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Caldesmon Antibody Phospho (pS759)

Rabbit Monoclonal Antibody

  • WB - Caldesmon Antibody Phospho (pS759) AJ1117c
    A. Western blot analysis on HeLa lysates using anti-Phospho-Caldesmon (pS759) RabMAb (Cat. #AJ1117c), 1:3000 dilution. Cells were either (A) untreated (B) treated with Calyculin A
Product Information
  • Applications Legend:
  • WB=Western Blot
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin-embedded Sections)
  • IHC-F=Immunohistochemistry (Frozen Sections)
  • IF=Immunofluorescence
  • FC=Flow Cytopmetry
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • IP=Immunoprecipitation
  • DB=Dot Blot
  • CHIP=Chromatin Immunoprecipitation
  • FA=Fluorescence Assay
  • IEM=Immunoelectronmicroscopy
  • EIA=Enzyme Immunoassay
Primary Accession Q05682
Reactivity Human
Host Rabbit
Clonality Monoclonal
Clone Names EPR2212
Calculated MW 93231 Da
Gene ID 800
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.
Dilution WB~~1:1500~3000
Format 50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.
StorageMaintain 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.
PrecautionsCaldesmon Antibody Phospho (pS759) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name CALD1
Synonyms CAD, CDM
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 {ECO:0000250|UniProtKB:P13505}. Cytoplasm, myofibril {ECO:0000250|UniProtKB:P13505}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:P13505}. Note=On thin filaments in smooth muscle and on stress fibers in fibroblasts (nonmuscle) {ECO:0000250|UniProtKB:P13505}
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
Research Areas
Citations (0)

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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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Cat# AJ1117c
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