Immunofluorescent analysis of SERCA1 ATPase using Anti-SERCA1 ATPase Monoclonal Antibody (IIH11) (Product# MA3-911) shows staining in C6 Cells. SERCA1 ATPase 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 SERCA1 ATPase (Product# MA3-911) at a dilution of 1:200 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, Guinea pig, Human, Mouse, Rabbit, Rat|
|Published species reactivity||Dog, Rabbit, Rat, Mouse, Human, Not Applicable|
|Host / Isotype||Mouse / IgG1|
|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 *|
|Immunohistochemistry (Frozen) (IHC (F))||1:20-200|
|Western Blot (WB)||1:500-1:5000|
* 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.
MA3-911 detects sarcoplasmic or endoplasmic reticulum calcium 1 (SERCA1) ATPase from canine, human, rabbit, rat, mouse and guinea pig tissues.
MA3-911 has been successfully used in Western blot, immunohistochemistry, and immunofluorescence procedures. By Western blot, this antibody detects an ~110 kDa protein representing SERCA1 ATPase in canine skeletal muscle extracts. Immunofluorescence staining of SERCA1 ATPase in canine skeletal muscle with MA3-911 results in strong labeling of the entire type II (fast) myofiber.
The MA3-911 antigen is purified rabbit skeletal muscle sarcoplasmic reticulum. This antibody recognizes an epitope between amino acids 199-505 of rabbit skeletal muscle ATPase, a region that is not exposed in native sarcoplasmic reticulum.
ATP dependent calcium pumps are responsible, in part, for the maintenance of low cytoplasmic free calcium concentrations. The ATP pumps that reside in intracellular organelles are encoded by a family of structurally related enzymes, termed the sarcoplasmic or endoplasmic reticulum calcium (SERCA) ATPases. The SERCA1 gene is exclusively expressed in type II (fast) skeletal muscle. The SERCA2 gene is subject to tissue dependent processing which is responsible for the generation of SERCA2a muscle-specific form expressed in type I (slow) skeletal, cardiac and smooth muscle and the SERCA2b isoform expressed in all cell types. The SERCA3 gene is not as well characterized and is found in non-muscle cells.
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.
MA3-911 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|
Caloric restriction induces energy-sparing alterations in skeletal muscle contraction, fiber composition and local thyroid hormone metabolism that persist during catch-up fat upon refeeding.
MA3-911 was used in western blot to study the effects of caloric restriction skeletal muscle contraction, thyroid hormone metabolism, and fiber composition upon refeeding
|De Andrade PB,Neff LA,Strosova MK,Arsenijevic D,Patthey-Vuadens O,Scapozza L,Montani JP,Ruegg UT,Dulloo AG,Dorchies OM||Frontiers in physiology (6:null)||2015|
Muscle dysfunction associated with adjuvant-induced arthritis is prevented by antioxidant treatment.
MA3-911 was used in western blot to explore the mechanisms of arthritis-induced muscle dysfunction in rats with adjuvant-induced arthritis.
|Yamada T,Abe M,Lee J,Tatebayashi D,Himori K,Kanzaki K,Wada M,Bruton JD,Westerblad H,Lanner JT||Skeletal muscle (5:null)||2015|
Expression of calcium-buffering proteins in rat intrinsic laryngeal muscles.
MA3-911 was used in western blot to examine calcium-related proteins in the intrinsic laryngeal muscles, cricothyroid, and tibialis anterior muscles from male Sprague-Dawley rats
|Ferretti R,Marques MJ,Khurana TS,Santo Neto H||Physiological reports (3:null)||2015|
Mitsugumin 56 (hedgehog acyltransferase-like) is a sarcoplasmic reticulum-resident protein essential for postnatal muscle maturation.
MA3-911 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|
Higher PLIN5 but not PLIN3 content in isolated skeletal muscle mitochondria following acute in vivo contraction in rat hindlimb.
MA3-911 was used in western blot to study acute in vivo contraction in rat hindlimb and the higher level of PLIN5 and not PLIN3 in isolated skeletal muscle mitochondria
|Ramos SV,MacPherson RE,Turnbull PC,Bott KN,LeBlanc P,Ward WE,Peters SJ||Physiological reports (2:null)||2014|
Na+ dysregulation coupled with Ca2+ entry through NCX1 promotes muscular dystrophy in mice.
MA3-911 was used in western blot to study the ability of skeletal muscle-specific transgenic expression of the NCX1 exchanger to cause muscular dystrophy in a murine model
|Burr AR,Millay DP,Goonasekera SA,Park KH,Sargent MA,Collins J,Altamirano F,Philipson KD,Allen PD,Ma J,López JR,Molkentin JD||Molecular and cellular biology (34:1991)||2014|
Genetically encoded fluorescent thermosensors visualize subcellular thermoregulation in living cells.
MA3-911 was used in western blot to study subcellular thermoregulation in living cells using GFP-based thermosensors
|Kiyonaka S,Kajimoto T,Sakaguchi R,Shinmi D,Omatsu-Kanbe M,Matsuura H,Imamura H,Yoshizaki T,Hamachi I,Morii T,Mori Y||Nature methods (10:1232)||2013|
In vivo imaging of intracellular Ca2+ after muscle contractions and direct Ca2+ injection in rat skeletal muscle in diabetes.
MA3-911 was used in western blot to study Ca(2+) handling in diabetic rat skeletal muscle using in vivo imaging
|Eshima H,Tanaka Y,Sonobe T,Inagaki T,Nakajima T,Poole DC,Kano Y||American journal of physiology. Regulatory, integrative and comparative physiology (305:R610)||2013|
Isolation of sarcolemmal plasma membranes by mechanically skinning rat skeletal muscle fibers for phospholipid analysis.
MA3-911 was used in western blot to investigate the use of mechanical skinning of rat skeletal muscle to obtain sarcolemmal plasma membrane preparations for phospholipid analysis
|Fajardo VA,McMeekin L,Basic A,Lamb GD,Murphy RM,LeBlanc PJ||Lipids (48:421)||2013|
The anticancer drug tamoxifen counteracts the pathology in a mouse model of duchenne muscular dystrophy.
MA3-911 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|
Regulation and rate limiting mechanisms of Ca2+ ATPase (SERCA2) expression in cardiac myocytes.
MA3-911 was used in western blot to investigate the changes of SERCA2 levels with different treatments in heart myocytes
|Prasad AM,Inesi G||Molecular and cellular biochemistry (361:85)||2012|
Exposure to low mercury concentration in vivo impairs myocardial contractile function.
MA3-911 was used in western blot to investigate the effect of chronic mercury exposure on heart function
|Furieri LB,Fioresi M,Junior RF,Bartolomé MV,Fernandes AA,Cachofeiro V,Lahera V,Salaices M,Stefanon I,Vassallo DV||Toxicology and applied pharmacology (255:193)||2011|
Mitigation of muscular dystrophy in mice by SERCA overexpression in skeletal muscle.
MA3-911 was used in western blot to study the mechanisms by which overexpression of sarcoplasmic reticulum Ca(2+) ATPase in skeletal muscle mitigates murine muscular dystrophy.
|Goonasekera SA,Lam CK,Millay DP,Sargent MA,Hajjar RJ,Kranias EG,Molkentin JD||The Journal of clinical investigation (121:1044)||2011|
Superior calcium homeostasis of extraocular muscles.
MA3-911 was used in western blot to investigate the effect of calcium buffering on extraocular muscles
|Zeiger U,Mitchell CH,Khurana TS||Experimental eye research (91:613)||2010|
Increased store-operated Ca2+ entry in skeletal muscle with reduced calsequestrin-1 expression.
MA3-911 was used in western blot to investigate the role of calsequestrin-1 in calcium transport and homeostasis in skeletal muscle
|Zhao X,Min CK,Ko JK,Parness J,Kim DH,Weisleder N,Ma J||Biophysical journal (99:1556)||2010|
Stable structural analog of Ca2+-ATPase ADP-insensitive phosphoenzyme with occluded Ca2+ formed by elongation of A-domain/M1'-linker and beryllium fluoride binding.
MA3-911 was used in western blot to develop and evaluate a structural analog of calcium ATPase ADP-insensitive phosphoenzyme
|Daiho T,Danko S,Yamasaki K,Suzuki H||The Journal of biological chemistry (285:24538)||2010|
Aerobic exercise training improves Ca2+ handling and redox status of skeletal muscle in mice.
MA3-911 was used in western blot to investigate the effect of aerobic exercise on calcium signal and redox state of skeletal muscle
|Ferreira JC,Bacurau AV,Bueno CR,Cunha TC,Tanaka LY,Jardim MA,Ramires PR,Brum PC||Experimental biology and medicine (Maywood, N.J.) (235:497)||2010|
Succinate modulates Ca(2+) transient and cardiomyocyte viability through PKA-dependent pathway.
MA3-911 was used in western blot to study the role of succinate in calcium homeostasis and cardiomyocyte viability
|Aguiar CJ,Andrade VL,Gomes ER,Alves MN,Ladeira MS,Pinheiro AC,Gomes DA,Almeida AP,Goes AM,Resende RR,Guatimosim S,Leite MF||Cell calcium (47:37)||2010|
T-tubule disorganization and defective excitation-contraction coupling in muscle fibers lacking myotubularin lipid phosphatase.
MA3-911 was used in western blot to investigate the mechanisms for the loss of muscle function in X-linked myotubular myopathy.
|Al-Qusairi L,Weiss N,Toussaint A,Berbey C,Messaddeq N,Kretz C,Sanoudou D,Beggs AH,Allard B,Mandel JL,Laporte J,Jacquemond V,Buj-Bello A||Proceedings of the National Academy of Sciences of the United States of America (106:18763)||2009|
Effects of high-affinity inhibitors on partial reactions, charge movements, and conformational States of the Ca2+ transport ATPase (sarco-endoplasmic reticulum Ca2+ ATPase).
MA3-911 was used in western blot to investigate the mechanisms for high-affinity calcium ATPase inhibitors.
|Tadini-Buoninsegni F,Bartolommei G,Moncelli MR,Tal DM,Lewis D,Inesi G||Molecular pharmacology (73:1134)||2008|
Conformational fluctuations of the Ca2+-ATPase in the native membrane environment. Effects of pH, temperature, catalytic substrates, and thapsigargin.
MA3-911 was used in western blot to study the effects of various parameters on the conformational fluctuations of the SERCA Ca(2+)-ATPase in its native membrane environment
|Inesi G,Lewis D,Toyoshima C,Hirata A,de Meis L||The Journal of biological chemistry (283:1189)||2008|
Proteomic profiling of chronic low-frequency stimulated fast muscle.
MA3-911 was used in western blot to study changes in the proteomic profile of fast muscle subjected to chronic low frequency stimulation
|Donoghue P,Doran P,Wynne K,Pedersen K,Dunn MJ,Ohlendieck K||Proteomics (7:3417)||2007|
Sarco(endo)plasmic reticulum calcium pump isoforms in paralyzed rat slow muscle.
MA3-911 was used in western blot to examine the effects of spinal cord transection on sarco(endo)plasmic reticulum calcium ATPase pump isoform protein levels in the slow rat soleus
|Talmadge RJ,Paalani M||Biochimica et biophysica acta (1770:1187)||2007|
Thermogenic activity of Ca2+-ATPase from skeletal muscle heavy sarcoplasmic reticulum: the role of ryanodine Ca2+ channel.
MA3-911 was used in western blot to study the thermogenic activity of Ca2+-ATPase from skeletal muscle heavy sarcoplasmic reticulum
|Arruda AP,Nigro M,Oliveira GM,de Meis L||Biochimica et biophysica acta (1768:1498)||2007|
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.
MA3-911 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.
MA3-911 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|
Interference with phosphoenzyme isomerization and inhibition of the sarco-endoplasmic reticulum Ca2+ ATPase by 1,3-dibromo-2,4,6-tris(methylisothiouronium) benzene.
MA3-911 was used in western blot to study the effect of 1,3-dibromo-2,4,6-tris(methylisothiouronium) benzene on the sarco-endoplasmic reticulum calcium ATPase.
|Hua S,Xu C,Ma H,Inesi G||The Journal of biological chemistry (280:17579)||2005|
Expression levels of RyR1 and RyR3 control resting free Ca2+ in skeletal muscle.
MA3-911 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|
Subproteomics analysis of Ca+-binding proteins demonstrates decreased calsequestrin expression in dystrophic mouse skeletal muscle.
MA3-911 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 (271:3943)||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.
MA3-911 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|
Skeletal muscle sarcoplasmic reticulum glycogen status influences Ca2+ uptake supported by endogenously synthesized ATP.
MA3-911 was used in western blot to investigate the impact of sarcoplasmic reticulum (SR) glycogen status on SR calcium handling
|Lees SJ,Williams JH||American journal of physiology. Cell physiology (286:C97)||2004|
Hyperthyroidism increases the uncoupled ATPase activity and heat production by the sarcoplasmic reticulum Ca2+-ATPase.
MA3-911 was used in western blot to study the effects of T4 treatment on uncoupled ATPase activity and heat production by the sarcoplasmic reticulum Ca(2+)-ATPase and the significance for hyperthyroidism
|Arruda AP,Da-Silva WS,Carvalho DP,De Meis L||The Biochemical journal (375:753)||2003|
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.
MA3-911 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|
Mechanisms underlying increases in SR Ca2+-ATPase activity after exercise in rat skeletal muscle.
MA3-911 was used in western blot to investigate the mechanism for the increase in sarcoplasmic reticulum caclium-ATPase activity after exercise in rat skeletal muscle
|Schertzer JD,Green HJ,Duhamel TA,Tupling AR||American journal of physiology. Endocrinology and metabolism (284:E597)||2003|
Increased expression of the nicotinic acetylcholine receptor in stimulated muscle.
MA3-911 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.
MA3-911 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 (269:4607)||2002|
Drastic reduction of calsequestrin-like proteins and impaired calcium binding in dystrophic mdx muscle.
MA3-911 was used in western blot to characterize the changes of calsequestrin-like proteins in dystrophic mdx muscle
|Culligan K,Banville N,Dowling P,Ohlendieck K||Journal of applied physiology (Bethesda, Md. : 1985) (92:435)||2002|
Effects of moderate heart failure and functional overload on rat plantaris muscle.
MA3-911 was used in western blot to characterize the changes of rat plantaris muscles caused by moderate heart failure and functional overload
|Spangenburg EE,Lees SJ,Otis JS,Musch TI,Talmadge RJ,Williams JH||Journal of applied physiology (Bethesda, Md. : 1985) (92:18)||2002|
Calsequestrin binds to monomeric and complexed forms of key calcium-handling proteins in native sarcoplasmic reticulum membranes from rabbit skeletal muscle.
MA3-911 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|
Native skeletal muscle dihydropyridine receptor exists as a supramolecular triad complex.
MA3-911 was used in western blot to study the structure of the native skeletal muscle dihydropyridine receptor
|Froemming GR,Ohlendieck K||Cellular and molecular life sciences : CMLS (58:312)||2001|
Low-frequency stimulation of fast muscle affects the abundance of Ca(2+)-ATPase but not its oligomeric status.
MA3-911 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|
Comparative analysis of the isoform expression pattern of Ca(2+)-regulatory membrane proteins in fast-twitch, slow-twitch, cardiac, neonatal and chronic low-frequency stimulated muscle fibers.
MA3-911 was used in western blot to study the expression of Ca(2+) regulatory membrane protein isoforms in skeletal, cardiac and neonatal muscle fibres
|Froemming GR,Murray BE,Harmon S,Pette D,Ohlendieck K||Biochimica et biophysica acta (1466:151)||2000|
Protein modification during biological aging: selective tyrosine nitration of the SERCA2a isoform of the sarcoplasmic reticulum Ca2+-ATPase in skeletal muscle.
MA3-911 was used in western blot to investigate the modification of SERCA1 and SERCA2a related to aging in rat skeletal muscle
|Viner RI,Ferrington DA,Williams TD,Bigelow DJ,Schöneich C||The Biochemical journal (340 ( Pt 3):657)||1999|
Dyspedic mouse skeletal muscle expresses major elements of the triadic junction but lacks detectable ryanodine receptor protein and function.
MA3-911 was used in western blot to demonstrate that the proteins expressed in dyspedic skeletal muscle in the absence of Ry1R are critical for ryanodine receptor function
|Buck ED,Nguyen HT,Pessah IN,Allen PD||The Journal of biological chemistry (272:7360)||1997|
Transcriptional regulation of phospholamban gene and translational regulation of SERCA2 gene produces coordinate expression of these two sarcoplasmic reticulum proteins during skeletal muscle phenotype switching.
MA3-911 was used in western blot to investigate how coordinated expression of SERCA2a and phospholamban is achieved during skeletal muscle phenotype switching
|Hu P,Yin C,Zhang KM,Wright LD,Nixon TE,Wechsler AS,Spratt JA,Briggs FN||The Journal of biological chemistry (270:11619)||1995|
Analysis of excitation-contraction-coupling components in chronically stimulated canine skeletal muscle.
MA3-911 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 (202:739)||1991|
Vesicular transport system in myotubes: ultrastructural study and signposting with vesicle-associated membrane proteins.
MA3-911 was used in immunocytochemistry to study the morphology of the myotube vesicular transport system
|Tajika Y,Takahashi M,Khairani AF,Ueno H,Murakami T,Yorifuji H||Histochemistry and cell biology (141:441)||2014|
Myosin heavy chain and physiological adaptation of the rat diaphragm in elastase-induced emphysema.
MA3-911 was used in immunocytochemistry to examine MHC and to find related physiological changes in the diaphragms of rats with emphysema
|Kim DK,Zhu J,Kozyak BW,Burkman JM,Rubinstein NA,Lankford EB,Stedman HH,Nguyen T,Levine S,Shrager JB||Respiratory research (4:null)||2003|
Primary over-expression of AßPP in muscle does not lead to the development of inclusion body myositis in a new lineage of the MCK-AßPP transgenic mouse.
MA3-911 was used in immunohistochemistry to study the lack of inclusion body myositis resulting from skeletal muscle AbetaPP overexpression in a novel lineage of the MCK-AbetaPP transgenic mouse
|Luo YB,Johnsen RD,Griffiths L,Needham M,Fabian VA,Fletcher S,Wilton SD,Mastaglia FL||International journal of experimental pathology (94:418)||2013|
Diaphragm muscle remodeling in a rat model of chronic intermittent hypoxia.
MA3-911 was used in immunohistochemistry to study the differential effects of chronic intermittent hypoxia on the remodeling of rat diaphragm and sternohyoid muscles
|Shortt CM,Fredsted A,Bradford A,O'Halloran KD||The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society (61:487)||2013|
Defects in amphiphysin 2 (BIN1) and triads in several forms of centronuclear myopathies.
MA3-911 was used in immunohistochemistry to investigate the effect of BIN1 dysfunction on the pathogenesis of centronuclear myopathies
|Toussaint A,Cowling BS,Hnia K,Mohr M,Oldfors A,Schwab Y,Yis U,Maisonobe T,Stojkovic T,Wallgren-Pettersson C,Laugel V,Echaniz-Laguna A,Mandel JL,Nishino I,Laporte J||Acta neuropathologica (121:253)||2011|
Calsequestrin and junctin immunoreactivity in hexagonally cross-linked tubular arrays myopathy.
MA3-911 was used in immunohistochemistry to investigate the immunohistochemical features of hexagonally cross-linked tubular arrays myopathy
|Di Blasi C,Blasevich F,Bellafiore E,Mottarelli E,Gibertini S,Zanotti S,Saredi S,Mantegazza R,Morandi L,Mora M||Neuromuscular disorders : NMD (20:326)||2010|
Fusion of the endoplasmic reticulum and mitochondrial outer membrane in rats brown adipose tissue: activation of thermogenesis by Ca2+.
MA3-911 was used in immunohistochemistry to study the fusion of the ER and the mitochonrial outer membrane in brown adipose tissue and activation of thermogenesis by Ca2+
|de Meis L,Ketzer LA,da Costa RM,de Andrade IR,Benchimol M||PloS one (5:null)||2010|
SRP-27 is a novel component of the supramolecular signalling complex involved in skeletal muscle excitation-contraction coupling.
MA3-911 was used in immunohistochemistry to investigate the distribution of SRP-27 in muscle SR and ER
|Bleunven C,Treves S,Jinyu X,Leo E,Ronjat M,De Waard M,Kern G,Flucher BE,Zorzato F||The Biochemical journal (411:343)||2008|
Identification of a Ca2+-ATPase in brown adipose tissue mitochondria: regulation of thermogenesis by ATP and Ca2+.
MA3-911 was used in immunohistochemistry to investigate the role of the calcium ATPase in mitochondria during the thermogenesis.
|de Meis L,Arruda AP,da Costa RM,Benchimol M||The Journal of biological chemistry (281:16384)||2006|
Sarco(endo)plasmic reticulum Ca2+ ATPases (SERCA1 and -2) in human extraocular muscles.
MA3-911 was used in immunohistochemistry to identify SERCA1 and SERCA2 in human extraocular muscles.
|Kjellgren D,Ryan M,Ohlendieck K,Thornell LE,Pedrosa-Domellöf F||Investigative ophthalmology and visual science (44:5057)||2003|
Identification of Ank(G107), a muscle-specific ankyrin-G isoform.
MA3-911 was used in immunohistochemistry to characterize a muscle-specific ankyrin-G isoform AnkG107.
|Gagelin C,Constantin B,Deprette C,Ludosky MA,Recouvreur M,Cartaud J,Cognard C,Raymond G,Kordeli E||The Journal of biological chemistry (277:12978)||2002|
Two isoforms of sarco/endoplasmic reticulum calcium ATPase (SERCA) are essential in Caenorhabditis elegans.
MA3-911 was used in immunohistochemistry to investigate the role of sarco/endoplasmic reticulum calcium ATPase isoforms in Caenorhabditis elegans
|Cho JH,Bandyopadhyay J,Lee J,Park CS,Ahnn J||Gene (261:211)||2000|
Type 3 and type 1 ryanodine receptors are localized in triads of the same mammalian skeletal muscle fibers.
MA3-911 was used in immunohistochemistry to demonstrate that RyR3 and RyR1 are localized in the same mammalian skeletal muscle fibers.
|Flucher BE,Conti A,Takeshima H,Sorrentino V||The Journal of cell biology (146:621)||1999|
Small, membrane-bound, alternatively spliced forms of ankyrin 1 associated with the sarcoplasmic reticulum of mammalian skeletal muscle.
MA3-911 was used in immunohistochemistry to study the association of ankyrin splice variant with sarcoplasmic reticulum of mammalian skeletal muscle.
|Zhou D,Birkenmeier CS,Williams MW,Sharp JJ,Barker JE,Bloch RJ||The Journal of cell biology (136:621)||1997|
Characterization and ultrastructural localization of a novel 90-kDa protein unique to skeletal muscle junctional sarcoplasmic reticulum.
MA3-911 was used in immunohistochemistry to study a novel 90 kDa protein specifically localized to the junctional SR of rabbit skeletal muscle
|Guo W,Jorgensen AO,Campbell KP||The Journal of biological chemistry (269:28359)||1994|
Biochemical characterization of ultrastructural localization of a major junctional sarcoplasmic reticulum glycoprotein (triadin).
MA3-911 was used in immunohistochemistry to investigate the expression and distribution of triadin in sarcoplasmic reticulum
|Knudson CM,Stang KK,Jorgensen AO,Campbell KP||The Journal of biological chemistry (268:12637)||1993|