Mouse anti actin alpha-smooth muscle
| Code | Size | Price |
|---|
| MUB0100P | 0.05 mg | £399.00 |
Quantity:
Prices exclude any Taxes / VAT
Overview
Host Type: Mouse
Antibody Isotype: IgG2a
Antibody Clonality: Monoclonal
Antibody Clone: 1A4
Regulatory Status: RUO
Target Species:
- Amphibian
- Avian
- Caprine (goat)
- Human
- Monkey
- Porcine (pig)
- Rat
- Sheep
Applications:
- Electron microscopy
- Immunocytochemistry (ICC)
- Immunohistochemistry (IHC)
- Western Blot (WB)
Storage:
Store at 4°C or in small aliquots at -20°C.
Documents
Further Information
Applications Description:
?-SM1 is useful for immunohistochemistry on frozen and paraffin-embedded tissues, immunoblotting, immuno-electron microscopy and ELISA. Optimal antibody dilution should be determined by titration; recommended range is 1:100 ? 1:250 for immunohistochemistry with avidin-biotinylated horseradish peroxidase complex (ABC) as detection reagent, and 1:100 ? 1:500 for immunoblotting applications.
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, but the sequence of each of these actins is highly 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.
Caution:
This product is intended FOR RESEARCH USE ONLY, and FOR TESTS IN VITRO, not for use in diagnostic or therapeutic procedures involving humans or animals.
This product contains sodium azide. To prevent formation of toxic vapors, do not mix with strong acidic solutions. To prevent formation of potentially explosive metallic azides in metal plumbing, always wash into drain with copious quantities of water.
This datasheet is as accurate as reasonably achievable, but Nordic-MUbio accepts no liability for any inaccuracies or omissions in this information.
This product contains sodium azide. To prevent formation of toxic vapors, do not mix with strong acidic solutions. To prevent formation of potentially explosive metallic azides in metal plumbing, always wash into drain with copious quantities of water.
This datasheet is as accurate as reasonably achievable, but Nordic-MUbio accepts no liability for any inaccuracies or omissions in this information.
Field of Interest:
Cytoskeleton|Stem cell research
Formulation:
Each vial contains 50 ul 1 mg/ml purified monoclonal antibody in PBS containing 0.09% sodium azide.
Product:
Each vial contains 50 ul 1 mg/ml purified monoclonal antibody in PBS containing 0.09% sodium azide.
Source:
?-SM1 (clone 1A4) is a Mouse monoclonal IgG2a antibody derived by fusion of Sp2/0 Mouse myeloma cells with spleen cells from a BALB/c Mouse immunized with a peptide comprising the first 10 amino acids of ?-smooth muscle actin with an acetylated N-terminus coupled to keyhole limpet hemocyanin via the C-terminal cysteine (Ac-EEEDSTALVC).
Species Reactivity:
The epitope recognized by ?-SM1 is highly conserved. The antibody therefore cross-reacts with many species including protochordates, lower craniates and mammals.
Specificity:
?-SM1 reacts exclusively with ?-smooth muscle actin which is typical for vascular and visceral smooth muscle cells, but which is also present in myofibroblasts. The epitope that is recognized by ?-SM1 is Ac-EEED.
UniProt:
P62736
References
1. Skalli, O., Ropraz, P., Trzeciak, A., Benzonana, G., Gillessen, D. and Gabbiani, G. (1986). A monoclonal antibody anti alpha-smooth muscle actin: a new probe for smooth muscle differentiation. J Cell Biol 103, 2787-96.
2. Skalli, O., Schurch, W., Seemayer, T., Lagace, R., Montandon, D., Pittet, B. and Gabbiani, G. (1989). Myofibroblasts from diverse pathologic settings are heterogeneous in their content of actin isoforms and intermediate filament proteins. Lab Invest 60, 275-85.
3. 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.
4. Sappino, A. P., Schurch, W. and Gabbiani, G. (1990). Differentiation repertoire of fibroblastic cells: expression of cytoskeletal proteins as marker of phenotypic modulations. Lab Invest 63, 144-61.
5. Vyalov, S. L., Gabbiani, G. and Kapanci, Y. (1993). Rat alveolar myofibroblasts acquire alpha-smooth muscle actin expression during bleomycin-induced pulmonary fibrosis. Am J Pathol 143, 1754-65.
6. Chaponnier, C., Goethals, M., Janmey, P. A., Gabbiani, F., Gabbiani, G. and Vandekerckhove, J. (1995). 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 130, 887-95.
7. Simoncelli, F., Fagotti, A., Di Rosa, I., Panara, F., Chaponnier, C., Gabbiani, G. and Pascolini, R., (1996). Expression of an actin in protochordates and lower craniates defined by anti-aSM-1. European J of Cell Biol 69, 297-300.
8. Hinz, B., Celetta, G., Tomasek, J. J., Gabbiani, G. and Chaponnier, C. (2001). Alpha-smooth muscle actin expression upregulates fibroblast contractile activity. Mol Biol Cell 12, 2730-41.
9. Hinz, B., Gabbiani, G. and Chaponnier, C. (2002). The NH2-terminal peptide of alpha-smooth muscle actin inhibits force geneRation by the myofibroblast in vitro and in vivo. J Cell Biol 157, 657-63.
10. Hinz, B., Dugina, V., Ballestrem, C., Wehrle-Haller, B. and Chaponnier, C. (2003). Alpha-smooth muscle actin is crucial for focal adhesion maturation in myofibroblasts. Mol Biol Cell 14, 2508-19.
11. Cl?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.
12. Chaponnier, C. and Gabbiani, G. (2004). Pathological situation characterized by altered actin isoform expression. J Pathol 204, 386-95.
13. Cl?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.
14. De Visscher, G., Plusquin, R., Mesure, L. and Flameng, W. (2010). Selection of an immunohistochemical panel for cardiovascular research in Sheep. Appl Immunohistochem Mol Morphol 18, 382-91.
2. Skalli, O., Schurch, W., Seemayer, T., Lagace, R., Montandon, D., Pittet, B. and Gabbiani, G. (1989). Myofibroblasts from diverse pathologic settings are heterogeneous in their content of actin isoforms and intermediate filament proteins. Lab Invest 60, 275-85.
3. 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.
4. Sappino, A. P., Schurch, W. and Gabbiani, G. (1990). Differentiation repertoire of fibroblastic cells: expression of cytoskeletal proteins as marker of phenotypic modulations. Lab Invest 63, 144-61.
5. Vyalov, S. L., Gabbiani, G. and Kapanci, Y. (1993). Rat alveolar myofibroblasts acquire alpha-smooth muscle actin expression during bleomycin-induced pulmonary fibrosis. Am J Pathol 143, 1754-65.
6. Chaponnier, C., Goethals, M., Janmey, P. A., Gabbiani, F., Gabbiani, G. and Vandekerckhove, J. (1995). 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 130, 887-95.
7. Simoncelli, F., Fagotti, A., Di Rosa, I., Panara, F., Chaponnier, C., Gabbiani, G. and Pascolini, R., (1996). Expression of an actin in protochordates and lower craniates defined by anti-aSM-1. European J of Cell Biol 69, 297-300.
8. Hinz, B., Celetta, G., Tomasek, J. J., Gabbiani, G. and Chaponnier, C. (2001). Alpha-smooth muscle actin expression upregulates fibroblast contractile activity. Mol Biol Cell 12, 2730-41.
9. Hinz, B., Gabbiani, G. and Chaponnier, C. (2002). The NH2-terminal peptide of alpha-smooth muscle actin inhibits force geneRation by the myofibroblast in vitro and in vivo. J Cell Biol 157, 657-63.
10. Hinz, B., Dugina, V., Ballestrem, C., Wehrle-Haller, B. and Chaponnier, C. (2003). Alpha-smooth muscle actin is crucial for focal adhesion maturation in myofibroblasts. Mol Biol Cell 14, 2508-19.
11. Cl?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.
12. Chaponnier, C. and Gabbiani, G. (2004). Pathological situation characterized by altered actin isoform expression. J Pathol 204, 386-95.
13. Cl?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.
14. De Visscher, G., Plusquin, R., Mesure, L. and Flameng, W. (2010). Selection of an immunohistochemical panel for cardiovascular research in Sheep. Appl Immunohistochem Mol Morphol 18, 382-91.