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A recent rapid communication of 15 serous and two mucinous cystadenocarcinomas, used radiolabelled RC-160 binding assays, specific for sst2 and 5, RT PCR, to demonstrate expression of SRIF receptors in malignant ovarian tumours (Halmos et al, 2000).
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For radioligand binding assays specific binding was calculated by subtraction of non-specific binding (the highest unlabelled hAM concentration).
To develop mAb-specific binding assays for each antitoxin, we mapped the epitopes of the six mAbs.
The predominant assay type is termed "type-B" or binding assay because it encompasses the enzyme inhibition and receptor binding assays most commonly reported for compounds tested against molecular targets in vitro and, implicitly, with binding specificity.
Specific binding is defined as for receptor binding assays on tissue homogenates, and includes diminution of bound radioactivity by the addition of excess cold ligand and establishing a pharmacological profile using closely- and distantly-related compounds.
Non-specific binding was obtained from two competitive homologous binding assays with non-radioactive Ga68-PSMA-11.
The binding assays proceeded as follows.
Specific rapid filtration binding assays have been useful for almost 30 years both for drug discovery and understanding molecular mechanisms of drug action.
For the detection of allergen-specific IgE in sera, solid-phase IgE-binding assays like the CAP test are commonly used.
However, cell-binding assays require specific considerations to accurately quantify the binding affinity of a protein protein interaction.
Moreover, these different affinity measurement technologies require that binding assays are performed under specific conditions that differ from the conditions that are used for the competition assays, and also from conditions during a true plant pathogen interaction.
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