Cell Signaling Technology

Product Pathways - Cytoskeletal Signaling

Phospho-Troponin I (Cardiac) (Ser23/24) Antibody #4004

Applications Reactivity Sensitivity MW (kDa) Source
W H M R Endogenous 28 Rabbit

Applications Key:  W=Western Blotting
Reactivity Key:  H=Human  M=Mouse  R=Rat
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

Phospho-Troponin I (Cardiac) (Ser23/24) Antibody detects endogenous levels of cardiac troponin I only when phosphorylated at Ser23/24.This antibody does not cross-react with phosphorylated skeletal muscle troponin I.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser23/24 of human troponin I (cardiac). Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from mouse myocytes, untreated or stimulated with isoproterenol, using Phospho-Troponin I (Cardiac) (Ser23/24) Antibody (upper) or Troponin I Antibody #4002 (lower).

Background

Troponin, working in conjunction with tropomyosin, functions as a molecular switch, regulating muscle contraction in response to changes in the intracellular Ca2+ concentration. Troponin consists of three subunits: the Ca2+-binding subunit troponin C (TnC), the tropomyosin-binding subunit troponin T (TnT), and the inhibitory subunit troponin I (TnI) (1). In response to β-adrenergic stimulation of the heart, Ser23 and Ser24 of TnI (cardiac) are phosphorylated by PKA and PKC. This phosphorylation stimulates a conformational change of the regulatory domain of TnC, reduces the association between TnI and TnC, and decreases myofilament Ca2+ sensitivity by reducing the Ca2+ binding affinity of TnC (1-3).

  1. Ward, D.G. et al. (2002) J. Biol. Chem. 277, 41795-41801.
  2. Noland, T.A. et al. (1995) J. Biol. Chem. 270, 25445-25454.
  3. Gaponenko, V. et al. (1999) J. Biol. Chem. 274, 16681-16684.

Application References

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