Recombinant Human Anti-IAV HA Antibody (3.1) (CAT#: PABL-203)

Figure 1 Neutralizing activity of monomeric 3.1 isotypes. mAb 3.1 IgA1 (red-bordered circles), IgA2 (red circles), IgG1 (black circles), and IgG3 (gray circles) against rg-A/Chicken/Vietnam/C58/2004 (H5N3). Both IgA subtypes neutralized more potently than the IgG subtypes.

Maurer, M. A., Meyer, L., Bianchi, M., Turner, H. L., Le, N. P., Steck, M.,... & Hangartner, L. (2018). Glycosylation of Human IgA Directly Inhibits Influenza A and Other Sialic-Acid-Binding Viruses. Cell reports, 23(1), 90.

Figure 2 Neutralizing activity of IgG1/IgA1 chimeric 3.1 antibodies.

The four-letter code refers to the isotype origin of the CH1, hinge, CH2, and CH3, respectively. As a control, 3.1 was included as a pure IgG1 molecule (black closed circles) and an IgA1 molecule (black-bordered open circles) and plotted in each panel. The titration curves of the indicated chimeric molecules are depicted in gray-bordered open circles, while those for IgG1 and IgA1 are depicted in black and white circles, respectively. On top of each panel, the chimerism of the molecule is depicted with IgG1-derived areas in black, IgA1-derived areas in red, and the variable region in white.

Maurer, M. A., Meyer, L., Bianchi, M., Turner, H. L., Le, N. P., Steck, M.,... & Hangartner, L. (2018). Glycosylation of Human IgA Directly Inhibits Influenza A and Other Sialic-Acid-Binding Viruses. Cell reports, 23(1), 90.

Figure 3 Antiviral Effect of Non-specific IgA

Left panels: the antiviral activities of HIV-1 gp120- specific mAb b12 and H5-receptor binding sitespecific mAb 65c6 were tested against the indicated viruses. As a control, IgG1, IgA1 expressed in S cells (IgA1 S, red-bordered circles), and samples in which all IgA immunoglobulin has been depleted were used (red triangles). Right panels: antiviral activities of IgG1 or IgA1 of mAbs 3.1, 1.12, and HIV-gp41-specific mAb 2F5 were tested against Newcastle disease virus.

Maurer, M. A., Meyer, L., Bianchi, M., Turner, H. L., Le, N. P., Steck, M.,... & Hangartner, L. (2018). Glycosylation of Human IgA Directly Inhibits Influenza A and Other Sialic-Acid-Binding Viruses. Cell reports, 23(1), 90.

Figure 1 Recombinant Human Anti-IAV HA Antibody (3.1) (PABL-203) in SDS-PAGE

SDS-PAGE analysis of PABL-203 In non-reduced (lane 1) and β-mercaptoethanol-reduced (lane 2) conditions. Gel stained for 30 minutes with Coomassie Blue. As a result of different β-mercaptoethanol-reduced proteins (Heavy chain and Light chain) migrate as about 50 kDa and 25 kDa, respectively. And non-reduced protein migrates as 130-180 kDa.

Figure 2 Recombinant Human Anti-IAV HA Antibody (3.1) (PABL-203) in SEC-HPLC

The purity of PABL-203 was greater than 95% as determined by SEC-HPLC.

Figure 3 Recombinant Human Anti-IAV HA Antibody (3.1) (PABL-203) in ELISA

ELISA analysis of PABL-203 was performed by coating with Influenza A H1N1 (A/California/04/2009) Hemagglutinin / HA Protein (His Tag).

The secondary antibody: HRP-Anti-Human IgG (H+L)

Figure 4 Recombinant Human Anti-IAV HA Antibody (3.1) (PABL-203) in WB

Western blot analysis of PABL-203 was performed with Influenza A H1N1 (A/California/04/2009) Hemagglutinin / HA Protein (His Tag).
Lane 1: Reducing antigen (0.1 μg)
Lane 2: Reducing antigen (0.3 μg)
Lane 3: Reducing antigen (0.6 μg)
The secondary antibody: HRP-Anti-Human IgG (H+L)

Figure 5 Recombinant Human Anti-IAV HA Antibody (3.1) (PABL-203) in Dot Blot

Dot blot analysis of PABL-203 was performed with Influenza A H1N1 (A/California/04/2009) Hemagglutinin / HA Protein (His Tag).
The secondary antibody: HRP-Anti-Human IgG (H+L)