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|Tested species reactivity||Mouse, Rabbit, Rat|
|Published species reactivity||Rabbit, Rat, Pig, Mouse|
|Host / Isotype||Mouse / IgG|
|Immunogen||Purified rabbit fast skeletal muscle triadin.|
|Contains||0.05% sodium azide|
|Storage Conditions||-20° C, Avoid Freeze/Thaw Cycles|
|Tested Applications||Dilution *|
|ELISA (ELISA)||Assay dependent|
|Immunohistochemistry (Frozen) (IHC (F))||1:50|
|Immunoprecipitation (IP)||Assay dependent|
|Western Blot (WB)||1:500|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
MA3-927 detects triadin from mouse, rabbit and rat tissues.
MA3-927 has been successfully used in Western blot, immunohistochemistry, immunoprecipitation and ELISA procedures. By Western blot, this antibody detects a 95 kDa protein representing triadin from rabbit skeletal muscle extracts. Immunohistochemical staining of triadin in rat skeletal muscle with MA3-927 results in striated staining consistent with sarcoplasmic reticulum localization.
The MA3-927 antigen is purified rabbit fast skeletal muscle triadin.
The junction between the transverse tubules (T-tubules) and the sarcoplasmic reticulum (SR) of skeletal muscle is called the triad. At the triad, dihydropyridine receptors (DHPR"e;s) of the T-tubule serve as voltage sensors in excitation-contraction coupling, while ryanodine receptors (RyR"e;s), the calcium release channels, exist in the membrane of the terminal cisternae of the SR. It is thought that during slow phase depolarization of the T-tubule, a third protein, triadin (MW 95 kDa) transmits electrochemical signals to the SR through direct interaction with both DHPR"e;s and RyR"e;s.
Though its exact role in this signaling process is unclear, triadin has been shown to co-localize with both DHPR and RYR at the junctional face of the terminal cisternae.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Identification of Small Ankyrin 1 as a Novel Sarco(endo)plasmic Reticulum Ca2+-ATPase 1 (SERCA1) Regulatory Protein in Skeletal Muscle.
MA3-927 was used in western blot to test if sAnk and SERCA interact.
|Desmond PF,Muriel J,Markwardt ML,Rizzo MA,Bloch RJ||The Journal of biological chemistry (290:27854)||2015|
Mitsugumin 56 (hedgehog acyltransferase-like) is a sarcoplasmic reticulum-resident protein essential for postnatal muscle maturation.
MA3-927 was used in western blot to investigate Mitsugumin 56 in skeletal muscle maturation using knockout mice
|Van B,Nishi M,Komazaki S,Ichimura A,Kakizawa S,Nakanaga K,Aoki J,Park KH,Ma J,Ueyama T,Ogata T,Maruyama N,Takeshima H||FEBS letters (589:1095)||2015|
Transitions of protein traffic from cardiac ER to junctional SR.
MA3-927 was used in immunocytochemistry and western blot to study cellular mechanisms for sorting and trafficking proteins to junctional sarcoplasmic reticulum
|Sleiman NH,McFarland TP,Jones LR,Cala SE||Journal of molecular and cellular cardiology (81:34)||2015|
Triadin/Junctin double null mouse reveals a differential role for Triadin and Junctin in anchoring CASQ to the jSR and regulating Ca(2+) homeostasis.
MA3-927 was used in western blot to study the roles of triadin and junctin in anchoring calsequestrin to the junctional sarcoplasmic reticulum and in Ca(2+) homeostasis using triadin/junctin (-/-) knockout mice
|Boncompagni S,Thomas M,Lopez JR,Allen PD,Yuan Q,Kranias EG,Franzini-Armstrong C,Perez CF||PloS one (7:null)||2012|
Catecholaminergic-induced arrhythmias in failing cardiomyocytes associated with human HRCS96A variant overexpression.
MA3-927 was used in western blot to investigate the relationship between histidine-rich calcium binding protein HRC S96A variant overexpression and human arrhythmias
|Han P,Cai W,Wang Y,Lam CK,Arvanitis DA,Singh VP,Chen S,Zhang H,Zhang R,Cheng H,Kranias EG||American journal of physiology. Heart and circulatory physiology (301:H1588)||2011|
Non-proteolytic functions of calpain-3 in sarcoplasmic reticulum in skeletal muscles.
MA3-927 was used in western blot to study the localization and function of calpain-3 in sarcoplasmic reticulum
|Ojima K,Ono Y,Ottenheijm C,Hata S,Suzuki H,Granzier H,Sorimachi H||Journal of molecular biology (407:439)||2011|
Ablation of skeletal muscle triadin impairs FKBP12/RyR1 channel interactions essential for maintaining resting cytoplasmic Ca2+.
MA3-927 was used in western blot to investigate the importance of triadins in the regulation of resting cytoplasmic calcium
|Eltit JM,Feng W,Lopez JR,Padilla IT,Pessah IN,Molinski TF,Fruen BR,Allen PD,Perez CF||The Journal of biological chemistry (285:38453)||2010|
Unexpected structural and functional consequences of the R33Q homozygous mutation in cardiac calsequestrin: a complex arrhythmogenic cascade in a knock in mouse model.
MA3-927 was used in western blot to investigate the structural and functional consequences of the R33Q homozygous mutation in cardiac calsequestrin in a homozygous CASQ2 (R33Q/R33Q) knock in mouse model
|Rizzi N,Liu N,Napolitano C,Nori A,Turcato F,Colombi B,Bicciato S,Arcelli D,Spedito A,Scelsi M,Villani L,Esposito G,Boncompagni S,Protasi F,Volpe P,Priori SG||Circulation research (103:298)||2008|
Regulation and function of Ca2+-calmodulin-dependent protein kinase II of fast-twitch rat skeletal muscle.
MA3-927 was used in western blot to study the regulation and function of CaMKII during exercise/contraction in rat skeletal muscle.
|Rose AJ,Alsted TJ,Kobberø JB,Richter EA||The Journal of physiology (580:993)||2007|
Increased susceptibility to isoproterenol-induced cardiac hypertrophy and impaired weight gain in mice lacking the histidine-rich calcium-binding protein.
MA3-927 was used in western blot to investigate the role of HRCBP in sarcoplasmic reticulum (SR) calcium handling
|Jaehnig EJ,Heidt AB,Greene SB,Cornelissen I,Black BL||Molecular and cellular biology (26:9315)||2006|
Microarray profiling of skeletal muscle sarcoplasmic reticulum proteins.
MA3-927 was used in western blot to investigate the skeletal muscle sarcoplasmic reticulum proteins through microarray analyses
|Schulz JS,Palmer N,Steckelberg J,Jones SJ,Zeece MG||Biochimica et biophysica acta (1764:1429)||2006|
Expression levels of RyR1 and RyR3 control resting free Ca2+ in skeletal muscle.
MA3-927 was used in western blot to investigate the effect of the transient expression of ryanodine receptor (RyR) type 3 and 1 on calcium homeostasis in skeletal muscle
|Perez CF,López JR,Allen PD||American journal of physiology. Cell physiology (288:C640)||2005|
Conformation-dependent stability of junctophilin 1 (JP1) and ryanodine receptor type 1 (RyR1) channel complex is mediated by their hyper-reactive thiols.
MA3-927 was used in immunoprecipitation to investigate the physical interaction between junctophilin 1 and ryanodine receptor type 1.
|Phimister AJ,Lango J,Lee EH,Ernst-Russell MA,Takeshima H,Ma J,Allen PD,Pessah IN||The Journal of biological chemistry (282:8667)||2007|
Cardiac-specific overexpression of mouse cardiac calsequestrin is associated with depressed cardiovascular function and hypertrophy in transgenic mice.
MA3-927 was used in immunohistochemistry to demonstrate that calsequestrin overexpression is associated with depressed cardiovascular function and hypertrophy in transgenic mice
|Sato Y,Ferguson DG,Sako H,Dorn GW,Kadambi VJ,Yatani A,Hoit BD,Walsh RA,Kranias EG||The Journal of biological chemistry (273:28470)||1998|
Role of ryanodine receptors in the assembly of calcium release units in skeletal muscle.
MA3-927 was used in immunohistochemistry to investigate the important roles of RyRs in assembling skeletal muscle's calcium release units
|Protasi F,Franzini-Armstrong C,Allen PD||The Journal of cell biology (140:831)||1998|
Effects of anti-triadin antibody on Ca2+ release from sarcoplasmic reticulum.
MA3-927 was used in blocking/activating experiment to investigate the effect of triadin blockade on calcium release from sarcoplasmic reticulum
|Brandt NR,Caswell AH,Brunschwig JP,Kang JJ,Antoniu B,Ikemoto N||FEBS letters (299:57)||1992|
cardiac triadin; junctional sarcoplasmic reticulum glycoprotein; TRDN; triadin; triadin 1; triadin 32 kDa (TRISK 32); triadin 49 kDa (TRISK 49); triadin 95; TRISK
2310045H21Rik; EG432451; TDN; TRDN