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Immunofluorescent analysis of Calsequestrin using Anti-Calsequestrin Monoclonal Antibody (VIIID12) (Product# MA3-913) shows staining in MCF-7 Cells. Calsequestrin staining (green), F-Actin staining with Phalloidin (red) and nuclei with DAPI (blue) is shown. Cells were grown on chamber slides and fixed with formaldehyde prior to staining. Cells were probed without (control) or with or an antibody recognizing Calsequestrin (Product# MA3-913) at a dilution of 1:100 over night at 4 °C, washed with PBS and incubated with a DyLight-488 conjugated secondary antibody (Product# 35503, Goat Anti-Mouse). Images were taken at 60X magnification.
|Tested species reactivity||Dog, Chicken, Human, Mouse, Pig, Rabbit, Rat|
|Published species reactivity||Dog, Rabbit, Rat, Pig, Rodent, Mouse, Human, Chicken|
|Host / Isotype||Mouse / IgG2b|
|Immunogen||Purified rabbit skeletal muscle sarcoplasmic reticulum.|
|Storage buffer||ascites diluted in PBS|
|Contains||0.05% sodium azide|
|Storage Conditions||-20° C, Avoid Freeze/Thaw Cycles|
|Tested Applications||Dilution *|
|Western Blot (WB)||1:1,000|
* 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.
MA3-913 detects calsequestrin from human, mouse, rat, canine, porcine, chicken, and rabbit skeletal muscle tissues. This antibody recognizes calsequestrin in both type I (slow) and type II (fast) skeletal muscle tissues.
MA3-913 has been successfully used in Western blot procedures. By Western blot, this antibody detects a 63 kDa protein representing calsequestrin from canine skeletal muscle extracts. Higher molecular weight proteins are seen on the Western blot and are believed to be calsequestrin-like proteins found in the sarcoplasmic reticulum. The staining pattern yields double rows of fluorescent dots corresponding to triad pairs on either side of the Z-line.
The MA3-913 antigen is purified rabbit skeletal muscle sarcoplasmic reticulum.
The sarcoplasmic reticulum (SR) is, in part, responsible for maintaining the level of intracellular calcium in cardiac and skeletal muscle by storing and releasing calcium. Several intralumenal SR calcium binding proteins have been identified, the most prominent of these is calsequestrin. Calsequstrin is a calcium binding protein known to sequester calcium accumulated in the sarcoplasmic reticulum of muscle cells during relaxation and is found discretely localized to the junctional and corbular (terminal cisternae) SR. Calsequestrin functions to localize calcium near the junctional face of the terminal cisternae from which calcium can be released into the cytosol via the ryanodine receptor. This protein is highly acidic and has a large capacity and moderate to low affinity for calcium.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
A mutation in the CASQ1 gene causes a vacuolar myopathy with accumulation of sarcoplasmic reticulum protein aggregates.
MA3-913 was used in immunohistochemistry to study a missense mutation in the calsequestrin-1 gene discovered in a group of patients with a myopathy
|Rossi D,Vezzani B,Galli L,Paolini C,Toniolo L,Pierantozzi E,Spinozzi S,Barone V,Pegoraro E,Bello L,Cenacchi G,Vattemi G,Tomelleri G,Ricci G,Siciliano G,Protasi F,Reggiani C,Sorrentino V||Human mutation (35:1163)||2014|
Restricted distribution of mRNAs encoding a sarcoplasmic reticulum or transverse tubule protein in skeletal myofibers.
MA3-913 was used in immunohistochemistry to investigate the distribution of CSQ and DHPR proteins and corresponding mRNAs during myogenic development
|Nissinen M,Kaisto T,Salmela P,Peltonen J,Metsikkö K||The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society (53:217)||2005|
The stress protein/chaperone Grp94 counteracts muscle disuse atrophy by stabilizing subsarcolemmal neuronal nitric oxide synthase.
MA3-913 was used in western blot to study the role of sarcolemmal nNOS in the mechanism by which Gpr94 protects against atrophy in a rat model of muscle disuse
|Vitadello M,Gherardini J,Gorza L||Antioxidants & redox signaling (20:2479)||2014|
Application of fluorescence two-dimensional difference in-gel electrophoresis as a proteomic biomarker discovery tool in muscular dystrophy research.
MA3-913 was used in western blot to perform a comparative proteomic analysis of normal and dystrophic muscle using fluoresent difference in-gel electrophoresis
|Carberry S,Zweyer M,Swandulla D,Ohlendieck K||Biology (2:1438)||2014|
Distinct regions of triadin are required for targeting and retention at the junctional domain of the sarcoplasmic reticulum.
MA3-913 was used in western blot to study three regions of triadin that are involved in its targeting to the sarcoplasmic reticulum junctional domain
|Rossi D,Bencini C,Maritati M,Benini F,Lorenzini S,Pierantozzi E,Scarcella AM,Paolini C,Protasi F,Sorrentino V||The Biochemical journal (458:407)||2014|
Altered Ca2+ concentration, permeability and buffering in the myofibre Ca2+ store of a mouse model of malignant hyperthermia.
MA3-913 was used in western blot to study myofibre Ca(2+) metabolism in a murine model of malignant hyperthermia
|Manno C,Figueroa L,Royer L,Pouvreau S,Lee CS,Volpe P,Nori A,Zhou J,Meissner G,Hamilton SL,Ríos E||The Journal of physiology (591:4439)||2013|
Myotubularin and PtdIns3P remodel the sarcoplasmic reticulum in muscle in vivo.
MA3-913 was used in western blot to study the role of the phosphoinositide phosphatase myotublarin in the remodeling of skeletal muscle sarcoplasmic reticulum
|Amoasii L,Hnia K,Chicanne G,Brech A,Cowling BS,Müller MM,Schwab Y,Koebel P,Ferry A,Payrastre B,Laporte J||Journal of cell science (126:1806)||2013|
The anticancer drug tamoxifen counteracts the pathology in a mouse model of duchenne muscular dystrophy.
MA3-913 was used in western blot to study the beneficial effects of tamoxifen on muscle force and structure in a murine model of Duchenne muscular dystrophy
|Dorchies OM,Reutenauer-Patte J,Dahmane E,Ismail HM,Petermann O,Patthey- Vuadens O,Comyn SA,Gayi E,Piacenza T,Handa RJ,Décosterd LA,Ruegg UT||The American journal of pathology (182:485)||2013|
Abnormalities of calcium handling proteins in skeletal muscle mirror those of the heart in humans with heart failure: a shared mechanism?
MA3-913 was used in western blot to investigate the abnormalities of calcium handling proteins in skeletal and heart muscle during heart failure
|Middlekauff HR,Vigna C,Verity MA,Fonarow GC,Horwich TB,Hamilton MA,Shieh P,Tupling AR||Journal of cardiac failure (18:724)||2012|
Triadin/Junctin double null mouse reveals a differential role for Triadin and Junctin in anchoring CASQ to the jSR and regulating Ca(2+) homeostasis.
MA3-913 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|
Functional expression of transgenic 1sDHPR channels in adult mammalian skeletal muscle fibres.
MA3-913 was used in western blot to investigate the effect of alpha1sDHPR overexpression on calcium signaling in muscle fibers
|DiFranco M,Tran P,Quiñonez M,Vergara JL||The Journal of physiology (589:1421)||2011|
Ablation of skeletal muscle triadin impairs FKBP12/RyR1 channel interactions essential for maintaining resting cytoplasmic Ca2+.
MA3-913 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|
Proteomic profiling of naturally protected extraocular muscles from the dystrophin-deficient mdx mouse.
MA3-913 was used in western blot to conduct proteomic profiling of extraocular muscles in Duchenne muscular dystrophy mouse model
|Lewis C,Ohlendieck K||Biochemical and biophysical research communications (396:1024)||2010|
Triadin deletion induces impaired skeletal muscle function.
MA3-913 was used in western blot to study the role of triadin in skeletal muscle function
|Oddoux S,Brocard J,Schweitzer A,Szentesi P,Giannesini B,Brocard J,Fauré J,Pernet-Gallay K,Bendahan D,Lunardi J,Csernoch L,Marty I||The Journal of biological chemistry (284:34918)||2009|
Altered contractility of skeletal muscle in mice deficient in titin's M-band region.
MA3-913 was used in western blot to investigate the role of M-band region of titin in muscle contraction
|Ottenheijm CA,Hidalgo C,Rost K,Gotthardt M,Granzier H||Journal of molecular biology (393:10)||2009|
Diltiazem and verapamil protect dystrophin-deficient muscle fibers of MDX mice from degeneration: a potential role in calcium buffering and sarcolemmal stability.
MA3-913 was used in western blot to study the novel role of diltiazem and verapamil in calcium homeostasis and sarcolemmal stability
|Matsumura CY,Pertille A,Albuquerque TC,Santo Neto H,Marques MJ||Muscle & nerve (39:167)||2009|
Reduced expression of sarcalumenin and related Ca2+ -regulatory proteins in aged rat skeletal muscle.
MA3-913 was used in western blot to investigate the expression of sarcalumenin and related calcium-regulatory proteins in rodent skeletal muscle during aging
|O'Connell K,Gannon J,Doran P,Ohlendieck K||Experimental gerontology (43:958)||2008|
Triadins modulate intracellular Ca(2+) homeostasis but are not essential for excitation-contraction coupling in skeletal muscle.
MA3-913 was used in western blot to investigate the role of triadins in intracellular calcium homeostasis and excitation-contraction coupling in skeletal muscle.
|Shen X,Franzini-Armstrong C,Lopez JR,Jones LR,Kobayashi YM,Wang Y,Kerrick WG,Caswell AH,Potter JD,Miller T,Allen PD,Perez CF||The Journal of biological chemistry (282:37864)||2007|
Identification of a novel phosphorylation site in protein phosphatase inhibitor-1 as a negative regulator of cardiac function.
MA3-913 was used in western blot to study the mechanism for cardiac contractility regulation
|Rodriguez P,Mitton B,Waggoner JR,Kranias EG||The Journal of biological chemistry (281:38599)||2006|
Microarray profiling of skeletal muscle sarcoplasmic reticulum proteins.
MA3-913 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|
Reduced expression of regucalcin in young and aged mdx diaphragm indicates abnormal cytosolic calcium handling in dystrophin-deficient muscle.
MA3-913 was used in western blot to study the reduced regucalcin expression observed in diaphragm muscle in muscular dystrophy and the significance for calcium handling
|Doran P,Dowling P,Donoghue P,Buffini M,Ohlendieck K||Biochimica et biophysica acta (1764:773)||2006|
Expression of the skeletal muscle dystrophin-dystroglycan complex and syntrophin-nitric oxide synthase complex is severely affected in the type 2 diabetic Goto-Kakizaki rat.
MA3-913 was used in western blot to study the reduced expression of the dystrophin-dystroglycan complex and the syntrophin-NOS complex in skeletal muscle of type 2 diabetic rats and the significance for insulin resistance
|Mulvey C,Harno E,Keenan A,Ohlendieck K||European journal of cell biology (84:867)||2005|
Differential expression of the fast skeletal muscle proteome following chronic low-frequency stimulation.
MA3-913 was used in western blot to study the effects of chronic low frequency stimulation on the proteome of fast muscle fibres
|Donoghue P,Doran P,Dowling P,Ohlendieck K||Biochimica et biophysica acta (1752:166)||2005|
Triadins are not triad-specific proteins: two new skeletal muscle triadins possibly involved in the architecture of sarcoplasmic reticulum.
MA3-913 was used in western blot to demonstrate the role of two new skeletal muscle triadins in sarcoplasmic reticulum structure.
|Vassilopoulos S,Thevenon D,Rezgui SS,Brocard J,Chapel A,Lacampagne A,Lunardi J,Dewaard M,Marty I||The Journal of biological chemistry (280:28601)||2005|
Subproteomics analysis of Ca+-binding proteins demonstrates decreased calsequestrin expression in dystrophic mouse skeletal muscle.
MA3-913 was used in western blot to study the reduced expression of calsequestrin in dystrophic mouse skeletal muscle
|Doran P,Dowling P,Lohan J,McDonnell K,Poetsch S,Ohlendieck K||European journal of biochemistry / FEBS (271:3943)||2004|
Transcriptional changes following restoration of SERCA2a levels in failing rat hearts.
MA3-913 was used in western blot to characterize the effect of SERCA2a on transcriptional activity in failing rat hearts
|Del Monte F,Dalal R,Tabchy A,Couget J,Bloch KD,Peterson R,Hajjar RJ||FASEB journal : official publication of the Federation of American Societies for Experimental Biology (18:1474)||2004|
Insights into cardioprotection obtained from study of cellular Ca2+ handling in myocardium of true hibernating mammals.
MA3-913 was used in western blot to study mammalian hibernators' inborn cardioprotective functions during hibernation
|Yatani A,Kim SJ,Kudej RK,Wang Q,Depre C,Irie K,Kranias EG,Vatner SF,Vatner DE||American journal of physiology. Heart and circulatory physiology (286:H2219)||2004|
Drastic reduction of sarcalumenin in Dp427 (dystrophin of 427 kDa)-deficient fibres indicates that abnormal calcium handling plays a key role in muscular dystrophy.
MA3-913 was used in western blot to study the markedly reduced levels of sarcalumenin in Dp427-deficient muscle fibres and the pathological significance of the resulting abnormal Ca(2+) metabolism
|Dowling P,Doran P,Ohlendieck K||The Biochemical journal (379:479)||2004|
Increased sensitivity of the ryanodine receptor to halothane-induced oligomerization in malignant hyperthermia-susceptible human skeletal muscle.
MA3-913 was used in western blot to investigate the importance of RyR2 complex formation in the development of a metabolic crisis in malignant hyperthermia
|Glover L,Heffron JJ,Ohlendieck K||Journal of applied physiology (Bethesda, Md. : 1985) (96:11)||2004|
Comparative analysis of Dp427-deficient mdx tissues shows that the milder dystrophic phenotype of extraocular and toe muscle fibres is associated with a persistent expression of beta-dystroglycan.
MA3-913 was used in western blot to study the relative preservation of beta-dystoglycan in extraocular and toe muscles as the reason of the mild dystrophic phenotype of these tissues in Dp427-defficient muscular dystrophy
|Dowling P,Lohan J,Ohlendieck K||European journal of cell biology (82:222)||2003|
Increased expression of the nicotinic acetylcholine receptor in stimulated muscle.
MA3-913 was used in western blot to study the effect of chronic low frequency stimulation on nicotinic acetylcholine receptor expression in skeletal muscle
|O'Reilly C,Pette D,Ohlendieck K||Biochemical and biophysical research communications (300:585)||2003|
Supramolecular calsequestrin complex.
MA3-913 was used in western blot to investigate the formation of supramolecular calsequestrin complex
|Glover L,Quinn S,Ryan M,Pette D,Ohlendieck K||European journal of biochemistry / FEBS (269:4607)||2002|
Calsequestrin binds to monomeric and complexed forms of key calcium-handling proteins in native sarcoplasmic reticulum membranes from rabbit skeletal muscle.
MA3-913 was used in western blot to study the binding of calcium handling proteins to calsequestrin in rabbit skeletal muscle sarcoplasmic reticulum membranes
|Glover L,Culligan K,Cala S,Mulvey C,Ohlendieck K||Biochimica et biophysica acta (1515:120)||2001|
Expression of endoplasmic reticulum stress proteins during skeletal muscle disuse atrophy.
MA3-913 was used in western blot to study the expression of endoplasmic reticulum stress proteins during skeletal muscle disuse atrophy
|Hunter RB,Mitchell-Felton H,Essig DA,Kandarian SC||American journal of physiology. Cell physiology (281:C1285)||2001|
Improvement in survival and cardiac metabolism after gene transfer of sarcoplasmic reticulum Ca(2+)-ATPase in a rat model of heart failure.
MA3-913 was used in western blot to study the effect of SERCA2a gene transfer into failing rodent hearts.
|del Monte F,Williams E,Lebeche D,Schmidt U,Rosenzweig A,Gwathmey JK,Lewandowski ED,Hajjar RJ||Circulation (104:1424)||2001|
Glucocorticoids increase sodium pump alpha(2)- and beta(1)-subunit abundance and mRNA in rat skeletal muscle.
MA3-913 was used in western blot to investigate the role of glucocorticoids on sodium pump alpha (2)- and beta (1)-subunit abundance in muscle
|Thompson CB,Dorup I,Ahn J,Leong PK,McDonough AA||American journal of physiology. Cell physiology (280:C509)||2001|
Low-frequency stimulation of fast muscle affects the abundance of Ca(2+)-ATPase but not its oligomeric status.
MA3-913 was used in western blot to investigate the possible effects of stimulation-induced changes in the abundance of calcium pump on protein-protein interactions
|Harmon S,Froemming GR,Leisner E,Pette D,Ohlendieck K||Journal of applied physiology (Bethesda, Md. : 1985) (90:371)||2001|
Exogenous Ca2+-ATPase isoform effects on Ca2+ transients of embryonic chicken and neonatal rat cardiac myocytes.
MA3-913 was used in western blot to investigate the role of calsequestrin during the regulation of calcium by sarco-endoplasmic reticulum calcium-ATPase in skeletal and cardiac muscle.
|Cavagna M,O'Donnell JM,Sumbilla C,Inesi G,Klein MG||The Journal of physiology (528 Pt 1:53)||2000|
A transgenic myogenic cell line lacking ryanodine receptor protein for homologous expression studies: reconstitution of Ry1R protein and function.
MA3-913 was used in western blot to characterize a transgenic myogenic cell line without functioning skeletal muscle ryanodine receptor.
|Moore RA,Nguyen H,Galceran J,Pessah IN,Allen PD||The Journal of cell biology (140:843)||1998|
Effects of aging on in vivo synthesis of skeletal muscle myosin heavy-chain and sarcoplasmic protein in humans.
MA3-913 was used in western blot to investigate the effects of age on the synthesis rate of myosin heavy chain and sarcoplasmic protein in humans
|Balagopal P,Rooyackers OE,Adey DB,Ades PA,Nair KS||The American journal of physiology (273:E790)||1997|
Analysis of excitation-contraction-coupling components in chronically stimulated canine skeletal muscle.
MA3-913 was used in western blot to investigate the protein components of skeletal muscle membranes in canine muscle
|Ohlendieck K,Briggs FN,Lee KF,Wechsler AW,Campbell KP||European journal of biochemistry / FEBS (202:739)||1991|
Calcium-binding proteins in skeletal muscles of the mdx mice: potential role in the pathogenesis of Duchenne muscular dystrophy.
MA3-913 was used in immunocytochemistry to study the role of calcium-binding proteins in the pathogenesis of Duchenne muscular dystrophy
|Pertille A,de Carvalho CL,Matsumura CY,Neto HS,Marques MJ||International journal of experimental pathology (91:63)||2010|
Dynamic localization and clustering of dendritic Kv2.1 voltage-dependent potassium channels in developing hippocampal neurons.
MA3-913 was used in immunocytochemistry to study the distribution of Kv2.1 channels in developing rat hippocampal neurons
|Antonucci DE,Lim ST,Vassanelli S,Trimmer JS||Neuroscience (108:69)||2001|
Conformation-dependent stability of junctophilin 1 (JP1) and ryanodine receptor type 1 (RyR1) channel complex is mediated by their hyper-reactive thiols.
MA3-913 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|
Aspartactin; calmitin; calmitine; calsequestrin 1 (fast-twitch, skeletal muscle); calsequestrin, skeletal muscle isoform; calsequestrin-1; Casq1; Csq; Laminin-binding protein; skeletal muscle calsequestrin 1
CASQ; CASQ1; CSQ; CSQ-1; CSQ1; PDIB1; sCSQ; VMCQA