Cell Signaling Technology

Product Pathways - Cytoskeletal Signaling

Tropomyosin-1/3 (D17B8) Rabbit mAb #3913

Applications Reactivity Sensitivity MW (kDa) Isotype
W H M R Endogenous 32 , 35, 36, 41 Rabbit IgG

Applications Key:  W=Western Blotting
Reactivity Key:  H=Human  M=Mouse  R=Rat
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

Tropomyosin-1/3 (D17B8) Rabbit mAb detects endogenous levels of total tropomyosin-1 and/or tropomyosin-3 protein.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Leu274 of human tropomyosin-1 protein.

Western blot analysis of extracts from human, mouse and rat heart tissue and C2C12 cells using Tropomyosin-1/3 (D17B8) Rabbit mAb.

Background

Tropomyosin-1 (TPM1) belongs to the high molecular weight members of tropomyosin family (1,2). The protein exists in an alpha-helical coiled-coil conformation and binds multiple acting monomers in a tight manner to stabilize and regulate the actin filament (3). Tropomyosins fullfill functions in muscle and non-muscle cells. In muscle cells, tropomyosins associate with the troponin complex and play a central role in the calcium-dependent regulation of striated muscle contraction in vertebrates. In non-muscle cells, tropomyosins are implicated in the formation and stabilization of cytoskeletal actin filaments to ensure normal cellular processes (1,2). Mutations of tropomysin-1 have been reported as a cause of dilated cardiac myopathies (4). Tropomyosin-1 also functions as a tumor suppressor, and many malignant tumors demonstrate downregulation of tropomyosin-1 expression (5-8). Tropomyosin-1 is phosphorylated at Ser283 through the Erk/DAPK pathway, which promotes stress fiber formation in response to oxidative stress (9-10).

  1. Perry, S.V. (2001) J Muscle Res Cell Motil 22, 5-49.
  2. Lin, J.J. et al. (2008) Adv Exp Med Biol 644, 201-22.
  3. Brown, J.H. et al. (2001) Proc Natl Acad Sci USA 98, 8496-501.
  4. Rajan, S. et al. (2007) Circ Res 101, 205-14.
  5. Bharadwaj, S. et al. (2004) J Biol Chem 279, 14039-48.
  6. Mahadev, K. et al. (2002) Exp Cell Res 279, 40-51.
  7. Varga, A.E. et al. (2005) Oncogene 24, 5043-52.
  8. Raval, G.N. et al. (2003) Oncogene 22, 6194-203.
  9. Houle, F. et al. (2003) Mol Biol Cell 14, 1418-32.
  10. Houle, F. et al. (2007) J Cell Sci 120, 3666-77.

Application References

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For Research Use Only. Not For Use In Diagnostic Procedures.

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