Sentence examples for binding to cell lysates from inspiring English sources

Diluted aliquots of rabbit polyclonal antipimonidazole antisera were used for the enzyme-linked immunosorbent assay (ELISA) of pimonidazole binding to cell lysates (Arteel et al, 1995).

Briefly, H-cAMP added to cell lysates was used to compete with endogenous cAMP for binding to a specific cAMP-binding protein.

Briefly, chloroform was added to cell lysates.

In most published studies of cancer cells, the presence of GNRHR is inferred on the basis of RT-PCR detection of mRNA and/or by detection of ligand binding to whole cell lysates.

The cell lysate is directed to cell lysate collecting chambers.

Nevertheless, the M2 and C-term regions also contribute to PABPC1 binding in cell lysates.

Importantly, the observation that the DmGW182 PAmotiftif directly interacts with DmPABPC1 in vitro, but is neither sufficient nor necessary for binding to DmPABPC1 in cell lysates, suggest that the DmPAM2 motif might not be able to efficiently compete with additional PAM2-containing proteins for binding to PABPC1 in D. melanogaster cells.

This idea is based on the observation that the SD of DmGW182 competes with eukaryotic initiation factor 4G (eIfor) for binding to PABPC1 in cell lysates (Zekri et al, 2009).

To more precisely elucidate the molecular modifications of 4E-BP1 induced by PP242 that induce eIF4E binding, whole cell lysates were prepared from HEK293 cells that were subjected to short (30 min) treatment with PP242 or rapamycin followed by 2DE (isoelectric focusing and SDS-PAGE) and western blot analyses.

Addition of a kinase inhibitor to the cell lysates enables it to bind to its specific target(s), occupying the binding sites and preventing binding to the kinobeads, whereas the binding of nontargeted kinases and other proteins are unaffected.

To evaluate how the interaction between GW182 and PABPC1 contributes to silencing, we tested whether DmGW182 mutants that are impaired in PABPC1 binding in cell lysates could complement silencing in cells lacking endogenous GW182.