Target Name: ST13
NCBI ID: G6767
Review Report on ST13 Target / Biomarker Content of Review Report on ST13 Target / Biomarker
ST13
Other Name(s): F10A1_HUMAN | Hsc70-interacting protein (isoform 1) | HIP | HSPABP1 | Progesterone receptor-associated p48 protein | Hsp70-interacting protein | suppression of tumorigenicity 13 protein | suppression of tumorigenicity 13 (colon carcinoma) (Hsp70 interacting protein) | progesterone receptor-associated p48 protein | renal carcinoma antigen NY-REN-33 | putative tumor suppressor ST13 | testis secretory sperm-binding protein Li 233m | Putative tumor suppressor ST13 | AAG2 | SNC6 | PRO0786 | Hsc70-interacting protein | FAM10A1 | FAM10A4 | aging-associated protein 2 | ST13 variant 1 | Renal carcinoma antigen NY-REN-33 | Hip | P48 | Aging-associated protein 2 | Protein FAM10A1 | ST13 Hsp70 interacting protein | HOP | HSPABP | heat shock 70kD protein binding protein | Suppression of tumorigenicity 13 protein | ST13 Hsp70 interacting protein, transcript variant 1 | Suppression of tumorigenicity protein 13

HSP70: A Protein Involved in Cellular Stress Response

ST13 (F10A1_HUMAN), also known as HSP70, is a protein that is expressed in various tissues throughout the body, including the heart, lungs, kidneys, and liver. It is a member of the heat shock protein (HSP) family, which are proteins that are expressed in response to increased temperatures, such as those caused by stress or exercise.

HSP70 is a protein that is involved in a variety of cellular processes, including the regulation of protein synthesis and degradation, DNA replication and repair, and cell signaling. It is also involved in the detoxification of harmful substances, such as drugs and radiation.

One of the unique features of HSP70 is its ability to form a stable complex with other proteins, known as cochymers. These complexes are thought to play a role in the regulation of cellular processes, including cell signaling and protein-protein interactions.

HSP70 has also been shown to be involved in the regulation of cellular stress responses. When cells are exposed to stressors, such as drugs or radiation, HSP70 can help to prevent the damage caused by these stressors by forming a stable complex with other proteins.

Despite its involvement in cellular stress responses, HSP70 is not a drug target or biomarker. However, research into its functions and interactions with other proteins may provide insights into the mechanisms underlying cellular stress responses and the potential therapeutic uses of drugs that target these processes.

Overall, HSP70 is a protein that is expressed in various tissues throughout the body and is involved in a variety of cellular processes. While it is not currently a drug target or biomarker, research into its functions and interactions with other proteins may provide insights into the mechanisms underlying cellular stress responses and the potential therapeutic uses of drugs that target these processes.

Protein Name: ST13 Hsp70 Interacting Protein

Functions: One HIP oligomer binds the ATPase domains of at least two HSC70 molecules dependent on activation of the HSC70 ATPase by HSP40. Stabilizes the ADP state of HSC70 that has a high affinity for substrate protein. Through its own chaperone activity, it may contribute to the interaction of HSC70 with various target proteins (By similarity)

The "ST13 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 ST13 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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