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To demonstrate that this mutant Pdr16p E235A, K267A is unable to bind PI we employed in vitro lipid binding assay in which purified lipid transfer protein is co-incubated with radiolabeled permeabilized HL60 cells.
Binding of rituximab to CD20 was determined using a cell-based competitive binding assay in which test samples were used to displace a fluorescently labeled rituximab from the CD20 expressed on the surface of the human Raji B cell line.
We then designed a novel cell-free cytoskeleton binding assay in which a set of GST LSP1 fusion proteins are allowed to bind to the cytoskeleton in NP-40 soluble lysates of BW5147 cells and are recovered in the low-speed detergent insoluble pellet.
The binding between LOX-1 and NadA was further corroborated by cellular binding assay in which the CHO cells transiently expressing LOX-1 were able to bind recombinant NadA.
To exclude this possibility we performed an in vitro binding assay in which HEK293T cells transfected with an APP-Citrine expressing construct were incubated with either antibody 6E10 as a positive control (Fig. 3 A), 22C4 IgG (Fig. 3 B), 22C4 scFv (Fig. 3 C) or corresponding non-specific antibodies for 30 min on ice (data not shown).
However, in an in vitro binding assay in which regions of recombinant PTPμ were expressed [ 17], the homophilic binding site was localized to the immunoglobulin (Ig -like domaIg -like
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Differences in our results may be explained by the aforementioned study using radioligand binding assays, in which IGF-1 ligand was used as the probe to evaluate receptor totals.
The technology is actually more based on traditional radioligand binding assays in which the bound marker ligand is now not analyzed by the radioactivity of the marker, but by its molecular mass.
We therefore carried out liposome binding assays in which we used liposomes containing 65% phosphatidylcholine, 20% phosphatidylethanolamine, 5% phosphatidylserine and 10% individual phosphoinositides and examined the sedimentation of GST-PH with the vesicles.
Employing a DNA affinity-binding assay in which endogenous proteins that bind to the NRE can be detected on a solid bead matrix, it was suggested that TRβ1 is recruited to NRE beads in a ligand-dependent manner [15].
The Bio-Rad Protein Assay is a dye-binding assay in which a differential color change of a dye occurs in response to various concentrations of protein.
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