Product Pathways - Cytoskeletal Signaling
Caldesmon-1 Antibody #2980
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PhosphoSitePlus® protein, site, and accession data: caldesmon
| Applications | Reactivity | Sensitivity | MW (kDa) | Source |
|---|---|---|---|---|
| W | H M R Mk | Endogenous | 70-80 non-muscle, 120-150 smooth muscle | Rabbit |
Applications Key:
W=Western Blotting
Reactivity Key:
H=Human
M=Mouse
R=Rat
Mk=Monkey
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
Protocols
- 2980:
- Western Blotting
Specificity / Sensitivity
Caldesmon-1 Antibody detects endogenous levels to total caldesmon-1 protein. Based on sequence homology, the antibody is expected to cross-react with both the smooth muscle and nonmuscle isoforms.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy terminus of human caldesmon-1. Antibodies are purified using peptide affinity chromatography.
Background
Caldesmon-1 is an actin filament stabilizing protein involved in the regulation of cell contraction. Binding of caldesmon-1 to actin is weakened by phosphorylation and by calmodulin in the presence of calcium. Caldesmon-1 is encoded by a single gene, which is spliced to generate a widely distributed low molecular weight form and a smooth muscle specific high molecular weight form (1,2). Caldesmon-1 is phosphorylated by the cyclin dependent kinase cdc2 and Erk1/2 MAP kinase, both of which prevent the activity of caldesmon-1 (3-5). Phosphorylation of caldesmon-1 by cdc2 is required for passage of cells through mitosis (6). Phosphorylation by Erk1/2 is important in regulating smooth muscle contraction (7). Caldesmon-1 activity may play a role in the formation of podosomes, adhesion complexes associated with the secretion of matrix metalloproteases, invasion, and metastasis (reviewed in 5).
- Hayashi, K. et al. (1992) Proc. Natl. Acad. Sci. USA 89, 12122-12126.
- Humphrey, M.B. et al. (1992) Gene 112, 197-204.
- Yamashiro, S. et al. (1991) Nature 349, 169-172.
- Mak, A.S. et al. (1991) J. Biol. Chem. 266, 6678-6681.
- Hai, C.M. and Gu, Z. (2006) Eur. J. Cell Biol. 85, 305-309.
- Yamashiro, S. et al. (2001) Mol. Biol. Cell 12, 239-250.
- Hedges, J.C. et al. (2000) Am. J. Physiol. Cell Physiol. 278, C718-C7126.
Application References
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For Research Use Only. Not For Use In Diagnostic Procedures.