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TRDN encodes an integral membrane protein that contains a single transmembrane domain. Additionally we are shipping Triadin Antibodies (2) and many more products for this protein.
Showing 6 out of 6 products:
These data for the first time demonstrate that Trisk 95's 200-231 region is responsible for ryanodine receptor activation.
Three regions in triadin are identified that mediate targeting to the junctional domain of sarcoplasmic reticulum.
in skeletal muscle the disruption of Tdn/CASQ (show CASQ1 Proteins) link has a more profound effect on jSR architecture and myoplasmic Ca(2 (show CA2 Proteins)+) regulation than Jct/CASQ (show CASQ1 Proteins) association.
The triadin-to-calsequestrin ratio is a critical modulator of the sarcoplasmic reticulum Ca(2 (show CA2 Proteins)+) signaling in ventricular myocytes.
Ablation of skeletal muscle triadin impairs FKBP12 (show FKBP1A Proteins)/RyR1 channel interactions essential for maintaining resting cytoplasmic Ca2 (show CA2 Proteins)+.
caveolin 3 (show CAV3 Proteins)-containing membrane domains and the calcium release complex are functionally linked and Trdn is instrumental to the regulation of this interaction, the integrity of which may be crucial for muscle physiology.
Results demonstrate a reduction in muscle strength in triadin knockout mice, indicating that triadin plays an essential role in skeletal muscle function and in skeletal muscle structure.
triadin 1 overexpression triggered time-dependent alterations in SR protein (show RNPS1 Proteins) expression, Ca(2 (show CA2 Proteins)+) homeostasis, and contractility, indicating for the first time an inhibitory function of triadin 1 on SR-Ca(2 (show CA2 Proteins)+) release in vivo.
Triadin(TRD)xjunctin(JCN) mice were studied to compensate the down-regulation of junctin (show ASPH Proteins) expression in triadin-expressing mice; exercise or stress provoked repetitive ventricular tachycardia in freely roaming TRDxJCN mice.
Histidine-rich Ca-binding protein may play a key role in the regulation of SR Ca cycling through its direct interactions with SERCA2 (show ATP2A2 Proteins) and triadin, mediating a fine cross talk between SR Ca uptake and release in the heart.
triadin has a role in regulating myoplasmic Ca(2 (show CA2 Proteins)+) homeostasis and organizing the molecular complex of the triad but not in regulating skeletal-type excitation-contraction coupling
We describe a new family with cathecholaminergic polymorphic ventricular tachycardia (CPVT) linked to the Triadin gene.
Common variants in TRDN and CALM1 (show CALM1 Proteins) are associated with increased risk of sudden cardiac death in patients with chronic heart failure.
TRDN is a novel underlying genetic basis for recessively inherited Long-QT syndrome.
Data show that triadin (TRDN) is a new gene responsible for an autosomal recessive form of ctecholaminergic polymorphic ventricular tachycardia (CPVT).
The researchers found evidence that TRDN may be a susceptibility or marker gene for IgA nephropathy
proteasome inhibition led to an accumulation of two new modified forms of triadin-1 that were seen with triadin-1 only when it is not glycosylated on Asn(75).
This gene encodes an integral membrane protein that contains a single transmembrane domain. As similar protein in rabbits plays a role in skeletal muscle excitation-contraction coupling as part of the calcium release complex in association with the ryanodine receptor. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene, and single nucleotide polymorphisms in this gene may be markers for IgA nephritis.
, junctional sarcoplasmic reticulum glycoprotein
, cardiac triadin
, triadin 1
, triadin 32 kDa (TRISK 32)
, triadin 49 kDa (TRISK 49)
, triadin 95