Exalpha Biologicals, Inc.

Accelerating the Pace of Discovery

Product Highlight

Mouse anti-M13 phage coat protein g8p

Antibodies recognising M13 filamentous phage coat proteins are instrumental in the selection and detection of phages expressing specific antibody fragments or peptide sequences at their surface. The monoclonal antibodies manufactured and supplied by Exalpha react with either the pIII (g3p) or pVIII (g8p) proteins of M13 filamentous bacteriophage. All antibodies are available in a purified format. The antibodies are fully validated and are suitable for a wide range of techniques including:

  • Flow Cytometry
  • Western Blot
  • Immunohistochemistry
  • Immunoprecipitation
For more information, click here for our M13 Bacteriophage information page.


Two more of our excellent products have been published by PubMed:

Potential actionable targets in appendiceal cancer detected by immunohistochemistry, fluorescent in situ hybridization, and mutational analysis
Borazanci, E., et al., J. Gastrointest. Oncol., 8, 164-172 (2017)
Using Exalpha SPARC Antibody (Cat. No. X1867P)

Molecular mechanism underlying the pharmacological interactions of the protein kinase C-β inhibitor enzastaurin and erlotinib in non-small cell lung cancer cells
Steen, N.V., et al., Am. J. Cancer Res., 7, 816-830 (2017)
Using Exalpha's FITC labeled anti PY20 Antibody (Cat. No. X1017)

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)







Product Type

Monoclonal Antibody


Human, Rat, Chicken


Western Blot, Immunohistochemistry, Immuno Electron Microscopy, ELISA


Protein A/G Chromatography


50 µg

Price (USD)



Among the six actin isoforms described in mammals, two are found in virtually all cells (β− and γ−cytoplasmic), two are detected in smooth muscle cells (α− and γ-smooth muscle) and two are present in striated muscles, one predominantly in skeletal (α-skeletal) and one in cardiac (α-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.


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


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

Customer Storage

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

Database Links:



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-αSM-1. European J of Cell Biol 69, 297-300.

10. Clément, 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. Clément, 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.