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Facts about Epithelial cell adhesion molecule.
Up-regulates the saying of FABP5, MYC and cyclins A and E. .
Human | |
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Gene Name: | EPCAM |
Uniprot: | P16422 |
Entrez: | 4072 |
Belongs to: |
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EPCAM family |
17-1A; 323/A3; ACSTD1; antigen identified by monoclonal AUA1; CD326 antigen; CD326; Cell surface glycoprotein Trop-1; chromosome 4, surface marker (35kD glycoprotein); DIAR5; EGP; EGP-2; EGP314; EGP40; EpCAM; epithelial cell adhesion molecule; Epithelial cell surface antigen; Epithelial glycoprotein 314; Epithelial glycoprotein; ESA; GA733-2; GA733-2EGP34; gp40; hEGP314; HNPCC8; KS 1/4 antigen; KS1/4; KSAHEA125; M1S2; M4S1; M4S1Ly74; Major gastrointestinal tumor-associated protein GA733-2; MIC18MH99; MOC31; TACST-1; TACSTD1; TROP1; TROP1CD326; Tumor-associated calcium signal transducer 1CO-17A
Mass (kDA):
34.932 kDA
Human | |
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Location: | 2p21 |
Sequence: | 2; NC_000002.12 (47369311..47387020) |
Highly and selectively expressed by undifferentiated rather than differentiated embryonic stem cells (ESC). Levels rapidly diminish as soon as ESC's differentiate (at protein levels). Expressed in almost all epithelial cell membranes but not on mesodermal or neural cell membranes. Found on the surface of adenocarcinoma.
Lateral cell membrane; Single-pass type I membrane protein. Cell junction, tight junction. Colocalizes with CLDN7 at the lateral cell membrane and tight junction.
You might be curious about whether the EPCAM marker can play an essential role in the treatment for cancer. This article will provide you with an understanding of the role that this tumor-derived analyte plays and its numerous uses in the field of cancer research. By the end of the article, you will have an understanding of the benefits of this marker and the potential to revolutionize the field of medicine. The benefits of this marker aren't limited to cancer research.
The detection of CTCs containing EpCAM has been proven to predict the outcome of cancer treatments. EpCAM has the ability to capture CTCs in a variety of cancer kinds and has strong connections with PFS and OS. For example for breast, colon, and prostate cancer, a change from a high to low CTC count following treatment is a useful indicator for prognosis. CTC analysis has many potential clinical applications, including monitoring the effectiveness of treatment in real-time and assessing metastatic relapse stratification of patients, and identification of drug targets and resistance mechanisms.
While EpCAM expression is different between cancer types and is associated with a better prognosis for HER2-positive and luminal breast cancers. Because of the diversity in molecular subtypes of cancer, EpCAM-based predictive biomarkers of cancer are not generalized in clinical studies. This could be the biggest limitation of future research examining EpCAM and CTCs.
Researchers have used commercially available antibodies to recognize EpCAM in human cancer cells. These antibodies have the benefit of avoiding the need to create feline-specific antibodies. However, they utilized mammary tumor and oropharyngeal squamous cell carcinoma cell lines. Researchers also tested antibodies against feline epithelial cells to confirm their findings.
CTC analysis cannot detect the metastasis-competent CTC population. These cells exhibit phenotypic plasticity, and can acquire migratory traits. It is important to remember that CTCs don't express EpCAM in healthy tissue. Routine CTC analysis can be used to stop or limit treatments against EpCAM.
EpCAM expression in cancer cells has been related to invasion, migration proliferative activity, as well as the expression of EpCAM. Edrecolomab is a monoclonal antibody that was made from mice and has been proven to cause complete remission of metastatic colorectal carcinoma. Due to its low affinity to EpCAM, the efficacy of edrecolomab has been questionable.
EpCAM is not present in all epithelial tissues. This makes it unlikely that it can be used as a universal marker for epithelial cancers. It was nevertheless detected in the gastric mucosa epithelium squamous. EpCAM was not expressed in epithelial pancreas cells and proximal convoluted tubes. Further studies are required to confirm EpCAM expression.
EpCAM could be used in CTC enrichment assays to help determine patients suffering from breast cancer. EpCAM has also been associated with decreased OS in many types of cancer. EpCAM regulation may provide new insights into the metastatic process. It's also a good indicator for CTC detection, as a large proportion of cancer cells are EpCAM-negative. Therefore, it is advisable to focus on the clinical application of EpCAM in the clinic.
The analysis of three cell lines showed that A549 and H358 cells were expressing high levels EpCAM. The H226 cell line also expressed low levels of the tumor cell protein. In comparison to these cell lines the efficiency of extraction for the H358 and A549 cells was quite low. In both cases, the efficiency of extraction was less than 2 percent. In the case of H358 cell line, the extraction efficiency was lower, suggesting that EpCAM cells express low levels of TTF1.
The EPCAM biomarker protein is composed of an N-terminal signal peptide, three compactly folded extracellular domains, a spanning transmembrane domain, and one c-terminal intracellular domain. It forms a heart-shaped dimer on the cell's surface. The Protein Data Base has identified the protein.
EpCAM is an transmembrane-related protein that plays a role in tumorigenesis and cancer metastasis. While the protein is not expressed in non-epithelial cancers, it is typically upregulated in tumor cells. FDA approved EpCAM-based cancer biomarkers and they are used to identify cancer cells that are circulating. EpCAM expression was observed to be high in laryngeal carcinoma, but lower in bone-marrow cancers, which has been a metastatic site for disseminated tumor cells.
The EPCAM protein is a distinctive tumor marker with profound biological properties that extend beyond intercellular adhesion. These biological properties can open new avenues for EpCAM use. As a biomarker for cancer, it can be used in liquid biopsy as a diagnostic tool in patients suffering from various types of cancer. It can be used to identify the presence of other cancerous conditions that could cause death.
The latest PE cancer biomarker is based on a novel method for investigating the immune system of an individual. In a lab setting, EVEpCAM-CD9 concentrations can aid in identifying cancer cells and make the tumor microenvironment more efficient. While this is a promising biomarker to detect cancer, it must be further tested to prove useful in clinical practice.
Boster Bio's newest cancer-fighting protein is highly expressed in a variety of types of cancer. Its expression on cancer cells is heterogeneous and has high epithelial neoplastic cell expression however, low levels of expression on CTCs which originate from solid tumors. EpCAM-positive tumors have been associated with improved survival rates in clinical studies.
Boster Bio's EPCAM biomarkers are an integral part of the treatment and clinical management of cancer. This biomarker is useful in determining the severity and stage of a patient's cancer. Furthermore, EpCAM overexpression is not related to the stage of cancer, its size or differentiation. It is not associated with TNM stage. The EpCAM transcript plays a significant role in the proliferation and differentiation of lung cancer cells. The protein is normally located on cell membranes but it is sometimes found in blood and plasma.
This groundbreaking cancer biomarker can help determine patients with an early diagnosis. It could provide the information needed to help guide treatment for cancer. The treatment for breast cancer is based on early detection and diagnosis. It is essential to detect cancerous metastases early. Biomarkers that are effective can help predict the prognosis of breast cancer. This is the reason why proteomic comparative studies are often performed on lymph nodes.
Epithelial cell adhesion mole (EpCAM), an antigen expressed on the surfaces of cancerous cells, is referred to as epithelial cell adhesion molecules. It is also known as epithelial glycoprotein 2 (EG2) 17-1A and tumor-associated calcium transducer. It is involved in cell proliferation, growth, differentiation. EpCAM is a highly effective marker to detect cancerous cells in patients.
In tumor cells, EpCAM is a highly expressed protein. It interacts with different adhesion proteins, such as CD44 and E-Cadherin. Due to its high expression, EpCAM is a promising tumor marker. It can also be utilized as a marker to determine whether a tumor is refractory to therapy or if it causes the disease to return.
In liquid biopsy, an aalyte can be detected to distinguish tumor cells from other blood cells. It allows scientists to gather information on a larger scale, at the DNA,RNA, and protein levels. Since the vast majority of cancers are epithelial in nature, targeting epithelial antigens became the first approach to discriminate cancer cells. EpCAM quickly became the most sought-after epithelial marker.
The EpCAM antibody available for sale eliminates the need for producing feline-specific antibodies. The antibody was made using two types of tumor cells , mammary tumor as well as oropharyngeal Squamous Cell carcinoma. The staining by immunohistochemical method was confirmed that the antibodies were formulated against cat tumor tissue. They can be utilized in cancer research studies using immunohistochemical methods when they are successful in staining tumor cells.
The tumor-derived analyte a-CAM contains the EpCAM protein. This protein plays a role in regulating the adhesion structures between cells and the cell-matrix. It forms a dimer that has a heart-shaped shape on the cell surface. This marker is part of the Protein Data Base (PDB).
TCF/bcatenin triggers EpCAM. The activation of the gene caused by two TCF binding elements within the promoter region. In addition, the EpCAM protein's intracellular region could interact with the TCF/b-catenin protein complex. This interaction could result in positive feedback loops for EpCAM expression. It is recommended to test this at an atomic level.
PMID: 2463074 by Strnad J., et al. Molecular cloning and characterization of a human adenocarcinoma/epithelial cell surface antigen complementary DNA.
PMID: 2469722 by Perez M.S., et al. Isolation and characterization of a cDNA encoding the KS1/4 epithelial carcinoma marker.
*More publications can be found for each product on its corresponding product page