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anti-Human Caveolin 3 Antibodies:
anti-Mouse (Murine) Caveolin 3 Antibodies:
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Human Polyclonal Caveolin 3 Primary Antibody for IHC (p), IHC - ABIN451754
Fine, Lisanti, Argani, Li: Caveolin-3 is a sensitive and specific marker for rhabdomyosarcoma. in Applied immunohistochemistry & molecular morphology : AIMM / official publication of the Society for Applied Immunohistochemistry 2005
Human Polyclonal Caveolin 3 Primary Antibody for FACS, ICC - ABIN258384
Dınız, Eryaşar, Türe, Akçay, Ortaç, Tekgül, Akhan: A regional panorama of dysferlinopathies. in Turk patoloji dergisi 2012
The CAV3-P104L mutation inhibits glycometabolism and cell growth but accelerates C2C12 cell proliferation by reducing CAV3 protein expression and cell membrane localization, which may contribute to the pathogenesis of LGMD-1C.
Under mechanical stress the regulation of mechanoprotection by caveolae is directly coupled with the regulation of IL6/STAT3 signaling in muscle cells and that this regulation is absent in Cav3-associated dystrophic patients.
Kir2.x isoforms have a unique intracellular pattern of distribution in association with specific Cav3 domains and that critically depends on interaction with N-terminal Kir2.x Cav3-binding motifs
T78M cav-3 induces complex modifications in ion channel function that ultimately alter membrane excitability and thus generate a susceptible substrate that, in concert with other structural alterations and/or genetic mutations, may become arrhythmogenic.
Case series demonstrates that exercise intolerance, myalgia and rhabdomyolysis may be caused by CAV3 mutations and broadens phenotypic spectrum of caveolinopathies. Percussion-induced rapid muscle contractions were seen in 5 of 6 patients. A previously reported heterozygous mutation in CAV3 (p.T78M) and 3 novel variants (p.V14I, p.F41S, p.F54V) were identified. >50% reduction of caveolin-3 in 5 patients vs controls.
our study indicates that TASK-1 is functionally regulated by caveolin-3, possibly via association with each other on the cell surface. These results point out a novel mechanism in the regulation of TASK-1.
The caveolin 3 G56S variant is not a clearly pathogenic mutation, but may influence cellular functions and morphologies resulting in an increased cellular vulnerability in terms of a modifying factor.
Our results indicate that HCN4 channel function is modulated by cav-3. LQTS-associated mutations of cav-3 differentially influence pacemaker current properties indicating a pathophysiological role in clinical manifestations.
This study demonstrated that the Caveolin-3 is aberrantly expressed in skeletal muscle cells in myasthenia gravis.
Study characterized the secondary structure, dynamics, and topology of a lipidated full-length human Cav3 construct, demonstrated that the N-terminal domain undergoes a dramatic topological rearrangement in both micelles and vesicles that is reversibly mediated by pH
The Cav3 P104L mutation of limb girdle muscular dystrophy-1C leads to disordered glucose metabolism in muscle cells.
Data (including data from studies using recombinant proteins that lack typical in-vivo post-translational modifications such as palmitoylation) suggest Cav3 exhibits little tendency to partition into liquid-ordered domains of unilamellar vesicles.
MURC/cavin-4, especially in combination with Cav-3, may play a consistent role in the differentiation process of rhabdomyosarcoma.
This study demonstrated that cav3 mutation in stinct disorders including limb-girdle muscular dystrophy 1C, rippling muscle disease, and isolated creatine kinase elevation in Greece.
In a nonreferred nationwide Danish cohort of SIDS cases, up to 5/66 (7.5%) of SIDS cases can be explained by genetic variants in the sodium channel complex genes.
We identified three novel sequence variations (c.183C>G, p.S61R; c.220C>A, p.R74S; c.220C>T, p.R74C) and found evidence that one was associated with hypercreatine kinase-emia
our results indicate that inhibition of Cav3 currents by 5,6-epoxyeicosatrienoic acid is an important mechanism controlling the vascular tone.
detrimental effect of Cav-3 V82I variant on cell viability may participate in determining the susceptibility to cardiac death.
The caveolin-3:p.T78M did not exhibit a long-QT syndrome phenotype.
Cav3 is an important negative regulator for cardiac late sodium cutrrent via nNOS dependent direct S-nitrosylation of SCN5A.
Results provide evidence that cav-3 differentially organizes serotonergic and cholinergic signaling in airway smooth muscle through mechanisms that are specific for airways of certain caliber and anatomical position.
Caveolin-3 KO disrupts t-tubule structure and decreases t-tubular ICa density in mouse ventricular myocytes, leading to cardiac hypertrophy and dysfunction.
these findings revealed a novel role of FAT10 in protection against ischemia-induced injury via stabilization of Cav-3
Pathogenic p.P104 mutation causes endoplasmic reticulum stress, impairs protein processing, ECM remodeling and sarcolemmal integrity.
Cav-3 and Smad3 may be involved in the occurrence and development of viral myocarditis.
CAV3 protein has a physiological role in glycometabolism, growth and proliferation, independent of insulin stimulation
Data show that caveolin-3 binds to low glycosylated extracellular matrix metalloproteinase inducer (LG-EMMPRIN) in cardiac cells and in the hearts of healthy mice.
Cav-3 overexpressing mice have changes in ECG intervals, heart rates, and cardiac ion channel expression
Loss of CAV3 interferes with downstream insulin signaling and lipid uptake and increases susceptibility to palmitate-induced insulin resistance.
eNOS, caveolin-3, and connexin-43 were detected in subsarcolemmal mitochondria
Data show increased expression of T-type Ca(2+) current and association of protein kinase C alpha (PKCalpha) with caveolin-3 (Cav-3)was disrupted in the hypertrophic ventricular myocyte.
Cardioprotection in myocardial infarction is abolished in caveolin-3 knockout mice.
The lithogenic diet was associated with significantly lower CAV3 in the liver and lower CAV3 and CCKAR in the gallbladder compared with the control mice.
Cav-3 may be a novel participant in B-cell expression, T-cell cytokine production and activation of inflammation
Cav3 protein can modify integrin function and mechanotransduction in the cardiomyocyte and intact heart
Deinactivation of Cav3 channels increases T-type Ca(2+) influx and increases feedback inhibition in olfactory bulb.
Data reveal the membrane cholesterol dependence of normoxic myocardial and coronary function, I/R tolerance, and morphine-mediated cardioprotection in murine hearts (all declining with cholesterol depletion).
The Cav-1 and Cav-3 knockout mice exhibited enhanced lesion volume and cytokine/chemokine production after Traumatic brain injury.
Cav-3 has a pivotal role in defending cardiomyocytes against the TNF pro-apoptotic action and alpha-linoleic acid has the capacity to regulate this mechanism preventing cardiac degenerative diseases.
Cav3 is involved in muscle development and is required for correct intracellular organization and myoblast fusion.
cloned and characterized caveolin-3 from porcine muscle; caveolin-3 was expressed specifically in skeletal muscle & heart; first evidence that caveolin-3 has a certain regulated expression pattern during the prenatal period of skeletal muscle development
This gene encodes a caveolin family member, which functions as a component of the caveolae plasma membranes found in most cell types. Caveolin proteins are proposed to be scaffolding proteins for organizing and concentrating certain caveolin-interacting molecules. Mutations identified in this gene lead to interference with protein oligomerization or intra-cellular routing, disrupting caveolae formation and resulting in Limb-Girdle muscular dystrophy type-1C (LGMD-1C), hyperCKemia or rippling muscle disease (RMD). Alternative splicing has been identified for this locus, with inclusion or exclusion of a differentially spliced intron. In addition, transcripts utilize multiple polyA sites and contain two potential translation initiation sites.
, calveolin 3
, caveolin 3