TPM1, Antibody

CMH3; TMSA; CMD1Y; C15orf13; HTM-alpha

For Research Use Only. Not for use in diagnostic procedures.

IgG

Rabbit

Affinity purification

Store at-20 degree C or-80 degree C. Avoid freeze/thaw cycles.

Small volumes of anti-TPM1 antibody vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

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).

Autophagy antibody; Cancer; Cardiovascular; Cell Biology; Epigenetics & Nuclear Signaling; Developmental Biologys; Immunology; Drug Discovery Products; Metabolism; Neuroscience; Signal Transduction; Stem Cells

Western Blot (WB), Immunohistochemistry (IHC)

WB: 1:500-1:2000
IHC: 1:50-1:200

33kDa

tropomyosin 1

tropomyosin alpha-1 chain

Tropomyosin alpha-1 chain

C15orf13; TMSA  [Similar Products]

This gene is a member of the tropomyosin family of highly conserved, widely distributed actin-binding proteins involved in the contractile system of striated and smooth muscles and the cytoskeleton of non-muscle cells. Tropomyosin is composed of two alpha-helical chains arranged as a coiled-coil. It is polymerized end to end along the two grooves of actin filaments and provides stability to the filaments. The encoded protein is one type of alpha helical chain that forms the predominant tropomyosin of striated muscle, where it also functions in association with the troponin complex to regulate the calcium-dependent interaction of actin and myosin during muscle contraction. In smooth muscle and non-muscle cells, alternatively spliced transcript variants encoding a range of isoforms have been described. Mutations in this gene are associated with type 3 familial hypertrophic cardiomyopathy. [provided by RefSeq, Jul 2008]

Binds to actin filaments in muscle and non-muscle cells (PubMed:23170982). Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction (PubMed:23170982). Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments.

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.

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