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anti-Human Phospholamban Anticorps:
anti-Mouse (Murine) Phospholamban Anticorps:
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Chicken Monoclonal Phospholamban Primary Antibody pour ICC, IF - ABIN152737
Liu, Hu, Wang, Xu, Wang, Gong, Mansoor, Lee, Hou, Zeng, Zhang, Jerosch-Herold, Guo, Bache, Zhang: Autologous stem cell transplantation for myocardial repair. dans American journal of physiology. Heart and circulatory physiology 2004
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Human Polyclonal Phospholamban Primary Antibody pour WB - ABIN1882182
Fujii, Zarain-Herzberg, Willard, Tada, MacLennan: Structure of the rabbit phospholamban gene, cloning of the human cDNA, and assignment of the gene to human chromosome 6. dans The Journal of biological chemistry 1991
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Human Polyclonal Phospholamban Primary Antibody pour ELISA, WB - ABIN4345330
Møller, Pham, Gustafsson, Hedley, Ersbøll, Bundgaard, Andersen, Torp-Pedersen, Køber, Christiansen: The role of Lamin A/C mutations in Danish patients with idiopathic dilated cardiomyopathy. dans European journal of heart failure 2009
LMOD1 (Montrer LMOD1 Anticorps), SYNPO2 (Montrer SYNPO2 Anticorps), PDLIM7 (Montrer PDLIM7 Anticorps), PLN, and SYNM (Montrer SYNM Anticorps) down-regulation reflect the altered phenotype of smooth muscle cells in vascular disease and could be early sensitive markers of SMC (Montrer DYM Anticorps) dedifferentiation.
microRNAs (miRNAs) 1 and 21 bind PLN strongly and relieve PLN inhibition of SERCA (Montrer ATP2A3 Anticorps) to a greater extent than a similar length random sequence RNA mixture.
Data suggest phospholamban (PLN) gene is a rare cause of cardiomyopathy in African patients.
Phospholamban and sarcolipin (Montrer SLN Anticorps) are membrane proteins that differentially regulate SERCA (Montrer ATP2A3 Anticorps) function. (Review)
PLN may be a key molecular player in rigid substrate-induced cellular hypertrophy in eosinophilic esophagitis.
These data suggest that PLN is, at least partially, oligo-ubiquitinated at Lys (Montrer LYZ Anticorps)(3) and degraded through Ser (Montrer SIGLEC1 Anticorps)(16)-phosphorylation-mediated poly-ubiquitination during heart failure.
hereditary mutants of phospholamban are associated with heart failure [review]
PLN pentamers reduce phosphorylation of monomers at baseline and delay monomer phosphorylation upon PKA stimulation leading to increased interaction of PLN monomers with SERCA2a (Montrer ATP2A2 Anticorps).
Phospholamban R14del mutation carriers are at high risk for malignant ventricular arrhythmias and end-stage heart failure, with left ventricular ejection fraction <45% and sustained or nonsustained ventricular tachycardia as independent risk factors.
Although SLN (Montrer SLN Anticorps) and PLB binding to SERCA (Montrer ATP2A3 Anticorps) have different functional outcomes on the coupling efficiency of SERCA (Montrer ATP2A3 Anticorps), both proteins decrease the apparent Ca(2 (Montrer CA2 Anticorps)+) affinity of the pump, suggesting that SLN (Montrer SLN Anticorps) and PLB inhibit SERCA (Montrer ATP2A3 Anticorps) by using a similar mechanism.
Phosphorylation of PLB induces spatial rearrangements between the N- and P-domain elements of proximal Ca-ATPase (Montrer CA-P60A Anticorps).
Molecular dynamics simulations of phospholamban in solution and in membrane bilayer show two main features: the presence of two well-defined helical domains at the N- and C-termini, and large-amplitude rigid-body motions of these domains.
The expression of SLN (Montrer SLN Anticorps) and PLB mRNA and protein relative to SERCA1 (Montrer ATP2A1 Anticorps) or SERCA2 (Montrer ATP2A2 Anticorps) was assessed in ventricle, atrium, and skeltal msucle of mouse, rat, rabbit and pig.
A single-dose injection of PLN-targeting locked nucleic acid antisense oligonucleotide improved contractility in pressure overload-induced cardiac dysfunction.
PLN overexpression is associated with severe muscle atrophy and weakness.
the commercially available overexpressing phospholamban mouse phenotypically resembles human Centronuclear myopathy and could be used as a model to test potential mechanisms and therapeutic strategies.
Cardioprotective effects of H2S are mediated through acGMP/PKG (Montrer PRKG1 Anticorps)/phospholamban pathway.
combined deletion of Phd2 (Montrer EGLN1 Anticorps) and Phd3 (Montrer EGLN3 Anticorps) dramatically decreased expression of phospholamban (PLN), resulted in sustained activation of calcium/calmodulin-activated kinase II (CaMKII (Montrer CAMK2G Anticorps)), and sensitized mice to chronic beta-adrenergic stress-induced myocardial injury
the N termini of SLN (Montrer SLN Anticorps) and PLB influence their respective unique functions
CaMKII (Montrer CAMK2G Anticorps)-dependent increase in PLN phosphorylation during reperfusion opposes rather than contributes to ischemia/reperfusion damage.
TNAP (Montrer ALPL Anticorps) plays a role in governing the phosphorylation status of phospholamban in the sarcoplasmic reticulum.
Acute expression of R9C mutation of phospholamban in cardiomyocytes was positively inotropic/lusitropic.
Ca(2 (Montrer CA2 Anticorps)+) and PLB phosphorylation relieve SERCA (Montrer ATP2A3 Anticorps)-PLB inhibition by distinct mechanisms, but both are achieved primarily by structural changes within the SERCA (Montrer ATP2A3 Anticorps)-PLB complex, not by dissociation of that complex.
Phosphorylated phospholamban stabilizes a unique conformation of SERCA (Montrer ATP2A3 Anticorps) that is characterized by a compact architecture.
Data suggest that phospholamban PLN's conformational equilibrium is central to maintain sarcoplasmic reticulum Ca(2+)-ATPase (Montrer CA-P60A Anticorps) SERCA's apparent Ca(2 (Montrer CA2 Anticorps)+) affinity within a physiological window.
demonstrate that the role of Arg(9) in phospholamban function is multifaceted: it is important for inhibition of SERCA (Montrer ATP2A3 Anticorps), it increases the efficiency of phosphorylation, and it is critical for protein kinase A recognition
The interaction energies between the N-terminal helix of phospholamban and different POPC lipid/cholesterol bilayers quantitatively confirm its stronger interaction with a higher cholesterol-containing membrane.
The lipid bilayer composition influences the regulation of SERCA (Montrer ATP2A3 Anticorps) by PLN.
Phospholamban overexpression in rabbit ventricular myocytes does not alter sarcoplasmic reticulum Ca transport.
The protein encoded by this gene is found as a pentamer and is a major substrate for the cAMP-dependent protein kinase in cardiac muscle. The encoded protein is an inhibitor of cardiac muscle sarcoplasmic reticulum Ca(2+)-ATPase in the unphosphorylated state, but inhibition is relieved upon phosphorylation of the protein. The subsequent activation of the Ca(2+) pump leads to enhanced muscle relaxation rates, thereby contributing to the inotropic response elicited in heart by beta-agonists. The encoded protein is a key regulator of cardiac diastolic function. Mutations in this gene are a cause of inherited human dilated cardiomyopathy with refractory congestive heart failure.
, cardiac phospholamban