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Solid-phase radiolabeling binding assays to test IG3 ability to bind to its targets.
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Examples of this approach include washing cell lysate extracts over a bead column fixed with an approved drug [ 64], high-throughput Biacore screening of an approved drug library against protein tyrosine phosphatase 1B [ 65], or high-throughput direct-binding assays to test drugs against 317 kinases [ 19].
We used a Far Western ligand binding assay to test the ability of the PBD to bind NPM/B23.
To substantiate this finding, we took advantage of chromatin immunoprecipitation (ChIP) assays to test whether the binding of NF-κB to its endogenous promoter was influenced in LRP16-knockdown cells.
In traditional approaches, investigators have used luciferase reporter assays to test individual TF binding sites of enhancers.
They use a western blot to determine whether mutant p53 levels are reduced, a DNA-binding assay to test whether recognition of any of three p53 target sequences is compromised, and fluorescence microscopy to assay nuclear localization.
Peptides predicted to bind were synthesized and tested in binding assays to determine those with high affinity.
The specificity of the enriched phages was tested in binding assays to RMS and normal cells individually (Fig. 1A).
To demonstrate whether the action of E2F1 on TSP1 occurs in vivo, we conducted chromatin Immunoprecipitation assay to test the binding of E2F1 in the TSP1 promoter.
Further, we performed ChIP assay to test the binding of OCT1 to synbindin promoter in vivo.
We have developed a straightforward pull-down assay to test ATP binding capability, and used N-glycosylation mutagenesis both to confirm the extent of N-linked glyconylation on hP2X4 and DdP2XA and validate homology models of the two receptors.
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CEO of Professional Science Editing for Scientists @ prosciediting.com