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- Table of Contents
Facts about Transient receptor potential cation channel subfamily V member 2.
May transduce physical stimuli in mast cells. Activated by temperatures greater than 52 degrees Celsius; is not activated by vanilloids and acidic pH.
Mouse | |
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Gene Name: | Trpv2 |
Uniprot: | Q9WTR1 |
Entrez: | 22368 |
Belongs to: |
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transient receptor (TC 1.A.4) family |
Osm-9-like TRP channel 2; transient receptor potential cation channel, subfamily V, member 2; TrpV2; Vanilloid receptor-like protein 1; VRL-1MGC12549; VRL1transient receptor potential cation channel subfamily V member 2; VRLOTRPC2
Mass (kDA):
85.965 kDA
Mouse | |
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Location: | 11|11 B2 |
Sequence: | 11; |
Abundantly expressed in spleen, placenta, skeleton muscle, lung and brain.
Developed in 1993, the TRPV2 marker has become one of the most common markers in the field of OC and transfections. Boster Bio's TRPV2 ELISA kit delivers high sensitivity and specificity. Read on to learn how this marker can help you improve the sensitivity and specificity of your experiments. We will also talk about its applications in OC.
TRPV2 is a protein expressed by the receptors in the central nervous system. This marker can be used to study a wide variety of human diseases, including inflammatory bowel disease, cancer, and neurodegenerative diseases. TRPV2 is overexpressed in cancer cells, but not in normal tissues. Transfections were done with small interfering RNA, or siRNA. In this study, the plasmid containing TRPV2 was transfected into MDA-MB231 cells. Afterward, the cells were treated with CBD or DOX (5 mM) for two hours. Cells were then analyzed using the MTT assay.
Activation of TRPV2 enhances DOX-mediated effects in breast cancer cells. In one study, TRPV2 overexpressing cells had higher drug uptake than the cells transfected with an empty vector. This finding suggests that the TRPV2 protein is involved in the uptake of chemotherapeutic drugs. But the best uses of the TRPV2 protein are in cancer research.
TRPV2 is a member of the TRPV family of proteins. It responds to noxious heat, cell membrane stretch, and changes in osmolarity. CBD, a compound found in marijuana, activates the TRPV2 channel and translocates towards the plasma membrane. CBD has been shown to have anti-proliferative properties against breast cancer cells.
TNBC is a subtype of breast cancer that lacks HER-2 or hormonal receptors. Its first-line treatment is chemotherapy, which is associated with poor response rates and resistance. Treatments with the TRPV2 protein may improve TNBC sensitivity to chemotherapy. However, it remains unclear whether or not the TRPV2 protein will improve RFS in these tumors.
The TRPV2 gene has numerous applications in the treatment of OC, including regulating the body's immune system. It is also known by many other names, including Shun Shi Xing Gan, Ce Shi De Qi Ta, and Jian Bie He Biao Zheng. In addition, the gene is also known by many other names, including Li Ru Da Ma, Benham, and Suo Shu Huo Xing.
The TRPV2 protein is a non-selective calcium channel and is implicated in several physiological and pathological processes. The protein contains six transmembrane domains, a putative pore-loop region, and three ankyrin-repeat domains. It is a tetramer with 761 residues, and it functions as a multichannel protein. This protein possesses a hanging gondola architecture and is activated by noxious heat.
The TRPV2 gene is expressed in many organ systems, including the pancreas, lungs, and the digestive system. The TRPV2 gene is expressed in all four tissues of the human body, and its methylation in the liver, pancreas, and spleen, as well as in the brain. Although the gene is expressed in many organs, its presence is associated with the onset of OC, which can lead to a deterioration of the immune system.
In addition to its role in OC, TRPV2 is also involved in chemoatrophy and infiltration of organs. Therefore, it may serve as a pharmacodynamic biomarker. For this reason, researchers are looking for a new drug that inhibits TRPV2 in the prostate. However, there are also other potential uses for TRPV2.
Researchers have shown that TRPV2 gene expression increases with grade and stage, but it is stronger in UC specimens during G3 pT4 stages. These findings suggest that receptor expression may be modulated during the differentiation process of urothelial cells. Further, researchers have shown that the s-TRPV2 variant of the gene is expressed in low-grade RT4 cells, but undetectable in high-grade EJ and J82 cells.
In addition, TRPV2 has many roles in skeletal, cardiac, and neuronal physiology. Activated TRPV2 increases transport between intracellular compartments and the plasma membrane. The resulting activation of signaling pathways leads to an increase in the proliferation of bladder smooth muscle cells. And TRPV2 recycling is an important pathway in OC. If a drug targets TRPV2, it should be carefully evaluated for potential side effects.
In glioma, TRPV2 has been found to be expressed in both benign astrocyte tissues and malignant glioma cells. Hence, it is important to understand the molecular mechanisms behind the benefit of the HELP device. These findings also provide important information about the roles of the TRPV2 receptor in regulating gastrointestinal motility. However, these findings are limited by the fact that TRPV2 is only one component of this gene and many more may play important roles in OC.
In addition to being present in the mucosa, TRPV2 is also found in the muscle layer of rats with reflux oesophagitis. This marker was used to determine the location of TRPV2-immunopositive cells. In double-labelling experiments, TRPV2 immunoreactivity was found to be associated with ED1 and ED2 markers, which indicate cells that contain CD68 or CD163, and CD117, which are a marker for mast cells.
To identify the location of TRPV2-expressing nerve fibers in the esophagus, we used a combination of the TRPV2 marker and CGRP as a biomarker. TRPV2 was found to co-localise with a-SMA and CD117 in the interstitial cells of the esophagus of normal and oesophagitis rats.
High-affinity polyclonal antibodies targeting TRPV2 in rat and mice were found to recognize this protein. Preabsorption blocking of the primary antibody removed the 80 kDa band. The antibody was also successfully used to identify TRPV2 in F-11 cells, which had positive staining for the protein. Moreover, a 32-P-labeled riboprobe detected a single 2.7 kb TRPV2 transcript. Although F-11 cells have lower levels of TRPV2 mRNA than rat DRG, the position of the RNA size marker is similar between the two cell lines.
Furthermore, siRNA-mediated knockdown of TRPV2 did not significantly affect the number of spontaneous flinches and the withdrawal latency to thermal stimulation. Further, siRNA against TRPV2 significantly improved weight bearing and limb use in mice with bone cancer. It did not affect mechanical or thermal sensitivity. This suggests that TRPV2 is involved in ongoing pain, albeit different from ongoing pain.
This study also examined the functional role of the TRPV2 protein in human cancer cells. RGA participates in the control of TRPV2 surface levels. Thus, co-expression of TRPV2 and RGA may be a critical component of experimental systems for studying TRPV2 physiology. Wiley-Liss, Inc. publishes these antibodies for the study of tumefamutation-related protein expression.
The TRPV2 protein is expressed in the DRG neurons of rat brain. The immunoreactivity of TRPV2 was determined using Western blot analysis. The protein level was higher in the rat brain at day two and four compared to the control group. This study supports the use of TRPV2 as a potential therapeutic target for functional dyspepsia. Prevention of TRPV2 activity may also be helpful for oesophagitis.
The TRPV2 marker is associated with a high level of expression in MM patients. The expression of TRPV2 correlates with bone lesions and a poor prognosis. This research supports the potential for developing antibodies against other TRP channels in the future. So, high-affinity primary antibodies using the TRPV2 marker are a promising tool for clinical trials.
PMID: 10559903 by Kanzaki M., et al. Translocation of a calcium-permeable cation channel induced by insulin-like growth factor-I.
PMID: 11707512 by Boels K., et al. The neuropeptide head activator induces activation and translocation of the growth-factor-regulated Ca(2+)-permeable channel GRC.