Technical Data
Cardiotin is a recently discovered, high molecular weight protein complex (300kD) located in the mitochondrial membrane. The cardiotin structure exists of subunits of 60kD and 100kD. Both subunits contain the same amino-terminal 14 amino-acid sequence, showing high homology to human skeletal muscle a-actinin, suggesting that the tetrameric configuration of the cardiotin protein structure is a transmembrane complex with the N-terminus at the cytoplasmic side of the membrane, able to interact with actin.

During cardiac contractile dysfunction, the cardiotin distribution is affected in pathlogical cardiomyocytes i.e. chronic ischemic myocardium. R2G and SR-2, SR-3 and SR-4, monoclonal cardiotin antibodies can be used in immunohistochemistry for the detection of a disturbed mitochondrial activity in cardiomyocytes i.e. during chronic ischemia or chronic atrial fibrillation.

Suitable for use in Immunohistochemistry (frozen and paraffin sections) and Western Blotting. Other applications not tested.

Optimal dilutions to be determined by researcher.

Storage and Stability:
May be stored at 4C for short-term only. For long-term storage, store at -20C. Aliquots are stable for at least 12 months at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
MabIgM4A18Affinity Purified
100ug-20CBlue IceHumanMouse
Purified by Protein G affinity chromatography.
Supplied as a liquid in PBS, pH 7.2, 0.09% sodium azide. No stabilizing proteins added.
This antibody reacts with the 60 and 100kD cardiotin subunits and the 300kD protein complex in immunoblotting. Reacts with cardiomyocytes, stromal and epithelial cells and tissues. Species crossreactivity: Human, porcine.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
Schaart G, Moens L, Endert JM, Ramaekers FCS - Biochemical characterization of cardiotin, a sarcoplasmic reticulum associated protein. FEBS Letters 403: 168-172 (1997).