Anti-PEG RabMAb® primary antibodies have been demonstrated to show enhanced binding and selectivity when compared to other Anti-PEG antibodies (e.g. Clone AGP3, Vendor A), in both sandwich and direct ELISA assays, for the quantification of PEG and PEG-modified proteins.
These results have been shown to be similar regardless of if it was PEG or PEG-modified targets being detected.
In-house Comparison Data
Figure 1b. Comparison of anti-PEG-47 RabMAb® primary antibody (ab51257) and Vendor A mouse MAb (Clone AGP3) in Direct ELISA assay. Goat anti-rabbit IgG-AP used for Anti-PEG-47 detection; goat anti-mouse IgM-AP used for Vendor A MAb detection. Fig. 1a. Direct ELISA using 1 ug/mL of PEG-GCSF. Fig. 1b. Direct ELISA using 1 ug/mL of PEG-IFN.
Figure 2. Comparison of sandwich ELISA using RabMAb®/RabMAb® antibodies (PEG 47/PEG 47, ab51257) and MAb/RabMAb® antibodies (Vendor A/PEG 47). PEG 47/PEG 47: Plated coated with 5 ug/mL of #47; 5 ug/mL of #47 used for detection. Vendor A/ PEG 47: Plates coated with 100 ug/mL of Vendor A Mouse MAb; 5 ug/mL of #47 used for detection. Vendor A = clone AGP3.
The relatively high (low nM) affinity of the (PEG RabMAb® primary antibody, ab53449) meant that we could extensively wash the wells of the assay (with PBS no Tween) and not remove the specifically bound Ab – this essentially meant we had a ‘sensitive’ assay with ‘low background levels’ and a ‘good signal-to-noise window.
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