Review



metal affinity chromatography plate  (TaKaRa)


Bioz Verified Symbol TaKaRa is a verified supplier
Bioz Manufacturer Symbol TaKaRa manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
    • 99
      Buy from Supplier

    Structured Review

    TaKaRa metal affinity chromatography plate
    a.) Purification of Fc-hel8-L1-3. Fc-hel8-L1-3 was purified from Expi293 supernatants by Ni-NTA affinity <t>chromatography,</t> 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).
    Metal Affinity Chromatography Plate, supplied by TaKaRa, used in various techniques. Bioz Stars score: 99/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/his+tag+affinity+chromatography/bio_rxiv__64898__2026__04__27__720530-400-17-26?v=TaKaRa
    Average 99 stars, based on 7 article reviews
    metal affinity chromatography plate - by Bioz Stars, 2026-07
    99/100 stars

    Images

    1) Product Images from "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"

    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

    Journal: bioRxiv

    doi: 10.64898/2026.04.27.720530

    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).
    Figure Legend 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).

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



    Similar Products

    metal affinity chromatography plate  (TaKaRa)
    99
    TaKaRa metal affinity chromatography plate
    a.) Purification of Fc-hel8-L1-3. Fc-hel8-L1-3 was purified from Expi293 supernatants by Ni-NTA affinity <t>chromatography,</t> 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).
    Metal Affinity Chromatography Plate, supplied by TaKaRa, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/his+tag+affinity+chromatography/bio_rxiv__64898__2026__04__27__720530-400-17-26?v=TaKaRa
    Average 99 stars, based on 1 article reviews
    metal affinity chromatography plate - by Bioz Stars, 2026-07
    99/100 stars
    		  Buy from Supplier
    ni nta sepharose 6hp his tag affinity chromatography resin  (Sangon Biotech)
    86
    Sangon Biotech ni nta sepharose 6hp his tag affinity chromatography resin
    a.) Purification of Fc-hel8-L1-3. Fc-hel8-L1-3 was purified from Expi293 supernatants by Ni-NTA affinity <t>chromatography,</t> 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).
    Ni Nta Sepharose 6hp His Tag Affinity Chromatography Resin, supplied by Sangon Biotech, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/his+tag+affinity+chromatography/pm42264255-53-38-49?v=Sangon+Biotech
    Average 86 stars, based on 1 article reviews
    ni nta sepharose 6hp his tag affinity chromatography resin - by Bioz Stars, 2026-07
    86/100 stars
    		  Buy from Supplier
    his tag affinity chromatography  (TaKaRa)
    99
    TaKaRa his tag affinity chromatography
    a.) Purification of Fc-hel8-L1-3. Fc-hel8-L1-3 was purified from Expi293 supernatants by Ni-NTA affinity <t>chromatography,</t> 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).
    His Tag Affinity Chromatography, supplied by TaKaRa, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/his+tag+affinity+chromatography/pm41912627-188-25-32?v=TaKaRa
    Average 99 stars, based on 1 article reviews
    his tag affinity chromatography - by Bioz Stars, 2026-07
    99/100 stars
    		  Buy from Supplier
    ni ida affinity chromatography  (MACHEREY NAGEL)
    93
    MACHEREY NAGEL ni ida affinity chromatography
    a.) Purification of Fc-hel8-L1-3. Fc-hel8-L1-3 was purified from Expi293 supernatants by Ni-NTA affinity <t>chromatography,</t> 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).
    Ni Ida Affinity Chromatography, supplied by MACHEREY NAGEL, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/his+tag+affinity+chromatography/pmc12826058-279-4-8?v=MACHEREY+NAGEL
    Average 93 stars, based on 1 article reviews
    ni ida affinity chromatography - by Bioz Stars, 2026-07
    93/100 stars
    		  Buy from Supplier
    his-tag affinity chromatography ni-nta  (Qiagen)
    90
    Qiagen his-tag affinity chromatography ni-nta
    a.) Purification of Fc-hel8-L1-3. Fc-hel8-L1-3 was purified from Expi293 supernatants by Ni-NTA affinity <t>chromatography,</t> 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).
    His Tag Affinity Chromatography Ni Nta, supplied by Qiagen, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/his+tag+affinity+chromatography/pm40653654-189-15-19?v=Qiagen
    Average 90 stars, based on 1 article reviews
    his-tag affinity chromatography ni-nta - by Bioz Stars, 2026-07
    90/100 stars
    		  Buy from Supplier
    his-tag affinity gravity-flow chromatography ni-nta matrices  (Qiagen)
    90
    Qiagen his-tag affinity gravity-flow chromatography ni-nta matrices
    a.) Purification of Fc-hel8-L1-3. Fc-hel8-L1-3 was purified from Expi293 supernatants by Ni-NTA affinity <t>chromatography,</t> 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).
    His Tag Affinity Gravity Flow Chromatography Ni Nta Matrices, supplied by Qiagen, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/his+tag+affinity+chromatography/pm40498451-126-16-19?v=Qiagen
    Average 90 stars, based on 1 article reviews
    his-tag affinity gravity-flow chromatography ni-nta matrices - by Bioz Stars, 2026-07
    90/100 stars
    		  Buy from Supplier
    his-tag affinity chromatography  (Beyotime)
    90
    Beyotime his-tag affinity chromatography
    a.) Purification of Fc-hel8-L1-3. Fc-hel8-L1-3 was purified from Expi293 supernatants by Ni-NTA affinity <t>chromatography,</t> 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).
    His Tag Affinity Chromatography, supplied by Beyotime, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/his+tag+affinity+chromatography/pm40424702-98-16-19?v=Beyotime
    Average 90 stars, based on 1 article reviews
    his-tag affinity chromatography - by Bioz Stars, 2026-07
    90/100 stars
    		  Buy from Supplier
    tag affinity chromatography purification  (Qiagen)
    99
    Qiagen tag affinity chromatography purification
    a.) Purification of Fc-hel8-L1-3. Fc-hel8-L1-3 was purified from Expi293 supernatants by Ni-NTA affinity <t>chromatography,</t> 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).
    Tag Affinity Chromatography Purification, supplied by Qiagen, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/his+tag+affinity+chromatography/pmc11957540-200-0-8?v=Qiagen
    Average 99 stars, based on 1 article reviews
    tag affinity chromatography purification - by Bioz Stars, 2026-07
    99/100 stars
    		  Buy from Supplier

    Image Search Results


    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