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Validated All-in-One™ qPCR Primer for CAV3(NM_033337.2) Search again
Product ID:
HQP061555
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
LGMD1C, LQT9, MPDT, RMD2, VIP-21, VIP21
Gene Description:
caveolin 3
Target Gene Accession:
NM_033337.2(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
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| A | B |
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Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
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Summary
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. [provided by RefSeq].
Gene References into function
- A heterozygous 80 G-->A substitution in the caveolin-3 gene is associated with sporadic distal myopathy
- A naturally occurring caveolin-3 mutation can inhibit signaling involving cholesterol-sensitive raft domains.
- P28L mutation in the CAV-3 gene and the consequent caveolin-3 deficiency is associated with elevated serum kreatine kinase levels.
- Effects of deleting a tripeptide sequence observed in muscular dystrophy patients on the conformation of peptides corresponding to the scaffolding domain of caveolin-3.
- caveolin-3 may play a role in lamellar granule assembly, trafficking, and/or function.
- severe form of rippling muscle disease associated with homozygous CAV3 mutations.
- A haploinsufficiency model is proposed in which reduced levels of wild-type caveolin-3, although not rendered dysfunctional due to the caveolin-3 R26Q mutant protein, are insufficient for normal muscle cell function.
- Adenovirus-mediated overexpression of human caveolin-3 inhibits hypertrophic responses in rat cardiomyocytes.
- An R27Q missense mutation in the CAV3 gene can lead to various clinical phenotypes including hyper-CK-emia, rippling muscle disease, distal myopathy, and limb-girdle musclar dystrophy 1C.
- CD36 colocalizes with caveolin-3, suggesting that caveolae may regulate cellular fatty acid uptake by CD36. CD36 expression is higher in type 1 compared with type 2 fibers, whereas caveolin-3 expression is significantly higher in type 2 than in type 1
- the importance of dysferlin-caveolin 3 relationship for skeletal muscle integrity
- Review. Caveolin-3 mutations can result in four distinct, sometimes overlapping, muscle disease phenotypes: limb girdle muscular dystrophy, rippling muscle disease, distal myopathy, and hyperCKemia.
- A muscle biopsy showed a partial reduction of caveolin-3 at the sarcolemma of muscle fibres.Mutational analysis identified a novel heterozygous mutation and generating a Val-->Met change at codon 57 of the amino acid chain.
- demonstrate that Cav-3 is specifically expressed in human cardiac and skeletal myocytes, with high specificity and relatively high sensitivity (88%) for tumors with skeletal muscle differentiation
- The authors describe a family with autosomal dominant rippling muscle disease (RMD) and prominent early-onset toe walking. Molecular analysis revealed a novel heterozygous G > A transition at nucleotide position 136 in exon 2 of the caveolin-3 gene.
- The co-localization of Cav-3 with COX-2 in the caveolae suggests that the caveolins might play an important role for regulating the function of COX-2.
- CAV3 identified and immunolocalized in the caveola-vesicle complexes (CVC )present in erythrocytes infected with P. vivax
- Our findings suggest that caveolin exhibits growth inhibition in a Ca2+-dependent manner, most likely through PKC, in cardiac myoblasts.
- Our findings contribute to the clarification of unexplained persistent hyper-CK-emia, but further research is needed before CAV3 gene mutation analysis becomes part of the routine evaluation of these patients.
- caveolin-3 normally suppresses the myostatin-mediated signal
- Reports of first CAV3 mutations in subjects with long-QT syndrome and functional data demonstrating gain-of-function increase in late sodium current.
- We demonstrated that 9.5% of cases diagnosed as SIDS carry functionally significant genetic variants in LQTS genes (KCNQ1, KCNH2, SCN5A, KCNE1, KCNE2, KCNJ2, CAV3).
- the first molecular and functional evidence implicating CAV3 as a pathogenic basis of Sudden infant death syndrome
- Cav-3 mediates defective gallbladder contraction in the presence of cholesterol stones. Increased expression of Cav-3 results in the sequestration of CCK-1 receptors in the caveolae, probably by inhibiting the functions of Galpha(i3) proteins.
- Molecular analysis revealed a novel heterozygous A>C transition at nucleotide position 140 in exon 2 of the caveolin-3 gene in 17-year-old patient with rippling muscle disease.
- We encountered a Korean male patient with RMD who had suffered from muscle stiffness for 3 years. Mutation analysis of the CAV3 gene revealed the patient to be heterozygous for a novel in-frame deletion mutation.
- This study describe a 39-year-old Japanese man with rippling muscle disease who carried a novel homozygous mutation (Trp70 to a stop codon) in the caveolin-3 gene.
- The presence of different caveolin isoforms in many cell types of the human retina, is reported.
- Caveolin 3 missense mutations lead to different phenotypes in vivo and in vitro.
- Here, we report the clinical, morphological and molecular analysis of a patient with autosomal-recessive RMD carrying two novel compound heterozygous CAV3 mutations that lead to a severe protein truncation.
- Expression of the muscular dystrophy-associated caveolin-3(P104L) mutant in adult mouse skeletal muscle specifically alters the Ca(2+) channel function of the dihydropyridine receptor.
- Two novel missense mutation in the CAV3 gene in Neuromuscul Disord.
- Mutation analysis revealed a novel heterozygous missense mutation in the caveolin-3 gene (c.79C > G; p.Arg27Gly) in both the index patient diagnosed with rippling muscle disease and his mother fasely diagnosed with acid maltase deficiency.
- Genetic studies revealed a G --> A transition at nucleotide position 80 in exon 1 of the Cav-3 gene (c.80G>A), generating a Arg --> Gln change at codon 27 (p.R27Q) of the amino acid chain in heterozygous state in this case.
- HCN4 associates with Cav3 to form a HCN4 macromolecular complex. Our results also indicated that disruption of caveolae using P104L alters HCN4 function and could cause a reduction of cardiac pacemaker activity.