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The protein encoded by TRPM2 is a calcium-permeable cation channel that is regulated by free intracellular ADP-ribose. De plus, nous expédions TRPM2 Protéines (6) et beaucoup plus de produits pour cette protéine.
Showing 10 out of 94 products:
Mouse (Murine) Polyclonal TRPM2 Primary Antibody pour ICC, IHC (fro) - ABIN259658
Bai, Lipski: Differential expression of TRPM2 and TRPV4 channels and their potential role in oxidative stress-induced cell death in organotypic hippocampal culture. dans Neurotoxicology 2010
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Human Polyclonal TRPM2 Primary Antibody pour ICC, IHC (fro) - ABIN153042
Partida-Sanchez, Gasser, Fliegert, Siebrands, Dammermann, Shi, Mousseau, Sumoza-Toledo, Bhagat, Walseth, Guse, Lund: Chemotaxis of mouse bone marrow neutrophils and dendritic cells is controlled by adp-ribose, the major product generated by the CD38 enzyme reaction. dans Journal of immunology (Baltimore, Md. : 1950) 2007
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Human Polyclonal TRPM2 Primary Antibody pour ICC, IF - ABIN153041
Moreau, Kirchberger, Swarbrick, Bartlett, Fliegert, Yorgan, Bauche, Harneit, Guse, Potter: Structure-activity relationship of adenosine 5'-diphosphoribose at the transient receptor potential melastatin 2 (TRPM2) channel: rational design of antagonists. dans Journal of medicinal chemistry 2013
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Mouse (Murine) Polyclonal TRPM2 Primary Antibody pour ICC, IF - ABIN4362934
Rah, Kwak, Chung, Kim: ADP-ribose/TRPM2-mediated Ca2+ signaling is essential for cytolytic degranulation and antitumor activity of natural killer cells. dans Scientific reports 2015
Cow (Bovine) Polyclonal TRPM2 Primary Antibody pour IHC, WB - ABIN2781840
Hecquet, Ahmmed, Vogel, Malik: Role of TRPM2 channel in mediating H2O2-induced Ca2+ entry and endothelial hyperpermeability. dans Circulation research 2008
Study determined the sequence of pig TRPC1 and TRPC3-7 channels and found pig TRPC cDNAs resemble their human homologs more than the others .
heteromeric cation channels comprised of the TRPP2 mutant and the TRPC3 (Montrer TRPC3 Anticorps) or TRPC7 protein induce enhanced receptor-activated Ca(2 (Montrer CA2 Anticorps)+) influx that may lead to dysregulated cell growth in ADPKD
oxidative stress activated the TRPM2 (Montrer CLU Anticorps)-CaMKII (Montrer CAMK2G Anticorps) cascade to further induce intracellular ROS (Montrer ROS1 Anticorps) production, which led to mitochondria fragmentation and loss of mitochondrial membrane potential
The work summarized here shows that TRPM2 (Montrer CLU Anticorps) channels protect cardiac myocytes from ischaemia-reperfusion injury and tumour cells from doxorubicin toxicity, and demonstrates that the mechanisms involve preservation of mitochondrial bioenergetics and modulation of ROS (Montrer ROS1 Anticorps)
Activation of TRPM2 (Montrer CLU Anticorps) channels, however, caused intracellular release of not only Ca(2 (Montrer CA2 Anticorps)+) but also of Zn(2+) Intriguingly, elevation of intracellular Zn(2+) faithfully reproduced all of the effects of H2O2, whereas Ca(2 (Montrer CA2 Anticorps)+) showed opposite effects. Interestingly, H2O2 caused increased trafficking of Zn(2+)-enriched lysosomes to the leading edge of migrating cells, presumably to impart polarisation of Zn(2+) location.
neutrophils sense reactive oxygen species via the TRPM2 (Montrer CLU Anticorps) channel to arrest migration at their target site.
The inhibitory function of oxidant sensing by TRPM2 (Montrer CLU Anticorps) requires the oxidation of Cys549, which then induces TRMP2 binding to formyl peptide receptor 1 (FPR1 (Montrer FPR1 Anticorps)) and subsequent FPR1 (Montrer FPR1 Anticorps) internalization and signaling inhibition
findings demonstrate the important function of TRPM2 (Montrer CLU Anticorps) in modulation of cell survival through mitochondrial ROS (Montrer ROS1 Anticorps), and the potential of targeted inhibition of TRPM2 (Montrer CLU Anticorps) as a therapeutic approach to reduce cellular bioenergetics, tumor growth, and enhance susceptibility to chemotherapeutic agents.
Study demonstrate that PRL (Montrer PRL Anticorps) is necessary for the survival of (retinal pigment epithelium) RPE (Montrer RPE Anticorps) under normal and advancing age conditions and, identified SIRT2 (Montrer SIRT2 Anticorps) and TRPM2 (Montrer CLU Anticorps) as molecular targets for the antioxidant and antiapoptotic actions of PRL (Montrer PRL Anticorps) in the RPE (Montrer RPE Anticorps).
TRPM2 (Montrer CLU Anticorps) has a role in the DNA damage response of T cell leukemia cells in a BCL-2 (Montrer BCL2 Anticorps) dependent manner
Data show that HEK293 cells expressing low levels of receptor potential melastatin 2 (TRPM2) chan (Montrer TRPM3 Anticorps)nel wer (Montrer CLU Anticorps)e more susceptible to silica nanoparticles (NPs) than those expressing high levels of TRPM2.
This is expected to provide a basis for inhibiting TRPM2 (Montrer CLU Anticorps) for the improved treatment of breast cancer, which potentially includes treating breast tumors that are resistant to chemotherapy due to their evasion of apoptosis.
These findings of this study suggest that TRPM2 channels play an essential role in mediating hypoxic-ischemic brain injury in neonatal mice.
TRPM2 regulates phagosomal acidification, and is essential for the bacterial killing function of macrophages.
Lysophosphatidylcholine induces intracellular Ca(2 (Montrer CA2 Anticorps)+) influx and increases phosphorylation of p38 MAPK (Montrer MAPK14 Anticorps) via TRPM2, which in turn activates microglia.
The current study demonstrated that a physiological concentration of adrenaline attenuates insulin (Montrer INS Anticorps) release via coupling of alpha2A-adrenoceptor to cAMP/TRPM2 signaling.
Trpm2 does not seem to play a major role in myeloid leukemogenesis. Additionally, loss of Trpm2 does not augment the cytotoxicity of standard AML (Montrer RUNX1 Anticorps) chemotherapeutic agents.
TRPM2 channels contribute to visceral nociception in response to noxious stimuli under normal conditions and visceral hypersensitivity in pathological conditions.
Data show that macrophages from young mice showed lower transient receptor potential melastatin 2 (Montrer TRPM3 Anticorps) (TRPM2) expression than those from senescent mice and had lower viability after silica nanoparticles (NPs (Montrer NPS Anticorps)) exposure than those from senescent ones.
TRPM2 activation is likely to be mediated by ADP-ribose production via PARP (Montrer PARP1 Anticorps) pathway
mice in which TRPM2 had been genetically deleted showed a striking deficit in their sensation of non-noxious warm temperatures, consistent with the idea that TRPM2 initiates a 'warm' signal which drives cool-seeking behaviour
findings provide compelling evidence that F. tularensis catalase (Montrer CAT Anticorps) restricts reactive oxygen species to temper macrophage TRPM2-mediated Ca(2 (Montrer CA2 Anticorps)+) signaling and limit host immune function.
The protein encoded by this gene is a calcium-permeable cation channel that is regulated by free intracellular ADP-ribose. The encoded protein is activated by oxidative stress and confers susceptibility to cell death. Several alternatively spliced transcript variants of this gene have been described, but their full-length nature is not known.
transient receptor potential cation channel, subfamily M, member 2
, transient receptor potential cation channel, subfamily C, member 7
, transient receptor potential cation channel, subfamily C, member 7-like
, short transient receptor potential channel 7-like
, transient receptor potential cation channel subfamily M member 2-like
, transient receptor potential channel subfamily C member 7
, estrogen-responsive element-associated gene 1 protein
, long transient receptor potential channel 2
, transient receptor potential cation channel subfamily M member 2
, transient receptor potential channel 7
, transient receptor protein 7
, transient receptor potential melastatin family 2