Mucin-1(Ser24-Pro146)

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100ug, 50ug

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Product nameMucin-1(Ser24-Pro146)
Uniprot IDP15941
Origin speciesHomo sapiens (Human)
Expression systemProkaryotic expression
SequenceMGSSHHHHHHSSGLVPRGSHMSGHASSTPGGEKETSATQRSSVPSSTEKNAVSMTSSVLSSHSPGSGSSTTQGQDVTLAPATEPASGSAATWGQDVTSVPVTRPALGSTTPPAHDVTSAPDNKPAPGSTAPPAHGVTSAPDTRP
Molecular weight14.25 kDa
Protein delivered with Tag?N-terminal His Tag
Purity estimated>90%by SDS-PAGE
BufferPBS pH 7.5
Delivery conditionDry Ice
Delivery lead time in business daysEurope: 5-7 working days
USA & Canada: 7-10 working days
Rest of the world: 5-12 working days
Storage condition4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection)
BrandProteoGenix
Host speciesEscherichia coli (E.coli)
Fragment TypeSer24-Pro146
Aliases /SynonymsMUC-1,Breast carcinoma-associated antigen DF3,Cancer antigen 15-3,CA 15-3,Carcinoma-associated mucin,Episialin,H23AG,Krebs von den Lungen-6,KL-6 ,PEMT,Peanut-reactive urinary mucin,PUM,Polymorphic epithelial mucin,PEM,Tumor-associated epithelial membrane antigen,EMA,Tumor-associated mucin ,CD_antigen: CD227
ReferencePX-P4730
NoteFor research use only

Description of Mucin-1(Ser24-Pro146)

The Structure of Mucin-1(Ser24-Pro146)

Mucin-1(Ser24-Pro146) is a protein that is encoded by the MUC1 gene and is found on the surface of epithelial cells. It is a large, heavily glycosylated protein with a molecular weight of approximately 200 kDa. The protein is composed of two subunits, an extracellular subunit and a transmembrane subunit, connected by a short cytoplasmic tail.

The extracellular subunit of Mucin-1(Ser24-Pro146) is made up of a variable number of tandem repeats (VNTRs) of a 20 amino acid sequence, rich in proline, threonine, and serine residues. These repeats are heavily glycosylated, making up more than 50% of the protein’s mass. The glycosylation pattern of these repeats is highly variable, leading to a high degree of heterogeneity in the protein.

The transmembrane subunit of Mucin-1(Ser24-Pro146) is composed of a single transmembrane helix and a short cytoplasmic tail. This subunit is responsible for anchoring the protein to the cell membrane.

The Activity of Mucin-1(Ser24-Pro146)

Mucin-1(Ser24-Pro146) is primarily known for its role in providing protection and lubrication to epithelial cells. The heavily glycosylated extracellular subunit of the protein forms a gel-like layer on the surface of cells, protecting them from mechanical stress and preventing pathogens from adhering to the cell surface.

In addition to its protective function, Mucin-1(Ser24-Pro146) also plays a role in cell signaling. The cytoplasmic tail of the protein contains multiple tyrosine residues that can be phosphorylated, leading to the activation of various signaling pathways. This allows Mucin-1(Ser24-Pro146) to regulate processes such as cell proliferation, differentiation, and apoptosis.

The Role of Mucin-1(Ser24-Pro146) as a Drug Target

The unique structure and activity of Mucin-1(Ser24-Pro146) make it an attractive target for drug development. Due to its high expression on the surface of many cancer cells, Mucin-1(Ser24-Pro146) has been extensively studied as a potential target for cancer therapy.

One approach to targeting Mucin-1(Ser24-Pro146) is through the use of monoclonal antibodies. These antibodies can specifically bind to the extracellular subunit of the protein, disrupting its protective function and potentially triggering immune responses against cancer cells.

Another strategy is to target the cytoplasmic tail of Mucin-1(Ser24-Pro146). Inhibition of the phosphorylation of this region has been shown to decrease cell proliferation and induce cell death in cancer cells, making it a promising target for anti-cancer drugs.

The Potential Applications of Mucin-1(Ser24-Pro146) in Medicine

In addition to its potential as a drug target, Mucin-1(Ser24-Pro146) has other potential applications in medicine. The protein’s ability to form a protective layer on the surface of cells has led to its use in the development of artificial mucous membranes for medical purposes, such as wound healing and tissue engineering.

Furthermore, the unique glycosylation pattern of Mucin-1(Ser24-Pro146) has been found to be altered in various diseases, including cancer and inflammatory conditions. This makes it a potential biomarker for disease diagnosis and monitoring.

Conclusion

In summary, Mucin-1(Ser24-Pro146) is a large, heavily glycosylated protein that plays a crucial role in protecting and signaling in epithelial cells. Its unique structure and activity make it a potential drug target for cancer therapy, and it also has potential applications in other areas of medicine, such as tissue engineering and disease diagnosis.

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