slurry packing disposable polyethylene chromatography columns Search Results


86
Chrom Tech hplc slurry packing system
Hplc Slurry Packing System, supplied by Chrom Tech, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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IBA Lifesciences strep tactin super flow high capacity slurry
Preparation of antigens for immunization. ( A ) Purification of recombinant Junín virus (JUNV) GP1. JUNV GP1 containing a C-terminal Strep tag (GP1-Strep) was transiently expressed in HEK-293 cells <t>and</t> <t>purified</t> via affinity chromatography using <t>Strep-Tactin</t> resin. The eluted fractions were analyzed by Coomassie staining (left panel). Alternatively, JUNV GP1 containing a C-terminal hexahistidine (GP1-His) tag was expressed in Freestyle 293-F cells and purified via affinity chromatography using HisTrap columns. The resulting protein fraction was also analyzed by Coomassie staining (right panel). ( B ) Hepatitis B virus core-like particles (HBV-CLPs) carrying JUNV GP1 peptide loops. HBV-CLPs containing the indicated antigens (i.e., Loop 3, Loop 7, Loop 10, or a control FLAG tag) were produced in E. coli and isolated from the soluble fraction of lysates via Strep tag-mediated affinity purification. Eluates were analyzed by Coomassie staining (upper panel) and Western blot with an anti-Strep antibody (1:30,000; StrepMAB Classic-HRP; IBA Lifesciences, Göttingen, Germany; lower panel). The position of the HBV core protein is indicated. ( C ) Electron microscopic analysis of HBV-CLPs. The purified HBV-CLPs generated in ( B ) were further analyzed by electron microscopy with negative staining. The scale bar shown represents 80 nm.
Strep Tactin Super Flow High Capacity Slurry, supplied by IBA Lifesciences, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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strep tactin super flow high capacity slurry - by Bioz Stars, 2026-09
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Omnifit Inc chromatography media
Preparation of antigens for immunization. ( A ) Purification of recombinant Junín virus (JUNV) GP1. JUNV GP1 containing a C-terminal Strep tag (GP1-Strep) was transiently expressed in HEK-293 cells <t>and</t> <t>purified</t> via affinity chromatography using <t>Strep-Tactin</t> resin. The eluted fractions were analyzed by Coomassie staining (left panel). Alternatively, JUNV GP1 containing a C-terminal hexahistidine (GP1-His) tag was expressed in Freestyle 293-F cells and purified via affinity chromatography using HisTrap columns. The resulting protein fraction was also analyzed by Coomassie staining (right panel). ( B ) Hepatitis B virus core-like particles (HBV-CLPs) carrying JUNV GP1 peptide loops. HBV-CLPs containing the indicated antigens (i.e., Loop 3, Loop 7, Loop 10, or a control FLAG tag) were produced in E. coli and isolated from the soluble fraction of lysates via Strep tag-mediated affinity purification. Eluates were analyzed by Coomassie staining (upper panel) and Western blot with an anti-Strep antibody (1:30,000; StrepMAB Classic-HRP; IBA Lifesciences, Göttingen, Germany; lower panel). The position of the HBV core protein is indicated. ( C ) Electron microscopic analysis of HBV-CLPs. The purified HBV-CLPs generated in ( B ) were further analyzed by electron microscopy with negative staining. The scale bar shown represents 80 nm.
Chromatography Media, supplied by Omnifit Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Bio-Rad gravity flow poly prep chromatography columns
Preparation of antigens for immunization. ( A ) Purification of recombinant Junín virus (JUNV) GP1. JUNV GP1 containing a C-terminal Strep tag (GP1-Strep) was transiently expressed in HEK-293 cells <t>and</t> <t>purified</t> via affinity chromatography using <t>Strep-Tactin</t> resin. The eluted fractions were analyzed by Coomassie staining (left panel). Alternatively, JUNV GP1 containing a C-terminal hexahistidine (GP1-His) tag was expressed in Freestyle 293-F cells and purified via affinity chromatography using HisTrap columns. The resulting protein fraction was also analyzed by Coomassie staining (right panel). ( B ) Hepatitis B virus core-like particles (HBV-CLPs) carrying JUNV GP1 peptide loops. HBV-CLPs containing the indicated antigens (i.e., Loop 3, Loop 7, Loop 10, or a control FLAG tag) were produced in E. coli and isolated from the soluble fraction of lysates via Strep tag-mediated affinity purification. Eluates were analyzed by Coomassie staining (upper panel) and Western blot with an anti-Strep antibody (1:30,000; StrepMAB Classic-HRP; IBA Lifesciences, Göttingen, Germany; lower panel). The position of the HBV core protein is indicated. ( C ) Electron microscopic analysis of HBV-CLPs. The purified HBV-CLPs generated in ( B ) were further analyzed by electron microscopy with negative staining. The scale bar shown represents 80 nm.
Gravity Flow Poly Prep Chromatography Columns, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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gravity flow poly prep chromatography columns - by Bioz Stars, 2026-09
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96
Bio-Rad econo pac chromatography column
Preparation of antigens for immunization. ( A ) Purification of recombinant Junín virus (JUNV) GP1. JUNV GP1 containing a C-terminal Strep tag (GP1-Strep) was transiently expressed in HEK-293 cells <t>and</t> <t>purified</t> via affinity chromatography using <t>Strep-Tactin</t> resin. The eluted fractions were analyzed by Coomassie staining (left panel). Alternatively, JUNV GP1 containing a C-terminal hexahistidine (GP1-His) tag was expressed in Freestyle 293-F cells and purified via affinity chromatography using HisTrap columns. The resulting protein fraction was also analyzed by Coomassie staining (right panel). ( B ) Hepatitis B virus core-like particles (HBV-CLPs) carrying JUNV GP1 peptide loops. HBV-CLPs containing the indicated antigens (i.e., Loop 3, Loop 7, Loop 10, or a control FLAG tag) were produced in E. coli and isolated from the soluble fraction of lysates via Strep tag-mediated affinity purification. Eluates were analyzed by Coomassie staining (upper panel) and Western blot with an anti-Strep antibody (1:30,000; StrepMAB Classic-HRP; IBA Lifesciences, Göttingen, Germany; lower panel). The position of the HBV core protein is indicated. ( C ) Electron microscopic analysis of HBV-CLPs. The purified HBV-CLPs generated in ( B ) were further analyzed by electron microscopy with negative staining. The scale bar shown represents 80 nm.
Econo Pac Chromatography Column, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Dr Maisch HPLC reprosil-pur c18-aq 3- m reverse phase resin
Preparation of antigens for immunization. ( A ) Purification of recombinant Junín virus (JUNV) GP1. JUNV GP1 containing a C-terminal Strep tag (GP1-Strep) was transiently expressed in HEK-293 cells <t>and</t> <t>purified</t> via affinity chromatography using <t>Strep-Tactin</t> resin. The eluted fractions were analyzed by Coomassie staining (left panel). Alternatively, JUNV GP1 containing a C-terminal hexahistidine (GP1-His) tag was expressed in Freestyle 293-F cells and purified via affinity chromatography using HisTrap columns. The resulting protein fraction was also analyzed by Coomassie staining (right panel). ( B ) Hepatitis B virus core-like particles (HBV-CLPs) carrying JUNV GP1 peptide loops. HBV-CLPs containing the indicated antigens (i.e., Loop 3, Loop 7, Loop 10, or a control FLAG tag) were produced in E. coli and isolated from the soluble fraction of lysates via Strep tag-mediated affinity purification. Eluates were analyzed by Coomassie staining (upper panel) and Western blot with an anti-Strep antibody (1:30,000; StrepMAB Classic-HRP; IBA Lifesciences, Göttingen, Germany; lower panel). The position of the HBV core protein is indicated. ( C ) Electron microscopic analysis of HBV-CLPs. The purified HBV-CLPs generated in ( B ) were further analyzed by electron microscopy with negative staining. The scale bar shown represents 80 nm.
Reprosil Pur C18 Aq 3 M Reverse Phase Resin, supplied by Dr Maisch HPLC, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Midwest Bio Services LLC liquid chromatography-tandem mass chromatograpy
Preparation of antigens for immunization. ( A ) Purification of recombinant Junín virus (JUNV) GP1. JUNV GP1 containing a C-terminal Strep tag (GP1-Strep) was transiently expressed in HEK-293 cells <t>and</t> <t>purified</t> via affinity chromatography using <t>Strep-Tactin</t> resin. The eluted fractions were analyzed by Coomassie staining (left panel). Alternatively, JUNV GP1 containing a C-terminal hexahistidine (GP1-His) tag was expressed in Freestyle 293-F cells and purified via affinity chromatography using HisTrap columns. The resulting protein fraction was also analyzed by Coomassie staining (right panel). ( B ) Hepatitis B virus core-like particles (HBV-CLPs) carrying JUNV GP1 peptide loops. HBV-CLPs containing the indicated antigens (i.e., Loop 3, Loop 7, Loop 10, or a control FLAG tag) were produced in E. coli and isolated from the soluble fraction of lysates via Strep tag-mediated affinity purification. Eluates were analyzed by Coomassie staining (upper panel) and Western blot with an anti-Strep antibody (1:30,000; StrepMAB Classic-HRP; IBA Lifesciences, Göttingen, Germany; lower panel). The position of the HBV core protein is indicated. ( C ) Electron microscopic analysis of HBV-CLPs. The purified HBV-CLPs generated in ( B ) were further analyzed by electron microscopy with negative staining. The scale bar shown represents 80 nm.
Liquid Chromatography Tandem Mass Chromatograpy, supplied by Midwest Bio Services LLC, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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liquid chromatography-tandem mass chromatograpy - by Bioz Stars, 2026-09
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90
Merck KGaA acetonitrile chromatographic grade
Preparation of antigens for immunization. ( A ) Purification of recombinant Junín virus (JUNV) GP1. JUNV GP1 containing a C-terminal Strep tag (GP1-Strep) was transiently expressed in HEK-293 cells <t>and</t> <t>purified</t> via affinity chromatography using <t>Strep-Tactin</t> resin. The eluted fractions were analyzed by Coomassie staining (left panel). Alternatively, JUNV GP1 containing a C-terminal hexahistidine (GP1-His) tag was expressed in Freestyle 293-F cells and purified via affinity chromatography using HisTrap columns. The resulting protein fraction was also analyzed by Coomassie staining (right panel). ( B ) Hepatitis B virus core-like particles (HBV-CLPs) carrying JUNV GP1 peptide loops. HBV-CLPs containing the indicated antigens (i.e., Loop 3, Loop 7, Loop 10, or a control FLAG tag) were produced in E. coli and isolated from the soluble fraction of lysates via Strep tag-mediated affinity purification. Eluates were analyzed by Coomassie staining (upper panel) and Western blot with an anti-Strep antibody (1:30,000; StrepMAB Classic-HRP; IBA Lifesciences, Göttingen, Germany; lower panel). The position of the HBV core protein is indicated. ( C ) Electron microscopic analysis of HBV-CLPs. The purified HBV-CLPs generated in ( B ) were further analyzed by electron microscopy with negative staining. The scale bar shown represents 80 nm.
Acetonitrile Chromatographic Grade, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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acetonitrile chromatographic grade - by Bioz Stars, 2026-09
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BIOTAGE biotage flash chromatographer
Preparation of antigens for immunization. ( A ) Purification of recombinant Junín virus (JUNV) GP1. JUNV GP1 containing a C-terminal Strep tag (GP1-Strep) was transiently expressed in HEK-293 cells <t>and</t> <t>purified</t> via affinity chromatography using <t>Strep-Tactin</t> resin. The eluted fractions were analyzed by Coomassie staining (left panel). Alternatively, JUNV GP1 containing a C-terminal hexahistidine (GP1-His) tag was expressed in Freestyle 293-F cells and purified via affinity chromatography using HisTrap columns. The resulting protein fraction was also analyzed by Coomassie staining (right panel). ( B ) Hepatitis B virus core-like particles (HBV-CLPs) carrying JUNV GP1 peptide loops. HBV-CLPs containing the indicated antigens (i.e., Loop 3, Loop 7, Loop 10, or a control FLAG tag) were produced in E. coli and isolated from the soluble fraction of lysates via Strep tag-mediated affinity purification. Eluates were analyzed by Coomassie staining (upper panel) and Western blot with an anti-Strep antibody (1:30,000; StrepMAB Classic-HRP; IBA Lifesciences, Göttingen, Germany; lower panel). The position of the HBV core protein is indicated. ( C ) Electron microscopic analysis of HBV-CLPs. The purified HBV-CLPs generated in ( B ) were further analyzed by electron microscopy with negative staining. The scale bar shown represents 80 nm.
Biotage Flash Chromatographer, supplied by BIOTAGE, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Metrohm AG ion chromatograph
Preparation of antigens for immunization. ( A ) Purification of recombinant Junín virus (JUNV) GP1. JUNV GP1 containing a C-terminal Strep tag (GP1-Strep) was transiently expressed in HEK-293 cells <t>and</t> <t>purified</t> via affinity chromatography using <t>Strep-Tactin</t> resin. The eluted fractions were analyzed by Coomassie staining (left panel). Alternatively, JUNV GP1 containing a C-terminal hexahistidine (GP1-His) tag was expressed in Freestyle 293-F cells and purified via affinity chromatography using HisTrap columns. The resulting protein fraction was also analyzed by Coomassie staining (right panel). ( B ) Hepatitis B virus core-like particles (HBV-CLPs) carrying JUNV GP1 peptide loops. HBV-CLPs containing the indicated antigens (i.e., Loop 3, Loop 7, Loop 10, or a control FLAG tag) were produced in E. coli and isolated from the soluble fraction of lysates via Strep tag-mediated affinity purification. Eluates were analyzed by Coomassie staining (upper panel) and Western blot with an anti-Strep antibody (1:30,000; StrepMAB Classic-HRP; IBA Lifesciences, Göttingen, Germany; lower panel). The position of the HBV core protein is indicated. ( C ) Electron microscopic analysis of HBV-CLPs. The purified HBV-CLPs generated in ( B ) were further analyzed by electron microscopy with negative staining. The scale bar shown represents 80 nm.
Ion Chromatograph, supplied by Metrohm AG, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Metrohm AG compact ion chromatograph (ic) 861 chromatography instrument
Preparation of antigens for immunization. ( A ) Purification of recombinant Junín virus (JUNV) GP1. JUNV GP1 containing a C-terminal Strep tag (GP1-Strep) was transiently expressed in HEK-293 cells <t>and</t> <t>purified</t> via affinity chromatography using <t>Strep-Tactin</t> resin. The eluted fractions were analyzed by Coomassie staining (left panel). Alternatively, JUNV GP1 containing a C-terminal hexahistidine (GP1-His) tag was expressed in Freestyle 293-F cells and purified via affinity chromatography using HisTrap columns. The resulting protein fraction was also analyzed by Coomassie staining (right panel). ( B ) Hepatitis B virus core-like particles (HBV-CLPs) carrying JUNV GP1 peptide loops. HBV-CLPs containing the indicated antigens (i.e., Loop 3, Loop 7, Loop 10, or a control FLAG tag) were produced in E. coli and isolated from the soluble fraction of lysates via Strep tag-mediated affinity purification. Eluates were analyzed by Coomassie staining (upper panel) and Western blot with an anti-Strep antibody (1:30,000; StrepMAB Classic-HRP; IBA Lifesciences, Göttingen, Germany; lower panel). The position of the HBV core protein is indicated. ( C ) Electron microscopic analysis of HBV-CLPs. The purified HBV-CLPs generated in ( B ) were further analyzed by electron microscopy with negative staining. The scale bar shown represents 80 nm.
Compact Ion Chromatograph (Ic) 861 Chromatography Instrument, supplied by Metrohm AG, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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compact ion chromatograph (ic) 861 chromatography instrument - by Bioz Stars, 2026-09
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86
Merck & Co radial chromatography
Preparation of antigens for immunization. ( A ) Purification of recombinant Junín virus (JUNV) GP1. JUNV GP1 containing a C-terminal Strep tag (GP1-Strep) was transiently expressed in HEK-293 cells <t>and</t> <t>purified</t> via affinity chromatography using <t>Strep-Tactin</t> resin. The eluted fractions were analyzed by Coomassie staining (left panel). Alternatively, JUNV GP1 containing a C-terminal hexahistidine (GP1-His) tag was expressed in Freestyle 293-F cells and purified via affinity chromatography using HisTrap columns. The resulting protein fraction was also analyzed by Coomassie staining (right panel). ( B ) Hepatitis B virus core-like particles (HBV-CLPs) carrying JUNV GP1 peptide loops. HBV-CLPs containing the indicated antigens (i.e., Loop 3, Loop 7, Loop 10, or a control FLAG tag) were produced in E. coli and isolated from the soluble fraction of lysates via Strep tag-mediated affinity purification. Eluates were analyzed by Coomassie staining (upper panel) and Western blot with an anti-Strep antibody (1:30,000; StrepMAB Classic-HRP; IBA Lifesciences, Göttingen, Germany; lower panel). The position of the HBV core protein is indicated. ( C ) Electron microscopic analysis of HBV-CLPs. The purified HBV-CLPs generated in ( B ) were further analyzed by electron microscopy with negative staining. The scale bar shown represents 80 nm.
Radial Chromatography, supplied by Merck & Co, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


Preparation of antigens for immunization. ( A ) Purification of recombinant Junín virus (JUNV) GP1. JUNV GP1 containing a C-terminal Strep tag (GP1-Strep) was transiently expressed in HEK-293 cells and purified via affinity chromatography using Strep-Tactin resin. The eluted fractions were analyzed by Coomassie staining (left panel). Alternatively, JUNV GP1 containing a C-terminal hexahistidine (GP1-His) tag was expressed in Freestyle 293-F cells and purified via affinity chromatography using HisTrap columns. The resulting protein fraction was also analyzed by Coomassie staining (right panel). ( B ) Hepatitis B virus core-like particles (HBV-CLPs) carrying JUNV GP1 peptide loops. HBV-CLPs containing the indicated antigens (i.e., Loop 3, Loop 7, Loop 10, or a control FLAG tag) were produced in E. coli and isolated from the soluble fraction of lysates via Strep tag-mediated affinity purification. Eluates were analyzed by Coomassie staining (upper panel) and Western blot with an anti-Strep antibody (1:30,000; StrepMAB Classic-HRP; IBA Lifesciences, Göttingen, Germany; lower panel). The position of the HBV core protein is indicated. ( C ) Electron microscopic analysis of HBV-CLPs. The purified HBV-CLPs generated in ( B ) were further analyzed by electron microscopy with negative staining. The scale bar shown represents 80 nm.

Journal: Vaccines

Article Title: Immunization with GP1 but Not Core-like Particles Displaying Isolated Receptor-Binding Epitopes Elicits Virus-Neutralizing Antibodies against Junín Virus

doi: 10.3390/vaccines10020173

Figure Lengend Snippet: Preparation of antigens for immunization. ( A ) Purification of recombinant Junín virus (JUNV) GP1. JUNV GP1 containing a C-terminal Strep tag (GP1-Strep) was transiently expressed in HEK-293 cells and purified via affinity chromatography using Strep-Tactin resin. The eluted fractions were analyzed by Coomassie staining (left panel). Alternatively, JUNV GP1 containing a C-terminal hexahistidine (GP1-His) tag was expressed in Freestyle 293-F cells and purified via affinity chromatography using HisTrap columns. The resulting protein fraction was also analyzed by Coomassie staining (right panel). ( B ) Hepatitis B virus core-like particles (HBV-CLPs) carrying JUNV GP1 peptide loops. HBV-CLPs containing the indicated antigens (i.e., Loop 3, Loop 7, Loop 10, or a control FLAG tag) were produced in E. coli and isolated from the soluble fraction of lysates via Strep tag-mediated affinity purification. Eluates were analyzed by Coomassie staining (upper panel) and Western blot with an anti-Strep antibody (1:30,000; StrepMAB Classic-HRP; IBA Lifesciences, Göttingen, Germany; lower panel). The position of the HBV core protein is indicated. ( C ) Electron microscopic analysis of HBV-CLPs. The purified HBV-CLPs generated in ( B ) were further analyzed by electron microscopy with negative staining. The scale bar shown represents 80 nm.

Article Snippet: The protein was then purified by affinity chromatography using Strep-Tactin Super-flow high-capacity slurry (IBA Lifesciences, Göttingen, Germany) following the manufacturer’s instructions.

Techniques: Purification, Recombinant, Strep-tag, Affinity Chromatography, Staining, FLAG-tag, Produced, Isolation, Affinity Purification, Western Blot, Generated, Electron Microscopy, Negative Staining