M13 Major Coat Protein Antibody (RL-ph2): sc-53005

M13 Major Coat Protein Antibody (RL-ph2) is a mouse monoclonal IgG2a kappa light chain antibody that detects M13 protein of M13 species reactivity by western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), and flow cytometry (FCM). Anti-M13 Major Coat Protein antibody (RL-ph2) plays a crucial role in understanding the morphogenesis of filamentous phage, particularly in the synthesis and assembly of the major coat protein, which is essential for the formation of infectious virions. M13 protein is primarily located in the host cell′s plasma membrane, where M13 binds to the E. coli cytoplasmic membrane, exposing its antigenic site to the exterior. This interaction is vital for the phage′s ability to infect bacterial cells, as M13 Major Coat Protein facilitates the entry of viral DNA into the host. M13 protein undergoes a series of modifications, including the initial synthesis of a 23 amino acid amino-terminal "leader peptide" known as "procoat," which is crucial for its maturation and subsequent assembly into the lipid-free virion. Understanding the structure and function of M13 Major Coat Protein not only sheds light on the viral life cycle but also provides insights into potential applications in biotechnology and phage therapy, where the ability to manipulate phage assembly can lead to innovative solutions in combating bacterial infections.

Alexa Fluor^® is a trademark of Molecular Probes Inc., OR., USA

LI-COR^® and Odyssey^® are registered trademarks of LI-COR Biosciences

M13 Major Coat Protein Antibody (RL-ph2) References:

1. Role of aromatic residues at the lipid-water interface in micelle-bound bacteriophage M13 major coat protein.  |  Yuen, CT., et al. 2000. Biochemistry. 39: 16155-62. PMID: 11123944
2. Membrane-anchoring interactions of M13 major coat protein.  |  Meijer, AB., et al. 2001. Biochemistry. 40: 8815-20. PMID: 11467942
3. Dependence of M13 major coat protein oligomerization and lateral segregation on bilayer composition.  |  Fernandes, F., et al. 2003. Biophys J. 85: 2430-41. PMID: 14507706
4. Comprehensive mutational analysis of the M13 major coat protein: improved scaffolds for C-terminal phage display.  |  Held, HA. and Sidhu, SS. 2004. J Mol Biol. 340: 587-97. PMID: 15210356
5. Quantification of Protein-Lipid Selectivity using FRET: Application to the M13 Major Coat Protein.  |  Fernandes, F., et al. 2004. Biophys J. 87: 344-52. PMID: 15240469
6. Lipid bilayer topology of the transmembrane alpha-helix of M13 Major coat protein and bilayer polarity profile by site-directed fluorescence spectroscopy.  |  Koehorst, RB., et al. 2004. Biophys J. 87: 1445-55. PMID: 15345527
7. Anchoring mechanisms of membrane-associated M13 major coat protein.  |  Stopar, D., et al. 2006. Chem Phys Lipids. 141: 83-93. PMID: 16620800
8. FRET study of membrane proteins: determination of the tilt and orientation of the N-terminal domain of M13 major coat protein.  |  Nazarov, PV., et al. 2007. Biophys J. 92: 1296-305. PMID: 17114224
9. Reconstitution of the M13 major coat protein and its transmembrane peptide segment on a DNA template.  |  Li, W., et al. 2007. Biochemistry. 46: 8579-91. PMID: 17595059
10. Accessibility and dynamics of Cys residues in Bacteriophage IKe and M13 major coat protein mutants.  |  Khan, AR., et al. 1995. Biochemistry. 34: 12388-97. PMID: 7547983

The preferred M13 Major Coat Protein antibody is M13 Major Coat Protein Antibody (RL-ph1): sc-53004.