Cell Signaling Technology

Product Pathways - Cytoskeletal Signaling

Caldesmon-1 Antibody #2980

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

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.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell types using Caldesmon-1 Antibody.

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).

  1. Hayashi, K. et al. (1992) Proc. Natl. Acad. Sci. USA 89, 12122-12126.
  2. Humphrey, M.B. et al. (1992) Gene 112, 197-204.
  3. Yamashiro, S. et al. (1991) Nature 349, 169-172.
  4. Mak, A.S. et al. (1991) J. Biol. Chem. 266, 6678-6681.
  5. Hai, C.M. and Gu, Z. (2006) Eur. J. Cell Biol. 85, 305-309.
  6. Yamashiro, S. et al. (2001) Mol. Biol. Cell 12, 239-250.
  7. 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.

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