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We first analysed the binding of the individual domains (B1 B5) of PpL312 to human Vκ light chains (huVκ) subtypes 1 (huVκI) and 3 (huVκIII).
First, we analysed the binding of VAPBP56S to PTPIP51 in immunoprecipitation assays.
We analysed the binding of purified Arf1 to artificially generated liposomes in the presence of GTP or GDP.
Here we analysed the binding of the anti-rMal d 1 and anti-rApi g 1 Fab fragments against rBet v 1.
We therefore analysed the binding of Msk1 and Ezh2 and their associated histone marks (H3S28ph and H3K27me3, respectively) at MyoG and mCK regulatory regions.
As a control in our experiments, we analysed the binding of the non-toxic Cry1Ab F371A mutant that is affected in its irreversible binding to BBMVs [ 28].
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Chromatin immunoprecipitation (ChIP) was used to analyse the binding of p53 protein on the BAX gene promoter in the MI and MI + OxCy treated cardiac tissue.
Finally, chromatin immunoprecipitation assay (ChIP) was used to analyse the binding of IRF-1 to the PUMA promoter in AGS cells after IRF-1 induction.
We performed the ChIP and RT PCR to analyse the binding of Nap1 in wild-type and HTZ1 mutant (Supplementary Figure S11).
We next decided to verify these results and the affect of lysine acetylation in the context of the intact proteins by analysing the binding of the Wapl domain to an intact Smc3 globular head.
Here, we analyse the binding of the P14 soluble TCR to a broad panel of related H-2Db-peptide complexes by surface plasmon resonance, and compare this with their diverse cellular responses.
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