Target Name: STATH
NCBI ID: G6779
Review Report on STATH Target / Biomarker Content of Review Report on STATH Target / Biomarker
STATH
Other Name(s): STATH variant 1 | STR | statherin | STAT_HUMAN | Statherin, transcript variant 1 | Statherin

Understanding STATH: A Potential Drug Target for Cancer and Other Diseases

Stath (STATH variant 1) is a protein that is expressed in various tissues of the body, including the brain, heart, lungs, and liver. It is a key regulator of the cell cycle and has been implicated in the development and progression of many diseases, including cancer. While the exact function of STATH is not well understood, research has shown that it plays a crucial role in ensuring the proper functioning of cells and has been implicated in the regulation of cellular processes that are critical for human health.

The search for new drug targets and biomarkers has led to the identification of STATH as a potential drug target. Researchers are now studying the molecular mechanisms that regulate STATH function in order to develop new treatments for a variety of diseases.

Understanding STATH

STATH is a member of the T-cell factor (TGF) family, which includes a variety of cytokines and growth factors that play important roles in the regulation of cellular processes, including cell growth, differentiation, and inflammation. The TGF family of proteins is known for their ability to regulate the cell cycle, which is the process by which cells grow, divide, and prepare for cell death.

STATH is a 21-kDa protein that is expressed in a variety of tissues, including the brain, heart, lungs, and liver. It is highly conserved, with a calculated pI of 11.95 nM and a predicted localization in the cytoplasm as a protein associated with the endoplasmic reticulum (ER). STATH is a self-regulated protein, which means that it can interact with and regulate the activity of other proteins.

The function of STATH is not well understood, but research has shown that it plays a crucial role in the regulation of the cell cycle. STATH is involved in the regulation of the G1/S transition, which is the stage of the cell cycle where the cell prepares for cell division by duplicating its genetic material and ensuring that all necessary organelles are in place for cell division.

In addition to its role in the cell cycle, STATH has also been shown to play a role in the regulation of cellular processes that are critical for human health. For example, STATH has been shown to be involved in the regulation of angiogenesis, which is the process by which new blood vessels are formed to supply oxygen and nutrients to tissues.

Drug targeting STATH

The identification of STATH as a potential drug target has led to a great deal of interest and research in the field of pharmacology. Researchers are studying the molecular mechanisms that regulate STATH function in order to develop new treatments for a variety of diseases.

One of the main challenges in targeting STATH is its high conservation, which makes it difficult to develop small molecules that can specifically interact with it. However, researchers have been able to identify a number of potential drug targets that can interact with STATH and are currently studying the molecular mechanisms that regulate its activity.

One of the most promising targets for STATH is the protein p21, which is a key regulator of the cell cycle. Researchers have shown that the p21 protein can interact with STATH and that this interaction plays a role in the regulation of the cell cycle.

Another potential drug target for STATH is the protein p53, which is a well-known regulator of the cell cycle and has been shown to interact with STATH. Researchers have shown that the p53 protein can interact with STATH and that this interaction plays a role in the regulation of the cell cycle.

Another potential drug target for STATH is the protein

Protein Name: Statherin

Functions: Salivary protein that stabilizes saliva supersaturated with calcium salts by inhibiting the precipitation of calcium phosphate salts. It also modulates hydroxyapatite crystal formation on the tooth surface

The "STATH 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 STATH 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

More Common Targets

STAU1 | STAU2 | STAU2-AS1 | STBD1 | STC1 | STC2 | STEAP1 | STEAP1B | STEAP2 | STEAP2-AS1 | STEAP3 | STEAP3-AS1 | STEAP4 | STEEP1 | Steroid 5-alpha-Reductase | Sterol O-acyltransferase (ACAT) | Sterol Regulatory Element-Binding Protein | STH | STIL | STIM1 | STIM2 | STIMATE | STIN2-VNTR | STING1 | STIP1 | STK10 | STK11 | STK11IP | STK16 | STK17A | STK17B | STK19 | STK24 | STK25 | STK26 | STK3 | STK31 | STK32A | STK32A-AS1 | STK32B | STK32C | STK33 | STK35 | STK36 | STK38 | STK38L | STK39 | STK4 | STK4-DT | STK40 | STKLD1 | STMN1 | STMN2 | STMN3 | STMN4 | STMND1 | STMP1 | STN1 | STOM | STOML1 | STOML2 | STOML3 | STON1 | STON1-GTF2A1L | STON2 | Store-operating calcium channel channels | STOX1 | STOX2 | STPG1 | STPG2 | STPG3 | STPG3-AS1 | STPG4 | STRA6 | STRA6LP | STRA8 | STRADA | STRADB | STRAP | STRBP | STRC | STRCP1 | STRIP1 | STRIP2 | STRIT1 | STRN | STRN3 | STRN4 | STS | STT3A | STT3A-AS1 | STT3B | STUB1 | STUM | STX10 | STX11 | STX12 | STX16 | STX16-NPEPL1 | STX17