Unlocking the Potential of ITGA2B: A Promising Drug Target and Biomarker

Target Name: ITGA2B

NCBI ID: G3674

ITGA2B

Unlocking the Potential of ITGA2B: A Promising Drug Target and Biomarker

Introduction

ITGA2B (Protein Phosphatase 1, Regulatory Subunit 93) is a protein that plays a crucial role in cellular signaling and metabolism. Discovered in 1995, ITGA2B has been shown to regulate various cellular processes, including cell adhesion, migration, and survival. Its function as a protein phosphatase has been confirmed through various in vitro and in vivo experiments. In recent years, the research on ITGA2B has focused on its potential as a drug target and biomarker. In this article, we will explore the current understanding of ITGA2B, its potential drug targets, and its role as a biomarker in various diseases.

Current Understanding of ITGA2B

ITGA2B is a 21-kDa protein that belongs to the protein phosphatase family 1 (PP1). It is a key regulatory subunit of the PP1 enzyme, which is responsible for the phosphate orylation of various protein substrates. The N -terminus of ITGA2B contains a putative N-methylation site, which is known to play a role in post-translational modification (PTM).

In cellular signaling pathways, ITGA2B is involved in various signaling pathways, including the regulation of cell adhesion, migration, and survival. For example, ITGA2B has been shown to be involved in the regulation of cell-cell adhesion in various tissues. 7]. Additionally, ITGA2B has been shown to play a role in the regulation of cell migration and the establishment of cancer cell lines.

In addition to its role in cellular signaling, ITGA2B has also been shown to be involved in the regulation of various cellular processes, including DNA replication, apoptosis, and cellular stress.

Potential Drug Targets

ITGA2B has been identified as a potential drug target due to its various functions in cellular signaling pathways. One of the main drug targets of ITGA2B is its role in the regulation of cell adhesion, which is crucial for the development and maintenance of various tissues and organs. Therefore, compounds that can inhibit ITGA2B's function in cell adhesion may be useful for treating various diseases, such as cancer, neurodegenerative diseases, and skin diseases.

Another potential drug target of ITGA2B is its role in the regulation of cell survival and apoptosis. Prolonged exposure to various stressors, such as UV radiation, chemotherapeutic agents, and neurotoxins, can lead to the activation of cellular stress pathways and the onset of cellular stress. ITGA2B plays a role in the regulation of cellular stress through its role in the establishment of cell stress responses. Therefore, compounds that can inhibit ITGA2B's function in cellular stress may be useful for treating various diseases that are characterized by chronic stress, such as anxiety disorders and chronic pain.

In addition to its role in cell adhesion and stress, ITGA2B has also been shown to be involved in the regulation of various signaling pathways, including the regulation of cell survival and apoptosis. Therefore, compounds that can inhibit ITGA2B's function in these pathways may be useful for treating various diseases, such as neurodegenerative diseases, cancer, and cardiovascular diseases.

Biomarkers

ITGA2B has also been shown to be involved in the regulation of various biological processes, including cell adhesion, migration, and survival. Therefore, ITGA2B may be a useful biomarker for the diagnosis and monitoring of various diseases. For example, ITGA2B has been shown to be involved in the regulation of cancer cell growth and metastasis. Therefore, ITGA2B levels may be

Protein Name: Integrin Subunit Alpha 2b

Functions: Integrin alpha-IIb/beta-3 is a receptor for fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. It recognizes the sequence R-G-D in a wide array of ligands. It recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma chain. Following activation integrin alpha-IIb/beta-3 brings about platelet/platelet interaction through binding of soluble fibrinogen. This step leads to rapid platelet aggregation which physically plugs ruptured endothelial cell surface

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•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
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•   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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