Target Name: HSPA9P1
NCBI ID: G266724
Review Report on HSPA9P1 Target / Biomarker Content of Review Report on HSPA9P1 Target / Biomarker
HSPA9P1
Other Name(s): heat shock protein family A (Hsp70) member 9 pseudogene 1 | HSPA9BP | Heat shock 70kDa protein 9 pseudogene 1 | HSPA9P

Heat Shock Protein HSPA9P1: Potential Drug Targets

Heat shock protein (HSP) family A (Hsp70) member 9 pseudogene 1 (HSPA9P1) is a gene that encodes a protein known to play a critical role in the regulation of cellular processes that are important components of stress adaptive responses. HSPA9P1 is a key component of the HSP70 protein family, which is known to play a crucial role in the stress response of cells. HSPA9P1 functions as a protein that can interact with other proteins, including heat shock factor (HSF), which is a protein that is highly expressed in response to thermal stress.

The HSPA9P1 gene was first identified in 2007 and is located on chromosome 16 at position 7.1 kb. The gene encodes a protein that has a calculated molecular weight of 40.4 kDa and a predicted localization in the cytoplasm. HSPA9P1 is a single gene that encodes a protein that is expressed in a variety of tissues, including muscle, heart, and brain.

HSPA9P1 functions as a heat shock protein, which is a protein that is expressed in high levels in response to thermal stress, such as heat or cold shock. HSPA9P1 is involved in a variety of cellular processes that are critical for the survival and proper functioning of cells. One of the functions of HSPA9P1 is to regulate the levels of histone acetylation, which is a process that is involved in the regulation of gene expression.

HSPA9P1 has also been shown to play a role in the regulation of protein folding and stability. Studies have shown that HSPA9P1 can interact with other proteins, including the heat shock factor (HSF), which is a protein that is highly expressed in response to thermal stress. HSPA9P1 and HSF have been shown to interact and to play a role in the regulation of protein folding and stability.

In addition to its role in protein folding and stability, HSPA9P1 has also been shown to play a role in the regulation of cellular processes that are critical for the survival and proper functioning of cells. For example, studies have shown that HSPA9P1 is involved in the regulation of cell apoptosis, which is the process by which cells die when they are no longer able to maintain their normal function.

HSPA9P1 has also been shown to play a role in the regulation of cellular processes that are critical for the development and progression of diseases, such as cancer. Studies have shown that HSPA9P1 is involved in the regulation of the angiogenesis, which is the process by which new blood vessels develop in response to the growth of a tumor.

In conclusion, HSPA9P1 is a gene that encodes a protein that plays a critical role in the regulation of cellular processes that are important for the survival and proper functioning of cells. The HSPA9P1 gene has been shown to function as a heat shock protein, which is a protein that is expressed in high levels in response to thermal stress. HSPA9P1 is involved in a variety of cellular processes that are critical for the survival and proper functioning of cells, including the regulation of protein folding and stability, the regulation of cell apoptosis, and the regulation of cellular processes that are critical for the development and progression of diseases. Therefore, HSPA9P1 is a potential drug target or biomarker that could be targeted by therapeutic agents to treat a variety of diseases.

Protein Name: Heat Shock Protein Family A (Hsp70) Member 9 Pseudogene 1

The "HSPA9P1 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 HSPA9P1 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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