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affinity matrix chromatography  (New England Biolabs)


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    New England Biolabs affinity matrix chromatography
    Affinity Matrix Chromatography, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 7360 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    a.) Purification of Fc-hel8-L1-3. Fc-hel8-L1-3 was purified from Expi293 supernatants by Ni-NTA affinity chromatography, followed by removal of the purification tag, protein concentration and buffer exchange. Samples of culture supernatants at 24 h and 72 h post transfection, Ni-NTA eluates and samples after dialysis were taken and analyzed by SDS-PAGE under reducing and (where indicated) non-reducing conditions followed by Coomassie staining. b.) SEC behavior of Fc-hel8-L1-3. Dialyzed samples of purified Fc-hel8-L1-3 were analyzed by size exclusion chromatography (SEC) using a Superdex 200 increase 10/300 gl column. Protein absorbance at 280nm was normalized against the maximum signal recorded during the SEC run. The void volume of the column at ∼8 mL is indicated. c.) Impact of protein charge on PK and MIC of different Fc-LysM-CHAP variants. AUC at 4 h (AUC 4h , blue) was determined from the PK curves shown in . MIC values (red) are as determined in . AUC 4h (log10 scale) and MIC (log2 scale) were plotted against the charge at pH7 of each Fc-LysM-CHAP variant (as determined from the amino acid sequence). The relationship between charge and AUC was tested for linear correlation with the Pearson method; the relationship between charge and MIC was tested for non-linear correlation with the Spearman method (correlation coefficients (r) and significance values (P) are indicated). AUC: area under curve; MIC: minimal inhibiting concentration. d.) PK comparison of dimeric and monomeric Fc fusions. PK curves of dimeric (red) and monomeric (green) formats of Fc-hel8-L1 and the corresponding naked lysin (L1, blue) were determined as described in .). Datapoints represent mean and standard deviation (n=3).

    Journal: bioRxiv

    Article Title: Multi-dimensional optimization of a lysin towards a ribolysin against life-threatening S. aureus infections: Fc-LysM-CHAP and its strong synergy with standard of care antibiotics

    doi: 10.64898/2026.04.27.720530

    Figure Lengend Snippet: a.) Purification of Fc-hel8-L1-3. Fc-hel8-L1-3 was purified from Expi293 supernatants by Ni-NTA affinity chromatography, followed by removal of the purification tag, protein concentration and buffer exchange. Samples of culture supernatants at 24 h and 72 h post transfection, Ni-NTA eluates and samples after dialysis were taken and analyzed by SDS-PAGE under reducing and (where indicated) non-reducing conditions followed by Coomassie staining. b.) SEC behavior of Fc-hel8-L1-3. Dialyzed samples of purified Fc-hel8-L1-3 were analyzed by size exclusion chromatography (SEC) using a Superdex 200 increase 10/300 gl column. Protein absorbance at 280nm was normalized against the maximum signal recorded during the SEC run. The void volume of the column at ∼8 mL is indicated. c.) Impact of protein charge on PK and MIC of different Fc-LysM-CHAP variants. AUC at 4 h (AUC 4h , blue) was determined from the PK curves shown in . MIC values (red) are as determined in . AUC 4h (log10 scale) and MIC (log2 scale) were plotted against the charge at pH7 of each Fc-LysM-CHAP variant (as determined from the amino acid sequence). The relationship between charge and AUC was tested for linear correlation with the Pearson method; the relationship between charge and MIC was tested for non-linear correlation with the Spearman method (correlation coefficients (r) and significance values (P) are indicated). AUC: area under curve; MIC: minimal inhibiting concentration. d.) PK comparison of dimeric and monomeric Fc fusions. PK curves of dimeric (red) and monomeric (green) formats of Fc-hel8-L1 and the corresponding naked lysin (L1, blue) were determined as described in .). Datapoints represent mean and standard deviation (n=3).

    Article Snippet: Ala mutation (11–18,28,39,40–46) on LysM with Fc-hel14-L1-4 background in supernatants were purified using a membrane-based 24-well immobilized metal affinity chromatography plate (CapturemTM His-Tagged Purification 24-well Plate, Takara Bio, Cat. No. 635730) operated on a vacuum manifold.

    Techniques: Purification, Affinity Chromatography, Protein Concentration, Buffer Exchange, Transfection, SDS Page, Staining, Size-exclusion Chromatography, Variant Assay, Sequencing, Concentration Assay, Comparison, Standard Deviation