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[pSer282]Myosin-binding protein C (cardiac type) polyclonal antibody

ALX-215-057-R050 50 µl 354.00 USD
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Product Details

Alternative Name:cMyBP-C, MYBPC3
Immunogen:Synthetic peptide corresponding to aa 276-288 (G276AGRRTpSDSHEDA288) of myosin-binding protein 2 (cardiac type) (cMyBP-C) phosphorylated at Ser282.
UniProt ID:Q14896
Species reactivity:Human, Mouse, Rat
Specificity:Recognizes cMyBP-C phosphorylated at Ser282.
Applications:ICC, WB
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.
Application Notes:Detects a band of ~150kDa by Western blot.
Purity Detail:Affinity-purified.
Formulation:Liquid. In phosphate buffer, pH 7.4, containing 0.1% BSA and 0.01% thimerosal.
Handling:Avoid freeze/thaw cycles.
Shipping:Shipped on Blue Ice
Long Term Storage:-20°C
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.
Regulatory Status:RUO - Research Use Only
[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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[pSer282]Myosin-binding protein C (cardiac type) polyclonal antibody WB

Product Literature References

Long-Term PDE-5A Inhibition Improves Myofilament Function in Left and Right Ventricular Cardiomyocytes through Partially Different Mechanisms in Diabetic Rat Hearts: B. Bódi, et al.; Antioxidants 10, 1776 (2021), Abstract;
Pleiotropic, non-cell death-associated effects of inhibitors of receptor-interacting protein kinase 1 in the heart: C. Horvath, et al.; Mol. Cell. Biochem. 476, 3079 (2021), Abstract;
Receptor-independent modulation of cAMP-dependent protein kinase and protein phosphatase signaling in cardiac myocytes by oxidizing agents: S. Diering, et al.; J. Biol. Chem. 295, 15342 (2020), Abstract; Full Text
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

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