CloneID: 3F1A2
Antigen Long Description: The original antibody was generated by immunizing BALB/c mice with Egtved virus by intraperitoneal injections five times over two months, followed by an additional intravenous booster injection on week nine. The hybridoma cell line secreting clone 3F1A2 was selected from a subsequent fusion after three more months of continued immunization.
Origin Pub PMID: 10938729
Buffer Composition: PBS with 0.02% Proclin 300.
Available Custom Conjugation Options: AP, HRP, Fluorescein, APC, PE, Biotin Type A, Biotin Type B, Streptavidin, FluoroProbes 647H, Atto488, APC/Cy7, PE/Cy7
Uniprot Accession No.: P27662
Specificity Statement: This antibody is specific for the transmembrane envelope glycoprotein (G protein) of viral hemorrhagic septicemia virus (VHSV). The G protein is the only protein known to be present on the surface of the virus particle, and it constitutes less than 10% of the mass of the virus particle which is dominated by N, M1 and M2. This antibody demonstrated similar neutralizing activity to clone 3F1H10, and they were found to interfere with each other's binding reciprocally, which indicates they recognize the same or partially related epitopes.
Application Notes (Clone): The neutralizing activity of the original format of this antibody (mouse IgG1) against different VHSV isolates was determined by 50% PNT; it neutralized type I isolates VHSV (I-F1 and I-92) and type II isolate VHSV (II-31) well, but higher concentrations were needed to neutralize type III isolates (III-51 and III-37). ELISA was used to detect and quantify the antibody's binding efficiency to various VHSV strains. The antibody's binding kinetics were evaluated by surface plasmon resonance (SPR) analysis resulting in a KD of 2.4 nM for the immobilized G protein of VHSV strain I-F1 and a KD of 12.1 nM for the immobilized G protein of VHSV strain I-92 (Lorenzen et al., 2000; PMID: 10938729). The Fab and recombinant single-chain antibody fragments (scAbs) versions of this antibody neutralized VHSV, indicating that the Fc moiety and divalency of the antibody molecules are unnecessary for neutralization. However, the neutralizing activity of Fab and scAb fragments was generally lower compared to the parent antibody due to the higher avidity of the divalent parent molecules; the Fab and scAb fragments exhibited a 10-100-fold increase in kd compared to the parent MAb, while the kas were similar. The increased kd was accompanied by decreased neutralizing activity. The KD measured against immobilized G protein of VHSV strain DK-F1 was 2.4 nM for the parent MAb and 227 and 77 nM for the daughter Fab and scAb, respectively (Cupit et al., 2001; PMID: 11682124).
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