Target Name: TRAJ42
NCBI ID: G28713
Review Report on TRAJ42 Target / Biomarker Content of Review Report on TRAJ42 Target / Biomarker
TRAJ42
Other Name(s): T cell receptor alpha joining 42

Traj42: A Key Protein in T Cell Receptor Function

Traj42, also known as T cell receptor alpha- joining 42, is a protein that is expressed in T cells, a type of white blood cell that plays a crucial role in the immune system. T cells are responsible for recognizing and responding to foreign substances in the body, and their primary response is to destroy infected or abnormal cells. Traj42 is a key component of the T cell receptor, which is a protein that recognizes specific molecules on the surface of a cell.

The T cell receptor is composed of a伪尾尾 structure, with each subunit composed of a transmembrane domain and a cytoplasmic tail. The 伪 subunit consists of two distinct domains: an extracellular domain that is involved in cell adhesion and clustering, and an intracellular domain that contains the T cell receptor alpha- joining 42.

Traj42 is a 21-kDa protein that is located in the cytoplasmic tail of the 伪 subunit. It consists of 120 amino acid residues and has a molecular weight of 19.5 kDa. Traj42 is involved in the clustering and adhesion of T cells, as well as the regulation of their subsetting and activation.

One of the functions of Traj42 is to interact with the protein PD-L1. PD-L1 is a negative regulator of the T cell receptor, and it can prevent T cells from recognizing and responding to foreign substances on the surface of a cell. Traj42 has been shown to interact with PD-L1 and to regulate the activity of PD-L1.

Another function of Traj42 is its role in T cell subsetting. T cells are characterized by their ability to subset into different functional subpopulations based on the expression of specific antigens. Traj42 is involved in the regulation of this process, as it has been shown to interact with the protein PD-L1 and to influence the expression of genes involved in T cell subsetting.

In addition to its role in T cell subsetting, Traj42 is also involved in the regulation of T cell activation. T cells are activated when they recognize an antigen that is specific for their surface receptors, and Traj42 is involved in the regulation of this process. Traj42 has been shown to interact with the protein PD-L1 and to influence the activity of PD-L1, which is known to suppress T cell activation.

Traj42 has also been shown to be involved in the regulation of T cell death. T cells are a critical part of the immune system, and they are responsible for responding to foreign substances in the body. However, they are also prone to apoptosis, which is the process by which a cell dies naturally. Traj42 is involved in the regulation of T cell death, as it has been shown to interact with the protein PD-L1 and to influence the activity of PD-L1.

In conclusion, Traj42 is a protein that is expressed in T cells and is involved in the regulation of several important functions in the immune system. Its role in T cell subsetting, activation, and death makes it an attractive drug target and a potential biomarker for the development of cancer therapies. Further research is needed to fully understand the mechanisms of Traj42's function in the immune system and to explore its potential as a drug.

Protein Name: T Cell Receptor Alpha Joining 42

Functions: J region of the variable domain of T cell receptor (TR) alpha chain that participates in the antigen recognition (PubMed:24600447). Alpha-beta T cell receptors are antigen specific receptors which are essential to the immune response and are present on the cell surface of T lymphocytes. Recognize peptide-major histocompatibility (MH) (pMH) complexes that are displayed by antigen presenting cells (APC), a prerequisite for efficient T cell adaptive immunity against pathogens (PubMed:25493333). Binding of alpha-beta TR to pMH complex initiates TR-CD3 clustering on the cell surface and intracellular activation of LCK that phosphorylates the ITAM motifs of CD3G, CD3D, CD3E and CD247 enabling the recruitment of ZAP70. In turn, ZAP70 phosphorylates LAT, which recruits numerous signaling molecules to form the LAT signalosome. The LAT signalosome propagates signal branching to three major signaling pathways, the calcium, the mitogen-activated protein kinase (MAPK) kinase and the nuclear factor NF-kappa-B (NF-kB) pathways, leading to the mobilization of transcription factors that are critical for gene expression and essential for T cell growth and differentiation (PubMed:23524462). The T cell repertoire is generated in the thymus, by V-(D)-J rearrangement. This repertoire is then shaped by intrathymic selection events to generate a peripheral T cell pool of self-MH restricted, non-autoaggressive T cells. Post-thymic interaction of alpha-beta TR with the pMH complexes shapes TR structural and functional avidity (PubMed:15040585)

The "TRAJ42 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 TRAJ42 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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