Phospho-Troponin I-C (S22/S23) Polyclonal Antibody, 100µg, (ATB-P0675)

Description

Background:

Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity.

Product datasheet:

Overview
Product Description	Phospho-Troponin I-C (S22/S23) Polyclonal Antibody, 100µg, (ATB-P0675)
Image
Species Reactivities	Mouse,Rat
Immunogen	Synthesized peptide derived from human Troponin I-C around the phosphorylation site of S22/S23.
Properties
Form	Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Storage Instructions	-20°C/1 year
Clonality	Polyclonal

References:

1. Long term ablation of protein kinase A (PKA)-mediated cardiac troponin I phosphorylation leads to excitation-contraction uncoupling and diastolic dysfunction in a knock-in mouse model of hypertrophic cardiomyopathy. Dweck D, et al. J Biol Chem, 2014 Aug 15. PMID 24973218
2. Combined troponin I Ser-150 and Ser-23/24 phosphorylation sustains thin filament Ca(2+) sensitivity and accelerates deactivation in an acidic environment. Nixon BR, et al. J Mol Cell Cardiol, 2014 Jul. PMID 24657721
3. Restrictive cardiomyopathy mutations demonstrate functions of the C-terminal end-segment of troponin I. Akhter S, et al. Arch Biochem Biophys, 2014 Jun 15. PMID 24326031
4. Sexually dimorphic myofilament function and cardiac troponin I phosphospecies distribution in hypertrophic cardiomyopathy mice. McKee LA, et al. Arch Biochem Biophys, 2013 Jul 1. PMID 23352598 Free PMC Article
5. New insights into the functional significance of the acidic region of the unique N-terminal extension of cardiac troponin I. Henze M, et al. Biochim Biophys Acta, 2013 Apr. PMID 22940544 Free PMC Article
6. Structure and regulation of the mouse cardiac troponin I gene.
   Ausoni S., Campione M., Picard A., Moretti P., Vittadello M., de Nardi C., Schiaffino S.
   J. Biol. Chem. 269:339-346(1994) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
7. Mutagenesis of cardiac troponin I. Role of the unique NH2-terminal peptide in myofilament activation.
   Guo X., Wattanapermpool J., Palmiter K.A., Murphy A.M., Solaro R.J.
   J. Biol. Chem. 269:15210-15216(1994) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: CD-1.
   Tissue: Heart.
8. The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
   The MGC Project Team
   Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Heart.
9. Partial replacement of cardiac troponin I with a non-phosphorylatable mutant at serines 43/45 attenuates the contractile dysfunction associated with PKCepsilon phosphorylation.
   Scruggs S.B., Walker L.A., Lyu T., Geenen D.L., Solaro R.J., Buttrick P.M., Goldspink P.H.
   J. Mol. Cell. Cardiol. 40:465-473(2006) [PubMed] [Europe PMC] Cited for: PHOSPHORYLATION AT SER-43 AND SER-45.
10. Phosphorylation-dependent conformational transition of the cardiac specific N-extension of troponin I in cardiac troponin.
    Howarth J.W., Meller J., Solaro R.J., Trewhella J., Rosevear P.R.
    J. Mol. Biol. 373:706-722(2007) [PubMed] [Europe PMC] Cited for: STRUCTURE BY NMR OF 1-32, PHOSPHORYLATION AT SER-23 AND SER-24.