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By utilizing this assay, we studied the responses of gene-silenced plants to dehydration stress by evaluating the decline in fresh weight of detached leaves.
Utilizing this assay, we studied the expression and dimerization status of HER-kinase receptors in 16 paraffin-embedded tissue sections of normal human skin obtained from patients with solid tumours.
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Although only the phagocytosis of opsonized sRBCs was utilized in this assay, we hypothesize that there would also be different levels of cAMP generated in response to other internalized particles, particularity bacteria.
In the present study, we utilized this assay to examine ALDH1 enzymatic activity in epithelial tumor cells in vitro.
Here we utilize this assay to compare mutation rates of various mono- and dinucleotides.
Here we utilize this assay to compare mutations of mono- and dinucleotide repeats in human colorectal cells.
We utilized this assay to quantify fl-OPN in the plasma of healthy volunteers in comparison with patients with metastatic breast cancer.
We have utilized this assay in a non-destructive method to quantify free thiols in our hydrogels such that, if desired, gels may be rinsed of reagent, treated with tris 2-carboxyethyl phosphine (tris 2-carboxyethyl phosphine-used in addiTCEPal studies.
Since viable adults were required for this assay, we utilized the Slbp10 hypomorphic allele.
Utilizing a radioactive assay, we have shown that SETD6 does not methylate any of the coupling enzymes (Fig. 4c).
We utilized this biochemical assay for APP cleavage by gamma-secretase in a high-throughput screen of a chemical library and discovered amino-caprolactam sulfonamide leads, which demonstrated APP-selective inhibition of gamma-secretase activity in vitro.
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