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MYBPC3 encodes the cardiac isoform of myosin-binding protein C. Additionally we are shipping MYBPC3 Kits (16) and MYBPC3 Proteins (4) and many more products for this protein.
Showing 10 out of 62 products:
Human Polyclonal MYBPC3 Primary Antibody for EIA, IHC (p) - ABIN953556
Bailey, Xie, Do, Montpetit, Diaz, Mohan, Keavney, Yusuf, Gerstein, Engert, Anand: Variation at the NFATC2 locus increases the risk of thiazolidinedione-induced edema in the Diabetes REduction Assessment with ramipril and rosiglitazone Medication (DREAM) study. in Diabetes Care 2010
Show all 5 references for ABIN953556
N terminus of cMyBP-C interacts with F-actin through multiple distinct binding sites and that binding at one or more sites is reduced by phosphorylation
these data indicate a robust proinflammatory response in DCM hearts, likely in response to cellular damage triggered by MYBPC3 mutation and resultant contractile dysfunction.
We provide evidence that haploinsufficiency and poison polypeptide hypotheses are disease mechanisms and that EHTs can be used as a platform to evaluate the direct impact of (newly identified) MYBPC3 gene variants.
These results support the proposal that cMyBP-C stabilises the thick filament and that the loss of cMyBP-C results in an untethering of myosin heads.
Crypts are a normal part of cardiac development but, along with the mitral valve and trabeculae, their developmental trajectory is altered by the presence of HCM truncating Mybpc3 gene mutation
that in the homozygous hypertrophic cardiomyopathy mouse model, beta-AR stimulation leads to preferential PKA phosphorylation of phospholamban over cardiac troponin I, resulting in an impaired inotropic and lusitropic response
Phosphorylation of MYBPC3 contributes to the genesis of ventricular wall geometry, linking myofilament biology with multiscale cardiac mechanics and myoarchitecture.
The cMyBP-C hypertrophic cardiomyopathy variant L348P enhances thin filament activation through an increased shift in tropomyosin (show TPM2 Antibodies) position.
The contributions of cardiac myosin binding protein C and troponin I phosphorylation to beta-adrenergic enhancement of in vivo cardiac function
MYBPC3 mutations is elevated oxidative stress that corresponded to severe cardiac dysfunction, myocyte damage, and myocardial remodeling.
MBPC and troponin-I phosphorylation modulate myofilament length-dependent activation
The authors demonstrate myosin tail (S2)-dependent functional regulation of actin-activated human beta-cardiac myosin ATPase (show DNAH8 Antibodies). In addition, they show that both S2 and MyBP-C bind to S1 and that phosphorylation of either S1 or MyBP-C weakens these interactions.
Our study supports that mutations in MYH7 (show MYH7 Antibodies) and MYBPC3 should be the first focus of moleculargenetic analysis in HCM, and that mutations in TNNT2 (show TNNT2 Antibodies) have a low prevalence in Brazilian population. All mutations detected were missense mutations, whereas two mutations in MYH7 (show MYH7 Antibodies) had not been described before.
These findings point to the critical role of MYBPC3 during sarcomere assembly in cardiac myocyte differentiation and suggest developmental influences of MYBPC3 truncating mutations on the mature hypertrophic phenotype.
Study shows lack of phenotypic differences between MYH7 (show MYH7 Antibodies)- and MYBPC3-associated hypertrophic cardiomyopathy when assessed by cardiac magnetic resonance imaging.
MYBPC3 and MYH7 (show MYH7 Antibodies) were the most common mutated genes, accounting for 27% of the total Hypertrophic Cardiomyopathy patients and 83% of the putative mutations in the main sarcomeric genes.
MYBPC3 gene mutation is associated with Early-Onset Hypertrophic Cardiomyopathy.
The results showed that MYBPC3 25-bp deletion polymorphism was significantly associated with elevated risk of left ventricular dysfunction (LVD), while TTN 18 bp I/D, TNNT2 5 bp I/D and myospryn K2906N polymorphisms did not show any significant association with LVD.
we report a patient presenting with a complex phenotype consisting of severe, adult-onset, dilated cardiomyopathy, hearing loss and developmental delay, in which exome sequencing revealed two genetic variants that are inherited from a healthy mother: a variant, in MYBPC3, that is associated with hereditary cardiomyopathy.
5 out of 102 (4.9%) athletes carried mutations: a heterozygous MYH7 (show MYH7 Antibodies) Glu935Lys mutation, a heterozygous MYBPC3 Arg160Trp mutation and another heterozygous MYBPC3 Thr1046Met mutation, all of which had been reported as HCM-associated mutations
a significant role of MYBPC3 gene mutations in Hypertrophic cardiomyopathy(HCM) disease and can be used for pre-symptomatic diagnosis of at risk family members of affected individuals.
small es, CyrillicMyBP-C modulates interaction of myosin with actin
MYBPC3 encodes the cardiac isoform of myosin-binding protein C. Myosin-binding protein C is a myosin-associated protein found in the cross-bridge-bearing zone (C region) of A bands in striated muscle. MYBPC3, the cardiac isoform, is expressed exclussively in heart muscle. Regulatory phosphorylation of the cardiac isoform in vivo by cAMP-dependent protein kinase (PKA) upon adrenergic stimulation may be linked to modulation of cardiac contraction. Mutations in MYBPC3 are one cause of familial hypertrophic cardiomyopathy.
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