Anti-Cardiac Troponin I Anticorps [1G11] (A279108)

Anti-Cardiac Troponin I Antibody [1G11]

Mouse monoclonal [1G11] antibody to Cardiac Troponin I.

This antibody recognises the phosphorylated form of human cardiac Troponin I (cTnI). Troponin I is a 24kDa subunit of Troponin, a protein found on muscle tissue responsible for muscle contraction. When calcium binds to Troponin C, a conformational change moves Troponin I and tropomyosin out of the way of the myosin binding sites on the actin filaments in muscles. This allows cross-bridging to occur and the muscle to contract. Levels of cTnI in serum are commonly used as a marker for cardiac cell damage and death. Phosphorylation of cTnI results in changes in the activity and function of Troponin. One possible form of phosphorylation is by Protein kinase A. Protein kinase A phosphorylation of serine 22 and serine 23 reduces calcium sensitivity of Troponin and leads to an acceleration in relaxation. Changes in cTnI phosphorylation have been reported in failing hearts. recognises free cTnI and cTnI in complex with other Troponin components. It does not cross-react with skeletal Troponin I.

WB, ELISA

Human, Rat, Cat, Bovine, Dog, Goat, Pig

Phosphorylated form of human cardiac Troponin I.

Mouse

Monoclonal

1G11

IgG2b

Unconjugated

Protein A affinity chromatography of tissue culture supernatant.

Liquid

Supplied in Phosphate Buffered Saline with <0.1% Sodium Azide.

Shipped at ambient temperature. Upon delivery aliquot and store at -20°C. When thawed, aliquot the sample as needed. Short term (up to 4 weeks): store at 4°C. Long term: store at -20°C. Avoid freeze / thaw cycles. Storage in frost free freezers is not recommended.

Mouse anti Human Troponin I (Cardiac/Phosphorylated) antibody, clone 1G11 recognizes the phosphorylated form of human cardiac Troponin I (cTnI). Troponin I is a 24kDa subunit of Troponin, a protein found on muscle tissue responsible for muscle contraction. When calcium binds to Troponin C, a conformational change moves Troponin I and tropomyosin out of the way of the myosin binding sites on the actin filaments in muscles. This allows cross-bridging to occur and the muscle to contract. Levels of cTnI in serum are commonly used as a marker for cardiac cell damage and death. Phosphorylation of cTnI results in changes in the activity and function of Troponin. One possible form of phosphorylation is by Protein kinase A. Protein kinase A phosphorylation of serine 22 and serine 23 reduces calcium sensitivity of Troponin and leads to an acceleration in relaxation. Changes in cTnI phosphorylation have been reported in failing hearts. Mouse anti Human Troponin I (Cardiac/Phosphorylated) antibody, clone 1G11 recognizes free cTnI and cTnI in complex with other Troponin components. It does not cross-react with skeletal Troponin I.

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