·High lot-to-lot consistency
·Increased sensitivity and higher affinity
·Animal-free production
Description:
Anti-M13 Bacteriophage, AlpSdAbs® VHH is designed for detecting M13 bacteriophage specifically. Anti-M13 Bacteriophage, AlpSdAbs® VHH is based on monoclonal, recombinant, single domain antibody derived from the variable regions of heavy chain of Alpaca pacous. Based on ELISA, Anti-M13 Bacteriophage, AlpSdAbs® VHH reacts with the M13 bacteriophage selectively, no reactivity with other proteins.
Immunogen: Full length M13 phage coat protein
Host: Alpaca pacous
Isotype: VHH domain of alpaca IgG2b/2c
Conjugate: Unconjugated(6*his tag and one cys were added at the C terminal of the VHH)
Specificity: M13 phage coat protein, exact epitope not determined
Cross-Reactivity: Highly selective for M13 phage
Purity: Recombinant Expression and Affinity purified
Concentration: 1mg/ml
Formation: Liquid, 10mM PBS (pH 7.5), 0.05% sucrose, 0.1% trehalose, 0.01% proclin300
Storage: Store at –20 °C, (Avoid freeze / thaw cycles)
Background:
M13 is a fi¬lamentous bacteriophage composed of circular single stranded DNA (ssDNA) which is 6470 nucleotides long encapsulated in approximately 2700 copies of the major coat protein P8, and capped with 5 copies of two different minor coat proteins (P9, P6, P3) on the ends. Infection with fi¬lamentous phages is not lethal, however the infection causes turbid plaques in E. coli. It is a non-lytic virus. However a decrease in the rate of cell growth is seen in the infected cells. M13 plasmids are used for many recombinant DNA processes, and the virus has also been studied for its uses in nanostructures and nanotechnology.
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.
VHH are single-domain antibodies derived from the variable regions of heavy chain of Camelidae immunoglobulin. The size of VHH is extremely small(<15KDa) compared to other forms of antibody fragment, which significantly increase the permeability of VHH. Thus VHH is considered of great value for research, diagnostics and therapeutics.
ELISA: 1:10,000-1:50,000
Dilution factors are presented in the form of a range because the optimal dilution is a function of many factors, such as antigen density, permeability, etc. The actual dilution used must be determined empirically.
