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Principally in both assays (binding to Her2-positive cells or to Her2-coated tips), the homodimeric Fcab molecule could potentially interact with two Her2 molecules.
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Previous attempts to use this antibody in chromatin immunoprecipitation experiments in wild type animals to assay binding to cis-acting hlh-1 enhancer fragments known to be involved in positive auto-regulation were unsuccessful [7].
To this end, we assayed binding to a TEL2 pep-spot substitution array in which each residue in the polypeptide was substituted by all other amino acids.
With the aim of obtaining information on the mode of fragment binding, we synthesized a small library of derivatives based on 8 and assayed binding to MTIP by DSF (Table 3).
We treated BMDM with Pam3CSK4 for 8 h then stimulated with IFN-γ for 4 h, followed by chromatin immunoprecipitation (ChIP) to assay binding of PolII to the CXCL11, CIITA, and NOS2 promoters.
To assay cholesterol binding to NPC1L1 NTD), we utilized an assay previously developed for monitoring cholesterol binding to SCAP [13].
Human CLCA1 was assayed for binding to cell-surface TMEM16A using a flow cytometry-based binding assay.
Wild-type and mutant Snu13p proteins were assayed for binding to U4 snRNA and U3 snoRNA.
Six of the new compounds which displayed high in vitro CB1 binding affinities were assayed for binding to CB2 receptor.
Several compounds from each class were synthesized and assayed for binding to the human bradykinin B2 receptor.
The three preparations were used to assay for binding to 3FN- 9 11 3FN- 9 11inding in the presence of EDTalone mM), or carried out in the presence of MnCl2.
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