|Calculated MW||93231 Da|
|Other Names||Caldesmon, CDM, CALD1, CAD, CDM|
|Target/Specificity||A phospho-specific peptide corresponding to residues surrounding Serine 759 of human Caldesmon was used as an immunogen. The antibody only detects Caldesmon phosphorylated at Serine 759.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Caldesmon Antibody Phospho (pS759) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Actin- and myosin-binding protein implicated in the regulation of actomyosin interactions in smooth muscle and nonmuscle cells (could act as a bridge between myosin and actin filaments). Stimulates actin binding of tropomyosin which increases the stabilization of actin filament structure. In muscle tissues, inhibits the actomyosin ATPase by binding to F-actin. This inhibition is attenuated by calcium-calmodulin and is potentiated by tropomyosin. Interacts with actin, myosin, two molecules of tropomyosin and with calmodulin. Also play an essential role during cellular mitosis and receptor capping. Involved in Schwann cell migration during peripheral nerve regeneration (By similarity).|
|Cellular Location||Cytoplasm, cytoskeleton. Cytoplasm, myofibril. Note=On thin filaments in smooth muscle and on stress fibers in fibroblasts (nonmuscle)|
|Tissue Location||High-molecular-weight caldesmon (isoform 1) is predominantly expressed in smooth muscles, whereas low-molecular- weight caldesmon (isoforms 2, 3, 4 and 5) are widely distributed in non-muscle tissues and cells. Not expressed in skeletal muscle or heart|
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Caldesmon is a smooth muscle and nonmuscle regulatory protein that interacts with actin, myosin, tropomyosin, and calmodulin (1,2). Smooth muscle caldesmon is an elongated molecule with a calmodulin, tropomyosin, and actin-binding region at the C-terminus and a myosin-binding domain at the N-terminus (3). Caldesmon stimulates actin binding of tropomyosin which increases the stabilization of actin filament structure. In muscle tissues, caldesmon inhibits the actomyosin ATPase by binding to F-actin. This inhibition is reduced by calcium-calmodulin and is promoted by tropomyosin (4). Phosphorylation of caldesmon by extracellular signal-regulated kinase (ERK) and p38 mitogen-activated protein (MAP) kinases in smooth muscle are important for actin and tropomyosin binding, and actomyosin inhibitory activity. In intact vascular smooth muscle Caldesmon is phosphorylated by proline-directed protein kinases, members of the MAP kinase family, suggesting that caldesmon phosphorylation by MAP kinase may modulate smooth muscle contraction (5).
1. Humphrey, M.B., et al. Gene 112: 197-204 (1992).
2. Bryan, J., et al. J Biol Chem. 264: 13873-9 (1989).
3. Bryan, J., et al. Ann N Y Acad Sci. 599: 100-10 (1990).
4. Fraser, I.D., et al. Biochemistry 36: 5483-92 (1997).
5. Hedges J, et al. Am J Physiol Cell Physiol 278: C718-C726, 2000
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