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Immunoglobulin binding proteins (IBPs) are broadly used as reagents for the purification and detection of antibodies.
The novel fusion protein with optimized interdomain linker length will be a useful tool for the purification and detection of various IgGs including mouse IgG1 that binds only weakly to natural protein A.
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All other reagents for purification and detection of PrPres were from the Bio-Rad TeSeE and TeSeE Sheep & Goat kits.
The strong and specific interaction between SPA and the constant part (Fc) of certain immunoglobulins (Ig) have made it useful for purification and detection of immunoglobulins in a variety of different applications [ 45, 46] and therefore in our study the ZZ tag was used for purification of IGF-1 fusion proteíns expressed in chloroplasts.
Lectins have long been used for purification and detection of glycans in many studies [ 70]; many lectins have overlapping affinity while some others have unique specificity, allowing for the efficient detection of differential expression of glycan structure.
The advantage of using fusion proteins to facilitate purification and detection of the recombinant protein is now widely recognized.
Extraction, purification, and detection of the sterols are time-consuming and error-prone.
We show in this paper how such tags may be utilized for immobilization and separation as well as purification and detection of monoclonal and polyclonal phage populations.
The resultant expression plasmid contained a His6 tag at the C terminus of the RNF14 gene for protein purification and detection by antibodies.
Two types of activity-based probes are widely used in chemical proteomics: fluorescent probes for the rapid identification of certain targets and biotinylated probes for target purification and detection.
It combines turbulent flow chromatography for analyte extraction and purification with LC-MS/MS for analytical separation and detection of the analytes.
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