HSP13: A Protein for Cellular Heat Stress Response and Drug Development

Target Name: HSPA13

NCBI ID: G6782

HSPA13

Other Name(s): Heat shock protein family A (Hsp70) member 13 | Heat shock 70 kDa protein 13 | Microsomal stress-70 protein ATPase core | stress 70 protein chaperone, microsome-associated, 60kDa | Stress-70 protein chaperone microsome-associated 60 kDa protein | heat shock protein 70kDa family, member 13 | stress-70 protein chaperone microsome-associated 60 kDa protein | stress 70 protein chaperone, microsome-associated, 60kD | testis secretory sperm-binding protein Li 199a | heat shock protein family A (Hsp70) member 13 | HSP13_HUMAN | STCH | microsomal stress 70 protein ATPase core | Microsomal stress 70 protein ATPase core

HSP13: A Protein for Cellular Heat Stress Response and Drug Development

Heat shock protein (HSP) family is a class of proteins that play an important role in cellular heat stress response. The HSP70 family is the largest of the HSP families, containing approximately 200 members. Among them, HSP13 is a member of the HSP70 family and is a protein that plays an important role in cellular heat stress response.

HSP13 is a heat shock protein that is induced when cells undergo heat stress. The main function of HSP13 is to help cells maintain protein stability in high-temperature environments and prevent protein denaturation, aggregation and other adverse changes under high-temperature conditions. HSP13 maintains its stable three-dimensional structure by binding to hydrogen bonds, hydrogen bonds, and hydrophobic interactions on other proteins.

HSP13 plays an important role in cellular heat stress response. Under high temperature conditions, many biomolecules in cells will be denatured, resulting in serious disturbance of the intracellular environment. HSP13 helps cells maintain protein stability, thereby mitigating this effect. HSP13 can also combine with hydrogen bonds on other proteins to form complex protein-protein interactions, thereby enhancing the stability of intracellular proteins.

HSP13 is of high value in drug development. Because HSP13 plays an important role in cellular heat stress response, scientists are exploring the possibility of HSP13 as a drug target or biomarker. Some studies have shown that HSP13 can be used as a potential drug target for the treatment of heat illness. For example, the expression level of HSP13 is increased in disease models related to heat shock response in pig models, which can alleviate the impact of heat shock on pigs by inhibiting the activity of HSP13.

In addition, HSP13 can also be used as a potential target in tumor treatment. Because HSP13 is also expressed in tumor cells, scientists are exploring HSP13 as a potential target in tumor treatment. Studies have shown that the expression level of HSP13 is positively correlated with tumor invasion and metastasis. Therefore, HSP13 has attracted much attention as a potential tumor treatment target.

HSP13 is a protein that plays an important role in cellular heat stress response. HSP13 is of high value in both drug development and tumor treatment. Future research will continue to further explore the role of HSP13 in cellular heat stress response and provide new ideas and strategies for the treatment of heat diseases, tumors and other diseases.

Protein Name: Heat Shock Protein Family A (Hsp70) Member 13

Functions: Has peptide-independent ATPase activity

The "HSPA13 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 HSPA13 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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