Anti-Foldon domain of Fibritin Antibody, clone MF4

Fibritin (UniProt: P10104; also known as Collar protein, Whisker antigen control protein) is encoded by the wac gene (Gene ID: 1258630) in Enterobacteria phage T4 (Bacteriophage T4). The primary function of fibritin is to provide structural support to the bacteriophage. It acts as a chaperone helping to attach the long tail fibers to the virus during the assembly process. During phage assembly, twelve fibritin molecules attach to the phage neck via gp13: six molecules forming the collar and six molecules forming the whiskers. Fibritin may also have a role in mediating the release of the phage from the host after replication. Fibritin is usually expressed during the late stages of the bacteriophage life cycle, coinciding with the assembly of new viral particles. Fibritin is primarily localized within the viral particle itself. It is incorporated into the capsid during the assembly process and is not typically found free in the host cell cytoplasm. The central domain of fibritin consists of 13 alpha-helical domains (19-40 residues long) with coiled-coil structural patterns. The foldon domain constitutes the C-terminal 30 amino acid residues (aa 458-484) of the trimeric protein fibritin from bacteriophage T4. Its function is to promote folding and trimerization of fibritin. While bacteriophages like 4T are primarily studied for their potential therapeutic applications in treating bacterial infections, Fibritin itself is not directly associated with disease. However, the bacteriophages that express Fibritin can contribute to the lysis of pathogenic bacteria, thereby indirectly influencing disease dynamics by controlling bacterial populations.(Ref.: Battles, M.B., et al. (2017). Nat Commun. 8(1):1528; Trento, A., et al. (2017). Front Microbiol. 8:2301; Wrapp, D., et al. (2020). Cell. 181(6):1436-1441).

His-tagged Foldon domain (aa 458-484) of Fibritin from Tequatrovirus T4.

Quality Control Testing

Evaluated by Western Blotting using recombinant respiratory syncytial virus F protein (RSV-F).

Western Blotting Analysis: A 1:500 dilution of this antibody detected the Foldon domain of Fibritin using recombinant respiratory syncytial virus F protein (RSV-F).

Tested Applications

ELISA Analysis: A representative lot detected Foldon domain of Fibritin in ELISA application (Battles, M.B., et al. (2017). Nat Commun. 8(1):1528; Trento, A., et al. (2017). Front Microbiol. 8:2301; Wrapp, D., et al. (2020). Cell. 181(6):1436-1441).

Note: Actual optimal working dilutions must be determined by end user as specimens, and experimental conditions may vary with the end user.

Clone MF4 is a mouse recombinant monoclonal antibody that detects the Foldon domain of Fibritin. It targets an epitope within 27 amino acids from the C-terminal.

Purified mouse monoclonal antibody IgG2a in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

0.5 mg/mL. Please refer to guidance on suggested starting dilutions and/or titers per application and sample type.

Recommended storage: +2°C to +8°C.

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

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