SAMD14: A Potential Drug Target and Biomarker (G201191)

Target Name: SAMD14

NCBI ID: G201191

SAMD14

Other Name(s): Sterile alpha motif domain containing 14 | Sterile alpha motif domain-containing protein 14 (isoform 1) | SAMD14 variant 1 | Sterile alpha motif domain-containing protein 14 | SAM14_HUMAN | sterile alpha motif domain containing 14 | SAM domain-containing protein 14 | Sterile alpha motif domain containing 14, transcript variant 1

SAMD14: A Potential Drug Target and Biomarker

Sterile alpha motif (SAM) domains are a class of non-coding RNA molecules that have been identified as potential drug targets in various organisms. One such domain is the SAMD14 protein, which is a key component of the cell membrane and is involved in various cellular processes. SAMD14 has been shown to play a crucial role in the regulation of ion channels and signaling pathways, making it an attractive target for drug development.

The SAMD14 protein is a 14 kDa protein that is expressed in various cell types, including cardiac muscle, skeletal muscle, and plasma cells. It is localized to the endoplasmic reticulum (ER) and has been shown to be involved in the regulation of ion channels, including the Na+/K+-ATPase, which is responsible for maintaining the resting membrane potential of the cell. The SAMD14 protein is also involved in the regulation of several signaling pathways, including the TGF-β pathway and the NF-kappa-B pathway.

SAMD14 has been shown to play a crucial role in the regulation of ion channels and signaling pathways. It is a key component of the cell membrane and is involved in the regulation of the Na+/K+-ATPase, which is responsible for maintaining the resting membrane potential of the cell. The SAMD14 protein is also involved in the regulation of several signaling pathways, including the TGF-β pathway and the NF-kappa-B pathway.

One of the key challenges in the study of SAMD14 is its difficult to study in cell-based assays, as the protein is expressed in the endoplasmic reticulum and cannot be easily purified or manipulated. This has limited the ability to study its function in a cell-based assay, which is typically used to study the function of a protein in its native environment. However, researchers have been able to study the function of SAMD14 in vitro using cell-based assays, such as patch-electrophysiology (PE) assays. These assays involve the application of a small electrical current to the cell and can be used to study the rapid changes in the electrical activity of the cell.

In addition to its role in ion channels, SAMD14 has also been shown to play a crucial role in the regulation of several signaling pathways. The TGF-β pathway is a well-established signaling pathway that is involved in the regulation of cell growth, differentiation, and survival. SAMD14 has been shown to be involved in the regulation of TGF-β signaling by interacting with the transcription factor, SMAD1.

The SAMD14 protein is also involved in the regulation of the NF-kappa-B pathway, a signaling pathway that is involved in the regulation of inflammation and cellular stress. The NF-kappa-B pathway is activated in response to various stressors, including ion channels, which can induce the production of pro-inflammatory cytokines. SAMD14 has been shown to play a role in the regulation of NF-kappa-B signaling by interacting with the transcription factor, NF-kappa-B2.

SAMD14 has also been shown to play a role in the regulation of cellular processes that are important for the development and maintenance of cancer. For example, SAMD14 has been shown to be involved in the regulation of the production of extracellular matrix (ECM) proteins, which are involved in the support and structure of cancer cells.

In conclusion, SAMD14 is a protein that has been shown to play a crucial role in the regulation of ion channels and signaling pathways. Its involvement in these processes makes it an attractive target for drug development. While the study of SAMD14 in cell-based assays has been limited, researchers have been able to study its function in vitro using these assays. Further studies are needed to fully understand the function of SAMD14 and its potential as a drug target.

Protein Name: Sterile Alpha Motif Domain Containing 14

The "SAMD14 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 SAMD14 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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