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

 
ALX-215-057-R050 50 µl 295.00 USD
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Product Specification

Alternative Name:cMyBP-C, MYBPC3
 
Host:Rabbit
 
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
Dog
 
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.
 
215-057
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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215-057

Product Literature References

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
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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