The epitope recognized by alpha-SM1 is highly conserved. The antibody therefore cross-reacts with many species including protochordates, lower craniates and mammals (amongst others human, rat, chicken, goat, rabbit, mouse).
Aufreinigung
Purified
Immunogen
alpha-SM1 (clone 1A4) is a mouse monoclonal IgG2a antibody derived by fusion of Sp 2/0 mouse myeloma cells with spleen cells from a BALB/c mouse immunized with a peptide comprising the first 10 amino acids of alpha-smooth muscle actin with an acetylated N-terminus coupled to keyhole limpet hemocyanin via the C-terminal cysteine (Ac-EEEDSTALVC).
alpha-SM1 reacts exclusively with alpha-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 alpha-SM1 is Ac-EEED. alpha-SM1 is useful for immunocytochemistry, immunohistochemistry on frozen and paraffin-embedded tissues, immunoblotting, immuno- electron microscopy and ELISA. Optimal antibody dilution should be determined by titration, recommended range is 1:1000 - 1:10.000 for immunohistochemistry with avidin-biotinylated horseradish peroxidase complex (ABC) as detection reagent, and 1:10.000 - 1:50.000 for immunoblotting applications.
Beschränkungen
Nur für Forschungszwecke einsetzbar
Lagerung
4 °C
De Visscher, Plusquin, Mesure, Flameng: "Selection of an immunohistochemical panel for cardiovascular research in sheep." in: Applied immunohistochemistry & molecular morphology : AIMM / official publication of the Society for Applied Immunohistochemistry, Vol. 18, Issue 4, pp. 382-91, (2010) (PubMed).
Clément, Stouffs, Bettiol, Kampf, Krause, Chaponnier, Jaconi: "Expression and function of alpha-smooth muscle actin during embryonic-stem-cell-derived cardiomyocyte differentiation." in: Journal of cell science, Vol. 120, Issue Pt 2, pp. 229-38, (2007) (PubMed).
Clment, Hinz, Dugina, Gabbiani, Chaponnier: "The N-terminal Ac-EEED sequence plays a role in alpha-smooth-muscle actin incorporation into stress fibers." in: Journal of cell science, Vol. 118, Issue Pt 7, pp. 1395-404, (2005) (PubMed).
Chaponnier, Gabbiani: "Pathological situations characterized by altered actin isoform expression." in: The Journal of pathology, Vol. 204, Issue 4, pp. 386-95, (2004) (PubMed).
Hinz, Dugina, Ballestrem, Wehrle-Haller, Chaponnier: "Alpha-smooth muscle actin is crucial for focal adhesion maturation in myofibroblasts." in: Molecular biology of the cell, Vol. 14, Issue 6, pp. 2508-19, (2003) (PubMed).
Hinz, Gabbiani, Chaponnier: "The NH2-terminal peptide of alpha-smooth muscle actin inhibits force generation by the myofibroblast in vitro and in vivo." in: The Journal of cell biology, Vol. 157, Issue 4, pp. 657-63, (2002) (PubMed).
Hinz, Celetta, Tomasek, Gabbiani, Chaponnier: "Alpha-smooth muscle actin expression upregulates fibroblast contractile activity." in: Molecular biology of the cell, Vol. 12, Issue 9, pp. 2730-41, (2001) (PubMed).
Simoncelli, Fagotti, Di Rosa, Panara, Chaponnier, Gabbiani, Pascolini: "Expression of an actin in protochordates and lower craniates defined by anti-alpha SM-1." in: European journal of cell biology, Vol. 69, Issue 3, pp. 297-300, (1996) (PubMed).
Chaponnier, Goethals, Janmey, Gabbiani, Gabbiani, Vandekerckhove: "The specific NH2-terminal sequence Ac-EEED of alpha-smooth muscle actin plays a role in polymerization in vitro and in vivo." in: The Journal of cell biology, Vol. 130, Issue 4, pp. 887-95, (1995) (PubMed).
Vyalov, Gabbiani, Kapanci: "Rat alveolar myofibroblasts acquire alpha-smooth muscle actin expression during bleomycin-induced pulmonary fibrosis." in: The American journal of pathology, Vol. 143, Issue 6, pp. 1754-65, (1994) (PubMed).
Sappino, Schürch, Gabbiani: "Differentiation repertoire of fibroblastic cells: expression of cytoskeletal proteins as marker of phenotypic modulations." in: Laboratory investigation; a journal of technical methods and pathology, Vol. 63, Issue 2, pp. 144-61, (1990) (PubMed).
Babaev, Bobryshev, Stenina, Tararak, Gabbiani: "Heterogeneity of smooth muscle cells in atheromatous plaque of human aorta." in: The American journal of pathology, Vol. 136, Issue 5, pp. 1031-42, (1990) (PubMed).
Skalli, Schürch, Seemayer, Lagacé, Montandon, Pittet, Gabbiani: "Myofibroblasts from diverse pathologic settings are heterogeneous in their content of actin isoforms and intermediate filament proteins." in: Laboratory investigation; a journal of technical methods and pathology, Vol. 60, Issue 2, pp. 275-85, (1989) (PubMed).
Skalli, Ropraz, Trzeciak, Benzonana, Gillessen, Gabbiani: "A monoclonal antibody against alpha-smooth muscle actin: a new probe for smooth muscle differentiation." in: The Journal of cell biology, Vol. 103, Issue 6 Pt 2, pp. 2787-96, (1987) (PubMed).
Among the six actin isoforms described in mammals, two are found in virtually all cells (betaˆ’ and gammaˆ’cytoplasmic), two are detected in smooth muscle cells (alphaˆ’ and gamma-smooth muscle) and two are present in striated muscles, one predominantly in skeletal (alpha-skeletal) and one in cardiac (alpha-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.