|Tested species reactivity||Mouse, Rabbit|
|Published species reactivity||Rabbit, Mouse|
|Host / Isotype||Mouse / IgG1|
|Immunogen||Rabbit skeletal muscle triads.|
|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.
MA3-931 detects triadin from mouse and rabbit skeletal muscle tissues. This antibody does not detect triadin from cardiac tissues.
MA3-931 has been successfully used in Western blot and immunohistochemistry procedures. By Western blot, this antibody detects a single ~95 kDa band representing triadin in rabbit skeletal muscle extracts. Immunofluorescence staining of triadin in rabbit skeletal muscle with MA3-931 results in its co-localization with ryanodine receptor, which is consistent with the association of ryanodine receptor and triadin in triads.
The MA3-931 antigen is rabbit skeletal muscle triads.
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 and quote;s) of the T-tubule serve as voltage sensors in excitation-contraction coupling, while ryanodine receptors (RyR and quote;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 and quote;s and RyR and quote;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.
S-glutathionylation decreases Mg2+ inhibition and S-nitrosylation enhances Ca2+ activation of RyR1 channels.
MA3-931 was used in western blot to investigate the effect of S-glutathionylation and S-nitrosylation on the modulation of RyR1 channels by Mg2+ and calcium.
|Aracena P,Sánchez G,Donoso P,Hamilton SL,Hidalgo C||The Journal of biological chemistry (278:42927)||2003|
Supramolecular calsequestrin complex.
MA3-931 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|
Calsequestrin binds to monomeric and complexed forms of key calcium-handling proteins in native sarcoplasmic reticulum membranes from rabbit skeletal muscle.
MA3-931 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|
Low-frequency stimulation of fast muscle affects the abundance of Ca(2+)-ATPase but not its oligomeric status.
MA3-931 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|
Identification of a novel 45 kDa protein (JP-45) from rabbit sarcoplasmic-reticulum junctional-face membrane.
MA3-931 was used in western blot to characterize a novel 45kDa protein isolated from rabbit skeletal muscle sarcoplasmic reticulum junctional face membranes
|Zorzato F,Anderson AA,Ohlendieck K,Froemming G,Guerrini R,Treves S||The Biochemical journal (351 Pt 2:537)||2000|
Effects of chronic low-frequency stimulation on Ca2+-regulatory membrane proteins in rabbit fast muscle.
MA3-931 was used in western blot to study the effects of chronic low frequency stimulation of fast-twitch muscle on the levels of Ca(2+) regulatory membrane proteins
|Ohlendieck K,Frömming GR,Murray BE,Maguire PB,Leisner E,Traub I,Pette D||Pflugers Archiv : European journal of physiology (438:700)||1999|
A transgenic myogenic cell line lacking ryanodine receptor protein for homologous expression studies: reconstitution of Ry1R protein and function.
MA3-931 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|
Characterization and ultrastructural localization of a novel 90-kDa protein unique to skeletal muscle junctional sarcoplasmic reticulum.
MA3-931 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|
Phosphorylation of the 1,4-dihydropyridine receptor of the voltage-dependent Ca2+ channel by an intrinsic protein kinase in isolated triads from rabbit skeletal muscle.
MA3-931 was used in immunoprecipitation to characterize the intrinsic protein kinase in triads isolated from rabbit skeletal muscle and its function
|Imagawa T,Leung AT,Campbell KP||The Journal of biological chemistry (262:8333)||1987|