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MUC4(Mucin-4 alpha chain) Blocking Peptide (N-term)
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | Q99102 |
|---|
| Gene ID | 4585 |
|---|---|
| Other Names | Mucin-4, MUC-4, Ascites sialoglycoprotein, ASGP, Pancreatic adenocarcinoma mucin, Testis mucin, Tracheobronchial mucin, Mucin-4 alpha chain, Ascites sialoglycoprotein 1, ASGP-1, Mucin-4 beta chain, Ascites sialoglycoprotein 2, ASGP-2, MUC4 |
| Target/Specificity | The synthetic peptide sequence is selected from aa 529-540 of HUMAN MUC4 |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | MUC4 |
|---|---|
| Function | Membrane-bound mucin, a family of highly glycosylated proteins that constitute the major component of the mucus, the slimy and viscous secretion covering epithelial surfaces (PubMed:10880978). These glycoproteins play important roles in the protection of the epithelium and are implicated in epithelial renewal and differentiation (PubMed:10880978). Regulates cellular behavior through both anti- adhesive effects on cell-cell and cell-extracellular matrix interactions and its ability to act as an intramembrane ligand for ERBB2. Plays an important role in proliferation and differentiation of epithelial cells by inducing specific phosphorylation of ERBB2. In polarized epithelial cells, segregates ERBB2 and other ERBB receptors and prevents ERBB2 from acting as a coreceptor. The interaction with ERBB2 leads to enhanced expression of CDKN1B. The formation of a MUC4- ERBB2-ERBB3-NRG1 complex leads to down-regulation of CDKN1B, resulting in repression of apoptosis and stimulation of proliferation. Its ability to promote tumor growth may be mainly due to repression of apoptosis as opposed to proliferation. |
| Cellular Location | [Mucin-4 beta chain]: Cell membrane; Single-pass membrane protein. Note=Isoforms lacking the Cys-rich region, EGF-like domains and transmembrane region are secreted Secretion occurs by splicing or proteolytic processing [Isoform 3]: Cell membrane; Single-pass membrane protein [Isoform 15]: Secreted |
| Tissue Location | Expressed in the thymus, thyroid, lung, trachea, esophagus, stomach, small intestine, colon, testis, prostate, ovary, uterus, placenta, and mammary and salivary glands. Expressed in carcinomas arising from some of these epithelia, such as lung cancers, squamous cell carcinomas of the upper aerodigestive tract, mammary carcinomas, biliary tract, colon, and cervix cancers. Minimally or not expressed in the normal pancreas or chronic pancreatitis, but is highly expressed in pancreatic tumors and pancreatic tumor cell lines |
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Provided below are standard protocols that you may find useful for product applications.
Background
May play a role in tumor progression. Ability to promote tumor growth may be mainly due to repression of apoptosis as opposed to proliferation. Has anti-adhesive properties. Seems to alter cellular behavior through both anti-adhesive effects on cell-cell and cell-extracellular matrix interactions and in its ability to act as an intramembrane ligand for ERBB2. Plays an important role in cell proliferation and differentiation of epithelial cells by inducing specific phosphorylation of ERBB2. The MUC4-ERBB2 complex causes site-specific phosphorylation of the ERBB2 'Tyr-1248'. In polarized epithelilal cells segragates ERBB2 and other ERBB receptors and prevents ERBB2 from acting as a coreceptor. The interaction with ERBB2 leads to enhanced expression of CDKN1B. The formation of a MUC4-ERBB2-ERBB3-NRG1 complex leads to down-regulation of CDKN1B, resulting in repression of apoptosis and stimulation of proliferation.
References
Moniaux N.,et al.Eur. J. Biochem. 267:4536-4544(2000).
Choudhury A.,et al.J. Biochem. 128:233-243(2000).
Desseyn J.-L.,et al.Eur. J. Biochem. 269:3150-3159(2002).
Moniaux N.,et al.Biochem. J. 338:325-333(1999).
Escande F.,et al.Eur. J. Biochem. 269:3637-3644(2002).
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