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We compared the detection results tested by the protein chip assay and ELISA, respectively.
This might be due to the very low concentration of HBsAb in serum samples which could not be detected by the protein chip assay.
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By this approach, an immobilized single-stranded DNA (ssDNA) surface can be transferred/modified into a protein chip by flowing in ssDNA-conjugated protein when the protein chip measurement is needed.
The detection limit of the protein chip assay was demonstrated by incubation of model arrays with different concentrations of anti-IgG.
SELDI technology was commercialized in 1997 as the Protein Chip system and is marketed by Bio-Rad Laboratories.
TeloChIP is launched by clicking the link in the 'Location' column within the Telomeric Protein ChIP table browser.
To confirm the identity of the m/z 8558 protein peak by protein chip immunocapture, pre-activated RS100 protein chips (Bio-Rad) were pre-coupled with 2 μg of monoclonal anti-human ubiquitin antibody (R&D) in 50 mℳ NaHCO3 buffer (pH 9.2) at 4 °C.
In our study, we identified the peak at m/z 13870 as full-length TTR; however, a peak at m/z 13756 detected by Q10 protein chip was also significantly upregulated in the serum of breast cancer patients (Table S1 in Additional file 2).
Serum samples were analyzed by SELDI-TOF maspectrometrytry using the CM10 protein chip of Ciphergen (Fremont, CA, USA).
These approaches include yeast two-hybrid, protein co-immunoprecipitation followed by mass spectrometry (MS), protein chip technologies and tandem affinity purification (TAP) with MS. Such data have led researchers to discover protein functions through PPI networks, in which a node represents a protein and an edge mimics an interaction between two proteins.
However, for both techniques, the DNA fragments, co-purified with the target protein (ChIP-DNA), are generated by sonication and generally fall within the size range of 100 500 bp.
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