Human Predicted to work with:
Synthetic phosphopeptide derived from the Human Caldesmon protein (Q05682) around the phosphorylation site of serine 759 (N-K-SP-P-A).
Human lung carcinoma tissue.
Shipped at 4°C. Store at -20°C. Stable for 12 months at -20°C.
pH: 7.40 Preservative: 0.02% Sodium azide Constituents: PBS, 50% Glycerol, 0.88% Sodium chloride Note: PBS without calcium and magnesium
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Immunogen affinity purified
Affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific phosphopeptide. The antibody against non-phosphopeptide was removed by chromatography using non-phosphopeptide corresponding to the phosphorylation site.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
1/50 - 1/100. Perform heat mediated antigen retrieval via the pressure cooker method before commencing with IHC staining protocol. Antigen retrieval is heat-mediated with a pressure cooker for about 5 minutes in citrate buffer pH 6.0.
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.
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.
Belongs to the caldesmon family.
The N-terminal part seems to be a myosin/calmodulin-binding domain, and the C-terminal a tropomyosin/actin/calmodulin-binding domain. These two domains are separated by a central helical region in the smooth-muscle form.
In non-muscle cells, phosphorylation by CDK1 during mitosis causes caldesmon to dissociate from microfilaments. Phosphorylation reduces caldesmon binding to actin, myosin, and calmodulin as well as its inhibition of actomyosin ATPase activity. Phosphorylation also occurs in both quiescent and dividing smooth muscle cells with similar effects on the interaction with actin and calmodulin and on microfilaments reorganization.
Cytoplasm > cytoskeleton. Cytoplasm > myofibril. On thin filaments in smooth muscle and on stress fibers in fibroblasts (nonmuscle).
Immunohistochemistry analysis of paraffin-embedded human lung carcinoma tissue, using Caldesmon (Phospho-Ser759) antibody (ab111579). Without blocking peptide on left and with blocking peptide on the right.