Exact(3)
The secreted fusion protein was purified from serum-free culture medium by using affinity chromatography with Protein G Sepharose (GE Healthcare Europe).
By using affinity chromatography, we find that Arl8-GTP binds to the soluble protein SKIP (SifA and kinesin-interacting protein, aka PLEKHM2).
Recombinant soluble scFv antibodies were produced from the periplasmic extract of E. coli HB2151 cells, which were purified by using affinity chromatography with an anti-E-tag Sepharose column (Hi-Trap anti-E-tag column) according to the manufacturer's protocol.
Similar(57)
Upon proteolytic cleavage, the N- and C-terminal parts of BlaP remain strongly linked together and are separated from the ChBD domain by depletion using affinity chromatography via the C-terminal His-tag.
These proteins containing reduced thiols could be enriched by using PAO affinity chromatography.
The (His 6-p53 fusion protein was purified by using metal-affinity cHis 6-p53aphy.
WUPyV VP1 and KIPyV VP1 were expressed in bacteria as N-terminal, GST-tagged fusion proteins and subsequently purified by using glutathione-affinity chromatography.
By substituting tris 2-carboxyethyl phosphine (tris 2-carboxyethyl phosphineenTCEPor DTT, Foley et al. improved the capture of VTPs from a Tritononthiolsoluble reducingn extragenty using PAO-afornity chromatography.
Using affinity purification followed by liquid chromatography/mass spectrometry, we identified alpha-tubulin as a novel binding partner for dysferlin.
On the other hand, serine or threonine phosphorylated proteins or peptides are enriched by using immobilized-metal affinity chromatography (IMAC) and metal-oxide affinity chromatography (e.g. TiO2 based).
GST-LSD1 production from an E. coli expression system followed by purification using glutathione affinity chromatography were performed as previously described.
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