M13 Major Coat Protein Antibody (RL-ph1): sc-53004

M13 Major Coat Protein Antibody (RL-ph1) is a mouse monoclonal IgG2b kappa light chain antibody that detects M13 Major Coat Protein of M13 origin by western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), and flow cytometry (FCM). M13 Major Coat Protein (RL-ph1) antibody is available in both non-conjugated and various conjugated forms, including agarose, horseradish peroxidase (HRP), phycoerythrin (PE), fluorescein isothiocyanate (FITC), and multiple Alexa Fluor® conjugates. M13 Major Coat Protein plays a crucial role in filamentous phage morphogenesis, as this protein is essential for virion assembly. M13 Major Coat Protein is synthesized in a precursor form and undergoes modifications, including insertion into the host cell plasma membrane and subsequent cleavage to mature form. The mature coat protein then assembles into the viral structure, with approximately 2400 copies incorporated as viral DNA crosses the cytoplasmic membrane. The amino-terminus of M13 Major Coat Protein contains an antigenic site exposed to the E. coli cell exterior, facilitating interaction necessary for phage infection. Initial synthesis includes a 23 amino acid amino-terminal "leader peptide," known as "procoat," which serves as a biosynthetic precursor in vivo. Understanding M13 Major Coat Protein structure and function is vital for elucidating phage assembly and infection mechanisms, making anti-M13 Major Coat Protein antibody (RL-ph1) an invaluable tool for researchers studying bacteriophage biology and applications in molecular biology and biotechnology.

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M13 Major Coat Protein Antibody (RL-ph1) References:

1. Protein-lipid interactions of bacteriophage M13 major coat protein.  |  Stopar, D., et al. 2003. Biochim Biophys Acta. 1611: 5-15. PMID: 12659940
2. Membrane-associated assembly of M13 phage in extracts of virus-infected Escherichia coli.  |  Wickner, W. and Killick, T. 1977. Proc Natl Acad Sci U S A. 74: 505-9. PMID: 15248
3. Membrane assembly of M13 major coat protein: evidence for a structural adaptation in the hinge region and a tilted transmembrane domain.  |  Spruijt, RB., et al. 2004. Biochemistry. 43: 13972-80. PMID: 15518546
4. Membrane-bound conformation of M13 major coat protein: a structure validation through FRET-derived constraints.  |  Vos, WL., et al. 2005. J Biol Chem. 280: 38522-7. PMID: 16150733
5. Structure of membrane-embedded M13 major coat protein is insensitive to hydrophobic stress.  |  Vos, WL., et al. 2007. Biophys J. 93: 3541-7. PMID: 17704180
6. Soluble precursor of an integral membrane protein: synthesis of procoat protein in Escherichia coli infected with bacteriophage M13.  |  Ito, K., et al. 1979. Proc Natl Acad Sci U S A. 76: 1199-203. PMID: 375229
7. A mutation downstream from the signal peptidase cleavage site affects cleavage but not membrane insertion of phage coat protein.  |  Russel, M. and Model, P. 1981. Proc Natl Acad Sci U S A. 78: 1717-21. PMID: 7015343
8. 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
9. Asymmetric orientation of phage M13 coat protein in Escherichia coli cytoplasmic membranes and in synthetic lipid vesicles.  |  Wickner, W. 1976. Proc Natl Acad Sci U S A. 73: 1159-63. PMID: 772680
10. Local dynamics of the M13 major coat protein in different membrane-mimicking systems.  |  Stopar, D., et al. 1996. Biochemistry. 35: 15467-73. PMID: 8952500
11. Solution structure of the M13 major coat protein in detergent micelles: a basis for a model of phage assembly involving specific residues.  |  Papavoine, CH., et al. 1998. J Mol Biol. 282: 401-19. PMID: 9735296
12. Phage displayed antibodies specific for a cytoskeletal antigen. Selection by competitive elution with a monoclonal antibody.  |  Meulemans, EV., et al. 1995. Hum Antibodies Hybridomas. 6: 113-8. PMID: 8597626

Monoclonal antibodies for mammalian and non-mammalian protein targets represent essentially all targets covered by polyclonal antibodies. Over 8,300 of our antibodies are offered as ImmunoCruz^® conjugates which eliminates the need for a secondary antibody.

Santa Cruz Biotechnology antibodies have over 360,000 research citations. Anti-M13 Major Coat Protein Antibody (RL-ph1) has 15 citations in a variety of scientific publications.

Primary antibodies for mammalian target proteins are recommended for the detection of a range of mammalian species, primarily of mouse, rat and human species. Many mammalian antibodies are also ideal for veterinary research and reactive with ovine, porcine, caprine, feline, canine, bovine and equine protein targets. Santa Cruz Biotechnology primary monoclonal antibodies are suitable for laboratory research applications and are not intended for diagnostic or therapeutic use.

M13 Major Coat Protein Antibody (RL-ph1) Specifications

Alternate Product Name: M13 Major Coat Protein

Product Clone Name: RL-ph1

Classification: Primary Antibody

Clonality: Monoclonal Antibody

Antibody Isotype: IgG_2b kappa light chain

Amino Acids:

Epitope Target: M13 Major Coat Protein

Epitope Species: viral

Product Reactivity/Detection: M13 filamentous phage coat protein g8p

Species Reactivity/Detection: M13

Additional Mammalian Reactivity: N/A

Additional Non-Mammalian Reactivity: N/A

Applications: WB, IP, IF, FCM

Vialing Information: Each vial contains 200 µg IgG_2b kappa light chain in 1.0 ml of PBS with < 0.1% sodium azide and 0.1% gelatin

Research Citations: 15 citations in various scientific publications

Available Conjugates/Forms for M13 Major Coat Protein Antibody (RL-ph1): AC: Agarose, AF488: Alexa Fluor^® 488, AF546: Alexa Fluor^® 546, AF594: Alexa Fluor^® 594, AF647: Alexa Fluor^® 647, AF680: Alexa Fluor^® 680, AF790: Alexa Fluor^® 790, FITC: Fluoroscein, HRP: Horseradish Peroxidase, PE: Phycoerythrin