Coat Protein g8p Antikörper

Produktnummer ABIN335343

Produktdetails

Target: Coat Protein g8p

Reaktivität: Bacteriophage M13

Wirt: Maus

Klonalität: Monoklonal

Konjugat: Unkonjugiert

Applikation: ELISA, Western Blotting (WB), Affinity Chromatography (AC), Immunocytochemistry (ICC), Flow Cytometry (FACS), Immunohistochemistry (IHC)

Aufreinigung: Purified

Immunogen: RL-ph2 is a mouse monoclonal IgG2a, kappa antibody derived by fusion of SP2/0-Ag14 mouse myeloma cells with spleen cells from a BALB/c mouse immunized with isolated M13 phage coat proteins.

Klon: RL-ph2

Isotyp: IgG2a

Anwendungsinformationen

Applikationshinweise: RL-ph2 reacts with the major M13 filamentous phage coat protein g8p with a molecular weight of 5 kDa. RL-ph2 is particularly useful for immunoblotting of separated phage proteins, and is also suitable for detection of M13 phages in multistep immunoblotting procedures, immunocytochemistry, flow cytometry, affinity chromatography and ELISA. Optimal antibody dilution should be determined by titration, recommended range is 1:25 - 1:200 for flow cytometry, and for immunohistochemistry with avidin-biotinylated horseradish peroxidase complex (ABC) as detection reagent, and 1:100 - 1:1000 for immunoblotting applications.

Beschränkungen: Nur für Forschungszwecke einsetzbar

Handhabung

Lagerung: 4 °C

Referenzen

Meulemans, Nieland, Debie, Ramaekers, van Eys: "Phage displayed antibodies specific for a cytoskeletal antigen. Selection by competitive elution with a monoclonal antibody." in: Human antibodies and hybridomas, Vol. 6, Issue 3, pp. 113-8, (1996) (PubMed).

Meulemans, Slobbe, Wasterval, Ramaekers, van Eys: "Selection of phage-displayed antibodies specific for a cytoskeletal antigen by competitive elution with a monoclonal antibody." in: Journal of molecular biology, Vol. 244, Issue 4, pp. 353-60, (1995) (PubMed).

Antigendetails

Target: Coat Protein g8p

Substanzklasse: Phage Protein

Hintergrund: The display of repertoires of antibody fragments on the surface of filamentous phage offers a new way to produce immunoreagents with defined specificities. Phage derived antibody fragments offer a number of advantages over mouse monoclonal antibodies, such as better clearance from the blood, the possibility to select from human combinatorial libraries and the relative ease by which such fragments can be manipulated. The phage display technique thus facilitates the selection of antibody fragments of therapeutic value or research interest. Antibodies to M13 filamentous phage coat proteins are instrumental in the selection and detection of phages expressing specific antibody fragments or peptide sequences at their surface.