Technical Data
C1384-01
Cardiotin
Description:
Cardiotin is a high molecular weight protein complex (300kD) located in the mitochondria of cardiomyocytes and skeletal muscle. The cardiotin structure exists of subunits of 60kD and 100kD, probably in a tetrameric configuration. Both subunits contain the same amino-terminal 14 amino-acid sequence, showing high homology to human skeletal muscle alpha-actinin.

During cardiac contractile dysfunction and myocard cell differentiation, the cardiotin distribution is affected. Compared to other structural proteins, cardiotin is one of the first to respond to insults (ischemia, fibrillation) that influence the functional status of cardiomyocytes.

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

Recommended Dilution:
Immunohistochemistry: 1:25-1:100
Western Blot: 1:25-1:500

Optimal dilutions to be determined by researcher.

Hybridoma:
Derived by fusion of SP2/0-Ag14 mouse myeloma cells, with spleen cells from a mouse.

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.
TypeIsotypeCloneGrade
MabIgM4A17Affinity Purified
SizeStorageShippingSourceHost
100ug-20CBlue IceHumanMouse
Concentration:
1mg/ml
Immunogen:
Total protein extract of chicken gizzard.
Purity:
Purified by Protein G affinity chromatography.
Form
Supplied as a liquid in PBS, pH 7.2, 0.1% sodium azide. No stabilizing proteins added.
Specificity:
Recognizes cardiotin. Reacts with a 300kD protein complex and its 100kD and 60kD subunits in Western Blotting assays. Reacts exclusively with cardiomyocytes. Species crossreactivity: Human, monkey, porcine, feline, canine, goat, hamster, mouse, Xenopus.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Schaart, G., van der Ven, P. F., and Ramaekers, F. C. (1993). Characterization of cardiotin, a structural component in the myocard, Eur J Cell Biol 62, 34-48.
2. Schaart, G., Moens, L., Endert, J. M., and Ramaekers, F. C. (1997). Biochemical characterization of cardiotin, a sarcoplasmic reticulum associated protein, FEBS Lett 403, 168-72.
3. Ausma, J., Wijffels, M., van Eys, G., Koide, M., Ramaekers, F., Allessie, M., and Borgers, M. (1997). Dedifferentiation of atrial cardiomyocytes as a result of chronic atrial fibrillation, Am J Pathol 151, 985-97.
4. Dispersyn, G. D., Geuens, E., Ver Donck, L., Ramaekers, F. C., and Borgers, M. (2001). Adult rabbit cardiomyocytes undergo hibernation-like dedifferentiation when cocultured with cardiac fibroblasts, Cardiovasc Res 51, 230-40.
5. Ausma, J., Litjens, N., Lenders, M-H., Duimel, H., Mast, F., Wouters, L., Ramaekers, F., Allessie, M., and Borgers, M. (2001). Time course of atrial fibrillation-induced cellular structural remodeling in atria of the goat, J Mol
Cell Cardiol 33, 2083-94.
6. Dispersyn, G. D., Mesotten, L., Meuris, B., Maes, A., Mortelmans, L., Flameng, W., Ramaekers, F. C., and Borgers, M. (2002). Dissociation of cardiomyocyte apoptosis and dedifferentiation in infarct border zones, Eur
Heart J in press.