Exalpha Biologicals, Inc.

Accelerating the Pace of Discovery
Exalpha Biologicals, Inc.

Actin (alpha Smooth Muscle)

  • Product Code: X1722M
  • Size: 50 µg
  • Price (USD): $314

Cat #

X1722M		 Quantity:      

Data Sheet

Product Name

Actin (alpha Smooth Muscle)

Host/Source

Mouse

Clone

a-SM1

Isotype

IgG2a

Product Type

Monoclonal Antibody

Reactivity

Human, Rat, Chicken

Applications

Western Blot, Immunohistochemistry, Immuno Electron Microscopy, ELISA

Purification

Protein A/G Chromatography

Size

50 µg

Price (USD)

$314

Background

Among the six actin isoforms described in mammals, two are found in virtually all cells (?? and ??cytoplasmic), two are detected in smooth muscle cells (?? and ?-smooth muscle) and two are present in striated muscles, one predominantly in skeletal (?-skeletal) and one in cardiac (?-cardiac) muscle cells. These actin isoforms differ slightly in their N-terminus and the sequences of each of them are perfectly conserved in higher vertebrates. Alpha-smooth muscle actin is abundant in vascular and visceral smooth muscle cells. In addition, it has also been shown to appear in stress fibers of fibroblastic cells during pathological situations involving contractile phenomena such as wound healing and fibrocontractive diseases.

Immunogen

Hybridoma produced by the fusion of splenocytes from BALB/c mice immunized with a peptide derived from the N-terminus of ?-smooth muscle actin and Sp 2/0 mouse myeloma cells. The epitope that is recognized by a-SM1 is Ac-EEED..

Formulation

Provided as solution in phosphate buffered saline with 0.08% sodium azide

Customer Storage

Product should be stored at -20ºC. Aliquot to avoid freeze/thaw cycles

Database Links:

SwissProtP08023Chicken
SwissProtP62738Rat
SwissProtP62736Human

References

1. Skalli, O., et al. 'A monoclonal antibody against alpha-smooth muscle actin: a new probe for smooth muscle differentiation. J Cell Biol 1986, 103, 2787-2796. 2. Skalli, O., et al. 'Myofibroblasts from diverse pathologic settings are heterogeneous in their content of actin isoforms and intermediate filament proteins.' Lab Invest 1989, 60, 275-285. 3. Sappino, A. P., et al. 'Differentiation repertoire of fibroblastic cells: expression of cytoskeletal proteins as marker of phenotypic modulations.' Lab Invest 1990, 63, 144-161. 4. Vyalov, S. L., et al. Rat alveolar myofibroblasts acquire alpha-smooth muscle actin expression during bleomycin-induced pulmonary fibrosis. Am J Pathol 1993 143, 1754-1765. 5. Chaponnier, C., et al. The specific NH2-terminal sequence Ac-EEED of alpha-smooth muscle actin plays a role in polymerization in vitro and in vivo. J Cell Biol 1995, 130, 887-895. 6. Hinz, B., et al. Alpha-smooth muscle actin expression upregulates fibroblast contractile activity. Mol Biol Cell 2001, 12, 2730-2741. 7. Hinz, B., et al. 'The NH2-terminal peptide of alphasmooth muscle actin inhibits force generation by the myofibroblast in vitro and in vivo.' J Cell Biol 2002, 157, 657-663. 8. Babaev, V.R., Bobryshev, Y.V., Stenina, O.V., Tararak, E.M. and Gabani, G. (1990). Heterogeneity of smooth muscle in atheromatous plaque of human aorta. American Journal of Pathlogy 136, 1031-42. 9. Simoncelli, F., Fagotti, A., Di Rosa, I., Panara, F., Chaponnier, C., Gabbiani, G., Pascolini, R., (1996). Expression of an actin in protochordates and lower craniates defined by anti-?SM-1. European J of Cell Biol 69, 297-300. 10. Cle?ment, S., Hinz, B., Dugina, V., Gabbiani, G. and Chaponnier, C. (2004). The N-terminal Ac- EEED sequence plays a role in alpha-smooth- muscle actin incorporation into stress fibers. Journal of Cell Science 118, 1395-1404. 11. Chaponnier, C. and Gabbiani, G. (2004). Pathological situation characterized by altered actin isoform expression. J Pathol 204, 386-95. 12. Cle?ment, S., Stouffs, M., Bettiol, E., Kampf, S., Krause, K., Chaponnier, C. and Jaconi, M. (2006). Expression and function of alpha- smooth muscle actin during embryonic-stem- cell-derived cardiomyocyte differentiation. Journal of Cell Science 120, 229-38. 13. De Visscher, G., Plusquin, R., Mesure, L., Flameng, W. (2010). Selection of an immunohistochemical panel for cardiovascular research in sheep. Appl Immunohistochem Mol Morphol 18, 382-91.