Target Name: PGLYRP2
NCBI ID: G114770
Review Report on PGLYRP2 Target / Biomarker Content of Review Report on PGLYRP2 Target / Biomarker
PGLYRP2
Other Name(s): TAGL-like | N-acetylmuramoyl-L-alanine amidase | Tagl-beta | Peptidoglycan recognition protein 2 precursor | PGLYRP2 variant 2 | peptidoglycan recognition protein 2 | Peptidoglycan recognition protein 2, transcript variant 2 | tagL | peptidoglycan recognition protein long | peptidoglycan recognition protein L | PGLYRPL | TagL-alpha | N-acetylmuramoyl-L-alanine amidase isoform 2 precursor (isoform 2) | tagL-alpha | PGRP2_HUMAN | HMFT0141 | Peptidoglycan recognition protein 2 | PGRPL | Peptidoglycan recognition protein long | TagL | Peptidoglycan recognition protein L | PGRP-L | Peptidoglycan recognition protein-like | tagl-beta | PGLYRP2 variant 1 | N-acetylmuramoyl-L-alanine amidase (isoform 1) | Peptidoglycan recognition protein 2, transcript variant 1

Understanding PGLYRP2: A Potential Drug Target and Biomarker

PGLYRP2 (Proteasome-glutamylated lysine-2-protein) is a protein that is expressed in almost all human tissues and is involved in various cellular processes. PGLYRP2 has been identified as a potential drug target and a biomarker for various diseases, including cancer, neurodegenerative diseases, and autoimmune disorders.

The protein PGLYRP2 is composed of 198 amino acid residues and has a calculated molecular mass of 21.1 kDa. PGLYRP2 is a member of the proteasome family of proteins, which are involved in the processing and degradation of various proteins in the cell. PGLYRP2 is characterized by its unique post-translational modification, which involves the addition of a lysine residue to its protein via theja reaction.

The addition of this lysine residue to PGLYRP2 has important implications for its function and has been the subject of intense research. Lysine residues are known for their role in various cellular processes, including cell signaling, protein-protein interactions, and DNA binding. of a lysine residue to PGLYRP2 may have implications for its protein function and contribute to its unique structure and stability.

PGLYRP2 has been shown to play a role in various cellular processes, including cell signaling, DNA replication, and protein degradation. For example, PGLYRP2 has been shown to be involved in the regulation of the T-cell receptor (TCR), a protein that plays a critical role in cell signaling and immune response.

In addition to its role in cell signaling, PGLYRP2 has also been shown to be involved in the regulation of DNA replication. PGLYRP2 has been shown to interact with the protein responsible for regulating DNA replication, called MLL-1 (MutL homolog 1). This The interaction between PGLYRP2 and MLL-1 has important implications for the regulation of DNA replication and may contribute to the development of cancer.

PGLYRP2 has also been shown to play a role in protein degradation. PGLYRP2 has been shown to interact with the protein responsible for the degradation of the protein (ubiquitin), a protein that is involved in the regulation of protein levels in the cell. This interaction between PGLYRP2 and ubiquitin has important implications for the regulation of protein levels and may contribute to the development of neurodegenerative diseases.

In addition to its role in cell signaling and protein degradation, PGLYRP2 has also been shown to play a role in the regulation of inflammation. PGLYRP2 has been shown to interact with the protein responsible for the regulation of inflammation, called NF-kappa-B (nuclear factor kappa B). This interaction between PGLYRP2 and NF-kappa-B has important implications for the regulation of inflammation and may contribute to the development of autoimmune disorders.

The post-translational modification of PGLYRP2, in which a lysine residue is added to the protein via theja reaction, has important implications for its function and has been the subject of intense research. The addition of a lysine residue to PGLYRP2 may have implications for its stability and function, and may contribute to the development of various diseases.

In conclusion, PGLYRP2 is a protein that is involved in various cellular processes and has been identified as a potential drug target and biomarker for various diseases. The unique post-translational modification of PGLYRP2, in which a lysine residue is added to the protein via theja reaction, has important implications for its function and has been the subject of intense research. Further studies are needed to fully understand the role of PGLYRP2 in cell signaling and protein degradation, as well as its potential as a drug target and biomarker for various diseases.

Protein Name: Peptidoglycan Recognition Protein 2

Functions: May play a scavenger role by digesting biologically active peptidoglycan (PGN) into biologically inactive fragments. Has no direct bacteriolytic activity

The "PGLYRP2 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 PGLYRP2 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

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