We assayed a set of anti-CD20 IgG1 variants that had identical Fab regions, but alterations in the Fc regions, in both the soluble receptor-based and cell-based FcγRIIIa binding assays.
Through a high throughput screening assay, a set of compounds were found able to inhibit the enzymatic activity of cathepsin B. The binding structures of these active compounds were modeled through docking simulation.
In the X-peptide pulldown assay, a set of 12-mer peptides (X-I-F-S-T-I-E-G-R-T-Y-K-biotin) bearing N-terminal type 1 (Arg, His, and Lys), type 2 (Phe, Trp, Tyr, and Leu) or stabilizing (Val, Asp, and Gly) residues were cross-linked through C-terminal biotin to streptavidin agarose resin (0.5 mg peptide per ml settled resin).
In this assay, a set of forward and reverse primers were designed targeting the serotype conserved region at the NS5 gene, at the same time flanking a variable region for all four serotypes which were used to design the serotype-specific TaqMan probes.
We assayed a set of biochemical parameters to estimate the possible interference from either wild-type or mutant HPV-16 E7 with the cellular redox equilibrium.
Bataillon et al. 30 later assayed a set of favorable mutants in a large set of very simple environments (95 different carbon sources).
For the single colony formation assay, a set of serial dilutions was performed, and the number of viable ES cell colonies was assessed with alkaline phosphatase (Millipore).
To address this, the authors should include in this assay a set of negative controls, including a construct lacking luciferase, and a set of contexts with very low RTP scores, to establish a background readthrough rate.
To determine the detection limit of the protein chip assay, a set of model arrays in which human IgG was spotted were structured and the model arrays were incubated with different concentrations of anti-IgG.
In order to assess the analytical sensitivity of the QuanTAS-PCR assay, a set of mutant/wild-type mixes were prepared by mixing Cq normalised HEL DNA (MUT) and HL-60 DNA (WT).
