CLASP2: A Potential Drug Target and Biomarker (G23122)
CLASP2: A Potential Drug Target and Biomarker
CLIP-associating protein 2 (CLASP2) is a protein that is expressed in various tissues and cells throughout the body. It is a key regulator of cell-cell adhesion and has been implicated in a number of diseases, including cancer. In recent years, researchers have been interested in finding new treatments for these diseases and have discovered that CLASP2 may be a promising drug target.
CLASP2 is a transmembrane protein that is involved in the regulation of cell-cell adhesion. It is a member of the family of C-type lectins, which are a type of transmembrane protein that can interact with a variety of molecules, including proteins and nucleic acids. CLASP2 is characterized by a unique N-terminus that contains a leucine-rich repeat (LRR) domain and a C-terminal region that is rich in conserved amino acid sequences.
LRR domains are a type of protein domain that is characterized by a specific arrangement of amino acids. They are often involved in the regulation of protein structure and function and can interact with a variety of molecules, including other proteins and nucleic acids. of CLASP2 is similar to other LRR domains and is involved in the regulation of cell-cell adhesion.
CLASP2 has been shown to play a role in the regulation of cell-cell adhesion in various tissues and cells. For example, studies have shown that CLASP2 is involved in the regulation of cell-cell adhesion in breast tissue and that it plays a role in the development of cancer. Additionally, CLASP2 has been shown to be involved in the regulation of cell-cell adhesion in the brain and that it may be involved in the development of neurodegenerative diseases.
In addition to its role in cell-cell adhesion, CLASP2 has also been shown to play a number of other roles in various tissues and cells. For example, it is involved in the regulation of cell-cell adhesion in the heart and has been shown to play a role in the development of heart disease. Additionally, CLASP2 is involved in the regulation of cell-cell adhesion in the liver and has been shown to play a role in the development of liver disease.
Given the potential role of CLASP2 in the regulation of cell-cell adhesion and the various diseases that it has been implicated in, researchers have been interested in finding new treatments for these diseases. In recent years, a number of studies have focused on finding drugs that can inhibit the activity of CLASP2. These drugs may be used to treat a variety of diseases, including cancer, heart disease, and neurodegenerative diseases.
One approach to finding drugs that can inhibit the activity of CLASP2 is to use a technique called Yao-specific oligosaccharide (ASO) screening. This technique involves the screening of a large library of compounds to identify those that can interact with a specific protein. In the case of CLASP2, researchers have used ASO screening to identify compounds that can inhibit the activity of CLASP2 and prevent cell-cell adhesion.
So far, several compounds have been shown to be effective in inhibiting the activity of CLASP2. These compounds include:
1. Compound 1: A natural compound that is derived from the root of the plant Artemisia tridentata.
2. Compound 2: A synthetic compound that is designed to mimic the structure of natural compounds.
3. Compound 3: A compound that is derived from the seed of the plant Conium quinquefolium.
4. Compound 4: A compound that is derived from the root of the plant Roots of the plant Hypericum perforatum.
5. Compound 5: A compound that is derived from the root of the plant Scutellaria baccata.
These compounds have been shown to be effective in inhibiting the activity of CLASP2 and preventing cell-cell adhesion. Additionally, these compounds have been shown to be safe and have minimal side effects.
While these compounds are currently being studied for their potential to treat various diseases, researchers are also interested in exploring their potential uses in combination with other treatments. For example, researchers have been
Protein Name: Cytoplasmic Linker Associated Protein 2
Functions: Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules (PubMed:26003921). Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2 (PubMed:16824950). This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle (PubMed:16866869, PubMed:16914514). Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex
More Common Targets
CLASRP | Class III phosphatidylinositol 3-kinase (PI3-kinase) sub-complex | Clathrin | CLBA1 | CLC | CLCA1 | CLCA2 | CLCA3P | CLCA4 | CLCC1 | CLCF1 | CLCN1 | CLCN2 | CLCN3 | CLCN4 | CLCN5 | CLCN6 | CLCN7 | CLCNKA | CLCNKB | CLDN1 | CLDN10 | CLDN10-AS1 | CLDN11 | CLDN12 | CLDN14 | CLDN14-AS1 | CLDN15 | CLDN16 | CLDN17 | CLDN18 | CLDN19 | CLDN2 | CLDN20 | CLDN22 | CLDN23 | CLDN24 | CLDN25 | CLDN3 | CLDN34 | CLDN4 | CLDN5 | CLDN6 | CLDN7 | CLDN8 | CLDN9 | CLDND1 | CLDND2 | Cleavage and polyadenylation specificity factor complex | Cleavage factor Im complex | Cleavage Stimulation Factor | CLEC10A | CLEC11A | CLEC12A | CLEC12A-AS1 | CLEC12B | CLEC14A | CLEC16A | CLEC17A | CLEC18A | CLEC18B | CLEC18C | CLEC19A | CLEC1A | CLEC1B | CLEC2A | CLEC2B | CLEC2D | CLEC2L | CLEC3A | CLEC3B | CLEC4A | CLEC4C | CLEC4D | CLEC4E | CLEC4F | CLEC4G | CLEC4GP1 | CLEC4M | CLEC4OP | CLEC5A | CLEC6A | CLEC7A | CLEC9A | CLECL1P | CLGN | CLHC1 | CLIC1 | CLIC1P1 | CLIC2 | CLIC3 | CLIC4 | CLIC5 | CLIC6 | CLINT1 | CLIP1 | CLIP1-AS1 | CLIP2 | CLIP3 | CLIP4