Product Specification
| Alternative Name: | cMyBP-C, MYBPC3 |
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| Host: | Rabbit |
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| Immunogen: | Synthetic peptide corresponding to aa 276-288 (G276AGRRTpSDSHEDA288) of myosin-binding protein 2 (cardiac type) (cMyBP-C) phosphorylated at Ser282. |
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| UniProt ID: | Q14896 |
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| Species reactivity: | Human, Mouse, Rat
Dog
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| Specificity: | Recognizes cMyBP-C phosphorylated at Ser282. |
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| Applications: | ICC, WB
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| Recommended Dilutions/Conditions: | Western Blot (1:5000 or greater)
Immunocytochemistry (1:200)
Suggested dilutions/conditions may not be available for all applications.
Optimal conditions must be determined individually for each application. |
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| Application Notes: | Detects a band of ~150kDa by Western blot. |
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| Purity Detail: | Affinity-purified. |
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| Formulation: | Liquid. In phosphate buffer, pH 7.4, containing 0.1% BSA and 0.01% thimerosal. |
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| Handling: | Avoid freeze/thaw cycles. |
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| Shipping: | Shipped on Blue Ice |
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| Long Term Storage: | -20°C |
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| Scientific Background: | Myosin-binding protein 2 (cardiac type) (cMyBP-C) is a protein located in the C-zones of the A-band of the sarcomere and interacts specifically with myosin, titin and actin. Mutations in the human cMyBP-C gene are one of the most frequent causes of familial hypertrophic cardiomyopathy. cMyBP-C can be phosphorylated at three different sites by a cAMP-regulated protein kinase (PKA) and a Ca2+<-calmodulin kinase (CAMK) bound to the thick filament. The dephosphorylated form binds to the S2 subfragment of myosin whereas the phosphorylated form binds to actin. In solution, phosphorylation of cMyBP-C increases force of contraction, but both phospho- and dephosphorylated forms of cMyBP-C stimulate the actin-activated myosin ATPase activity. |
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| Regulatory Status: | RUO - Research Use Only |
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![[pSer282]Myosin-binding protein C (cardiac type) polyclonal antibody WB](https://www.enzolifesciences.com/fileadmin/files/image/215-057.gif "[pSer282]Myosin-binding protein C (cardiac type) polyclonal antibody WB")
Figure: Protein and phosphorylation levels of cMyBP-C in biopsies from patients with sinus rhythm and chronic atrial fibrillation.Upper panel: Representative immunoblots of total cMyBP-C (cMyBPC-Total), phospho-cMyBP-C (Ser282), and their densitometric analysis normalized to CSQ.Bottom panel: Specificity of Ser282 signal is demonstrated by the increase of band density in response to isoproterenol (ISO).
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Product Literature References
Lycium barbarum polysaccharides restore adverse structural remodelling and cardiac contractile dysfunction induced by overexpression of microRNA‐1: R. Zhang, et al.; J. Cell. Mol. Med.
22, 4830 (2018),
Abstract;
Full Text
β-Adrenergic regulation of cardiac type 2A protein phosphatase through phosphorylation of regulatory subunit B56δ at S573: A. Ranieri, et al.; J. Mol. Cell. Cardiol.
115, 20 (2018),
Abstract;
Full Text
Disulfide-activated protein kinase G Iα regulates cardiac diastolic relaxation and fine-tunes the Frank–Starling response: J. Scother, et al.; Nat. Commun.
7, 13187 (2016),
Abstract;
Full Text
Constitutive phosphorylation of cardiac myosin regulatory light chain in vivo: A.N. Chang, et al.; J. Biol. Chem.
290, 10703 (2015),
Abstract;
Full Text
Immobilization Stress With α2-Adrenergic Stimulation Induces Regional and Transient Reduction of Cardiac Contraction Through Gi Coupling in Rats: R. Kuroda, et al.; Int. Heart J.
56, 537 (2015),
Application(s): Western Blot,
Abstract;
Full Text
E258K HCM-causing mutation in cardiac MyBP-C reduces contractile force and accelerates twitch kinetics by disrupting the cMyBP-C and myosin S2 interaction: W.J. De Lange, et al.; J. Gen. Physiol.
142, 241 (2013),
Abstract;
Full Text
The Effects of Neuregulin on Cardiac Myosin Light Chain Kinase Gene-Ablated Hearts: A.N. Chang, et al.; PLoS One
8, e66720 (2013),
Abstract;
Full Text
The β-arrestin-biased ligand TRV120023 inhibits angiotensin II-induced cardiac hypertrophy while preserving enhanced myofilament response to calcium: M.M. Monasky, et al.; Am. J. Physiol. Heart Circ. Physiol.
305, H856 (2013),
Abstract;
Full Text
Ca²⁺ sensitization of cardiac myofilament proteins contributes to exercise training-enhanced myocardial function in a porcine model of chronic occlusion: V. Sarin, et al.; Am. J. Physiol. Heart Circ. Physiol.
301, H1579 (2011),
Abstract;
Full Text
Cardiac Myosin-binding protein C modulates the tuning of the molecular motor in the heart: Y. Lecarpentier, et al.; Biophys. J.
95, 720 (2008),
Abstract;
Full Text
Molecular determinants of altered Ca2+ handling in human chronic atrial fibrillation: A. El-Armouche, et al.; Circulation
114, 670 (2006),
Abstract;
Full Text
![[pSer282]Myosin-binding protein C (cardiac type) polyclonal antibody WB](https://www.enzolifesciences.com/fileadmin/thumbs/4348934a39cb2427236bdf5d94c9b4ba33bd33b8-215-057.gif.jpg "[pSer282]Myosin-binding protein C (cardiac type) polyclonal antibody WB")
