ECM interactions. MUC1 is cleaved proteolytically, and the large ectodomain can remain associated with the small 25 kDa carboxy-terminal domain that contains a transmembrane segment and a 72-residue cytoplasmic tail (1). MUC1 interacts with ErbB family receptors and potentiates ERK1/2 activation (2). MUC1 also interacts with β-catenin, which is regulated by GSK-3β, PKCγ, and Src through phosphorylation at Ser44, Thr41, and Tyr46 of the MUC1 cytoplasmic tail (3-5). Overexpression of MUC1 potentiates transformation (6) and attenuates stress-induced apoptosis through the Akt or p53 pathways (7,8).
- Baldus, S.E. et al. (2004) Crit Rev Clin Lab Sci 41, 189-231.
- Schroeder, J.A. et al. (2001) J Biol Chem 276, 13057-64.
- Li, Y. et al. (1998) Mol Cell Biol 18, 7216-24.
- Li, Y. et al. (2001) J Biol Chem 276, 6061-4.
- Ren, J. et al. (2002) J Biol Chem 277, 17616-22.
- Schroeder, J.A. et al. (2004) Oncogene 23, 5739-47.
- Raina, D. et al. (2004) J Biol Chem 279, 20607-12.
- Wei, X. et al. (2005) Cancer Cell 7, 167-78.
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