Target Name: MEP1B
NCBI ID: G4225
Review Report on MEP1B Target / Biomarker Content of Review Report on MEP1B Target / Biomarker
MEP1B
Other Name(s): PPH beta | Meprin A beta-subunit | meprin A subunit beta | N-benzoyl-L-tyrosyl-p-amino-benzoic acid hydrolase beta subunit | Meprin A subunit beta, transcript variant 1 | meprin A, beta | Endopeptidase-2 | N-benzoyl-L-tyrosyl-P-amino-benzoic acid hydrolase beta subunit | Meprin A subunit beta | endopeptidase-2 | Meprin beta | N-benzoyl-L-tyrosyl-P-amino-benzoic acid hydrolase subunit beta | Meprin A beta | MEP1B_HUMAN | Meprin B | Meprin A subunit beta (isoform 1) | MEP1B variant 1 | PABA peptide hydrolase | meprin B

Characterization of MEP1B as A Potential Drug Target Or Biomarker for Cancer

MEP1B (Mesothelin-Expresedited Protein 1B) is a protein that is expressed in various tissues throughout the body, including the placenta, mesothelial tissue, and various epithelial tissues. It is a member of the mesothelin family, which is characterized by the presence of a unique transmembrane protein called mesothelin.

MEP1B is known for its role in cell signaling and adhesion. It is a potent regulator of cell adhesion, playing a crucial role in the development and maintenance of tissue boundaries. In addition, MEP1B is involved in cell signaling, particularly in the regulation of angiogenesis , fibrosis, and cancer progression.

Despite its importance in various physiological processes, MEP1B has yet to be fully characterized as a drug target or biomarker. However, its potential role in cancer research makes it an attractive target for further investigation.

One of the key advantages of MEP1B as a drug target is its expression pattern. MEP1B is highly expressed in various tissues, including cancer, and has been shown to be involved in the development and progression of various types of cancer. This makes it an attractive target for cancer therapies that target this protein.

In addition, MEP1B has been shown to play a role in cell signaling and adhesion, making it a potential target for drugs that target these processes. For example, studies have shown that inhibiting MEP1B can lead to the breakdown of cell adhesion and an increase in cell migration, which could be a potential mechanism for the efficacy of certain anti-cancer drugs.

Another potential advantage of MEP1B as a drug target is its role in the regulation of angiogenesis. MEP1B has been shown to be involved in the regulation of angiogenesis, which is the process by which new blood vessels form in the body. This suggests that targeting MEP1B could be a potential way to treat certain types of cancer by inhibiting the formation of new blood vessels that could support the growth and progression of cancer cells.

Finally, MEP1B is also a potential biomarker for certain types of cancer. The expression of MEP1B has been shown to be associated with the development and progression of various types of cancer, including breast, ovarian, and colorectal cancers. This makes it an potential indicator for the diagnosis and prognosis of these types of cancer.

In conclusion, MEP1B is a protein that has the potential to be a drug target or biomarker for various types of cancer. Its expression pattern and involvement in cell signaling and adhesion make it an attractive target for further investigation. Further studies are needed to fully characterize

Protein Name: Meprin A Subunit Beta

Functions: Membrane metallopeptidase that sheds many membrane-bound proteins. Exhibits a strong preference for acidic amino acids at the P1' position. Known substrates include: FGF19, VGFA, IL1B, IL18, procollagen I and III, E-cadherin, KLK7, gastrin, ADAM10, tenascin-C. The presence of several pro-inflammatory cytokine among substrates implicate MEP1B in inflammation. It is also involved in tissue remodeling due to its capability to degrade extracellular matrix components

The "MEP1B Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about MEP1B comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

More Common Targets

MEPCE | MEPE | MERTK | MESD | MESP1 | MESP2 | MEST | MESTIT1 | MESTP3 | MESTP4 | MET | Metabotropic glutamate (mGluR) receptor | Metallothionein | METAP1 | METAP1D | METAP2 | Metaxin complex | Methionine adenosyltransferase | Methionine adenosyltransferase II | Methionyl aminopeptidase | Methylcytosine dioxygenase (TET) | METRN | METRNL | METTL1 | METTL13 | METTL14 | METTL15 | METTL15P1 | METTL15P2 | METTL16 | METTL17 | METTL18 | METTL21A | METTL21C | METTL21EP | METTL22 | METTL23 | METTL24 | METTL25 | METTL25B | METTL26 | METTL27 | METTL2A | METTL2B | METTL3 | METTL4 | METTL5 | METTL6 | METTL7A | METTL7B | METTL8 | METTL9 | MEX3A | MEX3B | MEX3C | MEX3D | MFAP1 | MFAP2 | MFAP3 | MFAP3L | MFAP4 | MFAP5 | MFF | MFF-DT | MFGE8 | MFHAS1 | MFN1 | MFN2 | MFNG | MFRP | MFSD1 | MFSD10 | MFSD11 | MFSD12 | MFSD13A | MFSD14A | MFSD14B | MFSD14CP | MFSD2A | MFSD2B | MFSD3 | MFSD4A | MFSD4A-AS1 | MFSD4B | MFSD4B-DT | MFSD5 | MFSD6 | MFSD6L | MFSD8 | MFSD9 | MGA | MGAM | MGAM2 | MGARP | MGAT1 | MGAT2 | MGAT3 | MGAT3-AS1 | MGAT4A | MGAT4B