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- Table of Contents
2 Citations 4 Q&As
1 Citations 17 Q&As
4 Citations 16 Q&As
Facts about Mucin-1.
May provide a protective layer on epithelial cells from bacterial and enzyme attack. .
Human | |
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Gene Name: | MUC1 |
Uniprot: | P15941 |
Entrez: | 4582 |
Belongs to: |
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No superfamily |
Breast carcinoma-associated antigen DF3; Carcinoma-associated mucin; CD227 antigen; CD227; DF3 antigen; EMA; Episialin; H23 antigen; H23AG; KL-6; MAM6; MUC-1; MUC1/ZD; mucin 1, cell surface associated; mucin 1, transmembrane; Mucin-1; Peanut-reactive urinary mucin; PEM; PEMMUC-1/SEC; PEMT; Polymorphic epithelial mucin; PUMMUC-1/X; tumor associated epithelial mucin; Tumor-associated epithelial membrane antigen; Tumor-associated mucin
Mass (kDA):
122.102 kDA
Human | |
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Location: | 1q22 |
Sequence: | 1; NC_000001.11 (155185824..155192915, complement) |
Expressed on the apical surface of epithelial cells, especially of airway passages, breast and uterus. Also expressed in activated and unactivated T-cells. Overexpressed in epithelial tumors, such as breast or ovarian cancer and also in non-epithelial tumor cells. Isoform Y is expressed in tumor cells only.
Apical cell membrane; Single-pass type I membrane protein. 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]: Cell membrane. Cytoplasm. Nucleus. On EGF and PDGFRB stimulation, transported to the nucleus through interaction with CTNNB1, a process which is stimulated by phosphorylation. On HRG stimulation, colocalize
As researchers, you may make use of this biomarker in order to determine the most efficient ways to utilize the product in your experiments. The benefits of this product include being capable of submitting results for species-specific samples and applications, and earning product credits for your research. This product is also available to scientists from all over the world. Here are some benefits of Boster Bio.
MUC1 is a membrane protein that exhibits hypoglycosylation core glycocans in cancer cells. Some antibodies against the MUC1 protein have ADCC properties. Others block the anti-apoptotic mechanism and reduce expression of pro-survival gene. Glycopeptide antibodies to MUC1 are powerful immunotherapies since they target specific tumor cells that express the protein.
The MUC1 molecule is expressed on the surface of cancer cells due the loss of the apicobasal Polarity. This allows it to be accessed by antibodies, which allows them to specifically target tumor-specific aberrant glycosylation, as well as carbohydrate antigens with truncated forms. Monoclonal or combination antimUC1 antibodies can be utilized to target different MUC1 domains.
The MUC1 gene encodes mucin, which is a membrane-bound protein. Mucins, also known as O-glycosylated proteins form protective mucous barriers on epithelial cells' surface and play an important role in intracellular signaling. Cell adhesion and antiadhesion properties of the mucin alpha protein subunit is provided by the mucin-alpha. The MUC1 protein is also found in epithelial cell epithelial tissues.
MUC1-targeting antibodies have a good safety profile and can be used in combination with standard chemotherapy treatments. Bispecific antibodies can also be utilized to modulate the immune system and enhance the effectiveness of cancer treatments. What is the most effective method to utilize the MUC1 Marker Monoclonal Antibody? Here are some examples. They all target the MUC1 antibody, but there isn't agreement on how they work.
Humanized MUC1–CD16-Bi is an antibody that recognizes MUC1–Mater bispecifically. This antibody was created human by the grafting of its CDRs onto the DP47 cell line. It increased the aggregation and stability of MUC1 glycoproteins at the one pole of the cell. It also increased E-cadherin-mediated cell interaction in breast cancer cell lines. Additionally, MUC1-based monoclonal antibodies increased the cytotoxic activity of lymphokine-activated killer cells.
In cancer treatment, monoclonal antibodies have many advantages. Monoclonal antibodies are stable and soluble in serum. They are affordable and can be used to treat tumors, however the cost of treatments could be more expensive. They also offer a significant improvement in survival rates over traditional chemotherapy and radiotherapy. They are an essential component of the cancer revolution and have become an essential part of the treatment.
Detailed workflow for the MUC1 marker has become a well-known tool in the detection and monitoring of various cancers. Its importance is attributed to its role in the pathogenesis of these disorders. So, the MUC1 marker is considered an important biomarker for OSCC. It is worth noting that there are some limitations to its use. To overcome these issues the procedure below is described. We hope that this guide will help you understand the workflow better.
The first step is to understand the MUC1 lectin signals from both CCA and PDAC tissue sections. The MUC1 lectin signals were normalized to the average signal intensity. The MUC1 glycan profiles from 71 patients overlapped at least partially. The MUC1 lectin profiles from 45 patients grouped the two groups into a number of clusters with distinct ancestors of the MUC1 glycoforms.
The MUC1 marker is frequently utilized in the field of immunotherapy and therapeutic clinic diagnosis. It is a protein that has multiple functions in the human body, such as acting as a decoy to mucosal pathogens as well as activating intracellular signaling pathways. We will be discussing some of the clinical applications of MUC1 in cancer. We will also look at its function in a variety of other disease states, including inflammation of the bowel and multiple sclerosis.
MUC1 is a key regulator for many cell processes like adhesion and invasion. It is controlled by numerous factors such as the growth factor receptors as well as the oestrogen receptor a (ORa). MUC1 is associated with EOC metastasis and tumor cell invasion. In cancer patients, high MUC1 levels are associated with a higher chance of developing metastatic diseases.
The MUC1 marker is a highly glycosylated protein that has two subunits. The N-terminus of MUC1 serves as a barrier against infection and the C-terminus is situated within tumor cells and is involved in signaling pathways. MUC1 also regulates the growth of tumors and invasion. The MUC1 marker plays a significant role in cancer metastasis.
MUC1's CT domain is associated with b–catenin, a transcriptional activator that regulates cell cycle progression. Its dysregulation is linked to various human malignancies. Disruption of this binding site in MUC1 inhibits its ability to promote anchorage-dependent and anchorage-independent growth, which is critical for tumorigenic activity.
While clinical trials haven't been conducted to assess the clinical implications of MUC1TM, it is possible that the protein could be used as an ovarian cancer treatment target. The high level of neoantigen has been linked to certain immune-therapy-related factors such as microsatellite instability. However, further investigation is required to fully understand the function of MUC1TM during cancer.
The MUC1 glycopeptide is associated with several inflammatory and immune responses. MUC1 is linked to a glycosyl-adjacent proteins, which makes it more resistant to degradation by glycosidases. This will not stop the MUC1 glycopeptide from being able to be a source of T cells in cancer immunotherapy. It is also known that immunosuppressive phenotypes are linked with the Glycan-optimized MUC1 Glypeptide.
The MUC1 marker is a widely used immunotherapy and therapeutic clinical diagnostic marker. The extracellular component serves as a decoy to mucosal pathogens, and also activates intracellular signaling pathways. Numerous indicators of prognosis in immunotherapy have been associated with it. Its safety and effectiveness in the clinic are being evaluated. The following review will provide additional details. This article highlights recent studies on the safety and efficacy of the MUC1 marker.
The MUC1 Nterminus is extracellular and has a highly conserved VNTR (of 20 amino acids). It is abundantly modified by O-linked glycans and acts as an physical barrier that protects the membrane of the apical cell from invasion and injury. In addition, MUC1-N plays an important role in lubrication as well as the repair of the epithelium. The protein is also essential for vascular adhesion and cancer progression.
The MUC1 molecules are involved in the invasion and migration of cancer cells. Its regulatory mechanisms are complex and redundant, however they are thought to regulate factors involved in metastasis and tumor cell invasion. The MUC1 protein also acts on the TGF-b signaling pathways, which enhances the invasive capabilities of cancer cells. The MUC1 signaling pathway regulates a variety of important immune functions and could play a major role in preventing or treating cancer.
Although the security of MUC1 isn't fully understood but it does provide many benefits. MUC1 triggers intracellular signaling pathways such as Ras/MAPK/JAK/STAT and PI3K/Akt. This activation, in turn aids in cell adhesion and tumor growth. It is important to understand that MUC1 activates the E-selection pathway and thus activating cancer cell binding.
MUC1 is a transmembrane-associated protein with an extensive O-linked glycosylation inside its extracellular domain. It plays an important role in protecting cells from infection by binding to pathogens that get to the cell's surface. It has recently been implicated in the treatment of metastatic HCC. It is available in diagnostic laboratories and medical centers across the globe.
PMID: 2394722 by Lan M.S., et al. Cloning and sequencing of a human pancreatic tumor mucin cDNA.
PMID: 2318825 by Ligtenberg M.J.L., et al. Episialin, a carcinoma-associated mucin, is generated by a polymorphic gene encoding splice variants with alternative amino termini.
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