Heat Shock Protein HSP2: Potential Drug Target Or Biomarker (G3306)

Target Name: HSPA2

NCBI ID: G3306

HSPA2

Heat Shock Protein HSP2: Potential Drug Target Or Biomarker

Heat shock-related 70 kDa protein 2 (HSP2) is a protein that is expressed in a variety of tissues and cells, including muscle, heart, brain, and various cell types. It is a heat shock protein (HSP), which means that it is produced in response to increased temperatures, such as those encountered during exercise or other stressful conditions.

HSP2 is a member of the HSP70 protein family, which consists of more than 20 different proteins that are expressed in a variety of tissues and cells. These proteins are involved in a variety of cellular processes, including stress response, DNA damage repair, and cell signaling.

One of the functions of HSP2 is its role in the regulation of cellular stress responses. During times of stress, such as exercise or exposure to environmental toxins, HSP2 helps to protect cells from damage caused by these stressors. This is done by increasing the stability of DNA in response to stress, as well as by regulating the expression of genes involved in stress response.

Another function of HSP2 is its role in cell signaling. HSP2 can interact with various signaling molecules, including transcription factors, to regulate the expression of genes involved in cellular signaling pathways. This is important for the regulation of cell proliferation, differentiation, and survival.

HSP2 is also involved in the regulation of inflammation. During times of inflammation, HSP2 can help to reduce the production of pro-inflammatory cytokines, which are important drivers of tissue damage and suffering. This is done by regulating the production of these cytokines by immune cells, as well as by promoting the production of anti-inflammatory cytokines.

In addition to its role in cellular stress response and inflammation, HSP2 is also involved in the regulation of cellular signaling pathways. This is done by interacting with various signaling molecules, including transcription factors, to regulate the expression of genes involved in these pathways. This is important for the regulation of cell growth, differentiation, and survival.

Given its involvement in so many cellular processes, HSP2 is a potential drug target or biomarker. For example, HSP2 has been shown to be involved in a variety of diseases, including heart disease, cancer, and neurodegenerative diseases. Additionally, HSP2 has been shown to be involved in the regulation of cellular signaling pathways, which makes it a potential target for drugs that are involved in these pathways.

In conclusion, HSP2 is a heat shock-related protein that is expressed in a variety of tissues and cells. It is involved in a variety of cellular processes, including stress response, DNA damage repair, and cell signaling, and is therefore a potential drug target or biomarker. Further research is needed to fully understand the role of HSP2 in cellular processes and its potential as a therapeutic agent.

Protein Name: Heat Shock Protein Family A (Hsp70) Member 2

Functions: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release (PubMed:26865365). Plays a role in spermatogenesis. In association with SHCBP1L may participate in the maintenance of spindle integrity during meiosis in male germ cells (By similarity)

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•   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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