peptide conjugated affi gel 102 beads Search Results


99
Bio-Rad agarose gel beads
Agarose Gel Beads, 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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Bio-Rad peptide conjugated to affi gel 102
Peptide Conjugated To Affi Gel 102, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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peptide conjugated to affi gel 102 - by Bioz Stars, 2026-08
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RAND Corporation affi liate
Affi Liate, supplied by RAND Corporation, 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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NSABP Foundation nsabp-b32 trial
Nsabp B32 Trial, supplied by NSABP Foundation, 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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Affibody affi aunrs
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90
XanTec bioanalytics affi ace2
(a) Amino acid differences of RaTG13/SARS-CoV-2 RBD and <t>affi</t> <t>ACE2/hACE2.</t> Proteins are depicted in ribbon, with the RBD/ACE2 binding interface at 8 Å in yellow and red transparent surface, respectively. Amino acid differences are depicted as spheres colored according to the distance from the binding interface: RBD and ACE2 mutations below 8 Å are in yellow and red, mutations above 8 Å in purple and cyan, respectively. (b) Identification of affi ACE2 allele associated to RaTG13. The regions of affi ACE2 mRNA covered by SRA reads from dataset SRR11085797 are depicted as yellow bars in the upper panel. Polymorphic sites and relative frequencies were generated with WebLogo . Sites not covered by SRA reads are reported in red. Amino acid identity percentage considering covered regions (in bold) or the entire deposited sequences (in brackets) are reported in the lower panel. Identical sequences were collapsed into a single representative. The full comparison of all deposited affi ACE2 sequences is reported in .
Affi Ace2, supplied by XanTec bioanalytics, 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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Average 90 stars, based on 1 article reviews
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Interacoustics AS affi nity audiometer
(a) Amino acid differences of RaTG13/SARS-CoV-2 RBD and <t>affi</t> <t>ACE2/hACE2.</t> Proteins are depicted in ribbon, with the RBD/ACE2 binding interface at 8 Å in yellow and red transparent surface, respectively. Amino acid differences are depicted as spheres colored according to the distance from the binding interface: RBD and ACE2 mutations below 8 Å are in yellow and red, mutations above 8 Å in purple and cyan, respectively. (b) Identification of affi ACE2 allele associated to RaTG13. The regions of affi ACE2 mRNA covered by SRA reads from dataset SRR11085797 are depicted as yellow bars in the upper panel. Polymorphic sites and relative frequencies were generated with WebLogo . Sites not covered by SRA reads are reported in red. Amino acid identity percentage considering covered regions (in bold) or the entire deposited sequences (in brackets) are reported in the lower panel. Identical sequences were collapsed into a single representative. The full comparison of all deposited affi ACE2 sequences is reported in .
Affi Nity Audiometer, supplied by Interacoustics AS, 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 affi gel 15
(a) Amino acid differences of RaTG13/SARS-CoV-2 RBD and <t>affi</t> <t>ACE2/hACE2.</t> Proteins are depicted in ribbon, with the RBD/ACE2 binding interface at 8 Å in yellow and red transparent surface, respectively. Amino acid differences are depicted as spheres colored according to the distance from the binding interface: RBD and ACE2 mutations below 8 Å are in yellow and red, mutations above 8 Å in purple and cyan, respectively. (b) Identification of affi ACE2 allele associated to RaTG13. The regions of affi ACE2 mRNA covered by SRA reads from dataset SRR11085797 are depicted as yellow bars in the upper panel. Polymorphic sites and relative frequencies were generated with WebLogo . Sites not covered by SRA reads are reported in red. Amino acid identity percentage considering covered regions (in bold) or the entire deposited sequences (in brackets) are reported in the lower panel. Identical sequences were collapsed into a single representative. The full comparison of all deposited affi ACE2 sequences is reported in .
Affi Gel 15, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/peptide+conjugated+affi+gel+102+beads/us07541438-348-71-98?v=Bio-Rad
Average 95 stars, based on 1 article reviews
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90
Biomol GmbH affi-t-thiosepharose
(a) Amino acid differences of RaTG13/SARS-CoV-2 RBD and <t>affi</t> <t>ACE2/hACE2.</t> Proteins are depicted in ribbon, with the RBD/ACE2 binding interface at 8 Å in yellow and red transparent surface, respectively. Amino acid differences are depicted as spheres colored according to the distance from the binding interface: RBD and ACE2 mutations below 8 Å are in yellow and red, mutations above 8 Å in purple and cyan, respectively. (b) Identification of affi ACE2 allele associated to RaTG13. The regions of affi ACE2 mRNA covered by SRA reads from dataset SRR11085797 are depicted as yellow bars in the upper panel. Polymorphic sites and relative frequencies were generated with WebLogo . Sites not covered by SRA reads are reported in red. Amino acid identity percentage considering covered regions (in bold) or the entire deposited sequences (in brackets) are reported in the lower panel. Identical sequences were collapsed into a single representative. The full comparison of all deposited affi ACE2 sequences is reported in .
Affi T Thiosepharose, supplied by Biomol GmbH, 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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Average 90 stars, based on 1 article reviews
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90
Sciomics Inc affinity-proteomics platform
(a) Amino acid differences of RaTG13/SARS-CoV-2 RBD and <t>affi</t> <t>ACE2/hACE2.</t> Proteins are depicted in ribbon, with the RBD/ACE2 binding interface at 8 Å in yellow and red transparent surface, respectively. Amino acid differences are depicted as spheres colored according to the distance from the binding interface: RBD and ACE2 mutations below 8 Å are in yellow and red, mutations above 8 Å in purple and cyan, respectively. (b) Identification of affi ACE2 allele associated to RaTG13. The regions of affi ACE2 mRNA covered by SRA reads from dataset SRR11085797 are depicted as yellow bars in the upper panel. Polymorphic sites and relative frequencies were generated with WebLogo . Sites not covered by SRA reads are reported in red. Amino acid identity percentage considering covered regions (in bold) or the entire deposited sequences (in brackets) are reported in the lower panel. Identical sequences were collapsed into a single representative. The full comparison of all deposited affi ACE2 sequences is reported in .
Affinity Proteomics Platform, supplied by Sciomics Inc, 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/peptide+conjugated+affi+gel+102+beads/10__3233_slash_tub___239003-18-6-1?v=Sciomics+Inc
Average 90 stars, based on 1 article reviews
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90
Millar Inc morb geochemical affinities
(a) Amino acid differences of RaTG13/SARS-CoV-2 RBD and <t>affi</t> <t>ACE2/hACE2.</t> Proteins are depicted in ribbon, with the RBD/ACE2 binding interface at 8 Å in yellow and red transparent surface, respectively. Amino acid differences are depicted as spheres colored according to the distance from the binding interface: RBD and ACE2 mutations below 8 Å are in yellow and red, mutations above 8 Å in purple and cyan, respectively. (b) Identification of affi ACE2 allele associated to RaTG13. The regions of affi ACE2 mRNA covered by SRA reads from dataset SRR11085797 are depicted as yellow bars in the upper panel. Polymorphic sites and relative frequencies were generated with WebLogo . Sites not covered by SRA reads are reported in red. Amino acid identity percentage considering covered regions (in bold) or the entire deposited sequences (in brackets) are reported in the lower panel. Identical sequences were collapsed into a single representative. The full comparison of all deposited affi ACE2 sequences is reported in .
Morb Geochemical Affinities, supplied by Millar Inc, 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/peptide+conjugated+affi+gel+102+beads/10__1130_slash_b31068__1-396-1-22?v=Millar+Inc
Average 90 stars, based on 1 article reviews
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BD Diagnostics affi rm vpiii
(a) Amino acid differences of RaTG13/SARS-CoV-2 RBD and <t>affi</t> <t>ACE2/hACE2.</t> Proteins are depicted in ribbon, with the RBD/ACE2 binding interface at 8 Å in yellow and red transparent surface, respectively. Amino acid differences are depicted as spheres colored according to the distance from the binding interface: RBD and ACE2 mutations below 8 Å are in yellow and red, mutations above 8 Å in purple and cyan, respectively. (b) Identification of affi ACE2 allele associated to RaTG13. The regions of affi ACE2 mRNA covered by SRA reads from dataset SRR11085797 are depicted as yellow bars in the upper panel. Polymorphic sites and relative frequencies were generated with WebLogo . Sites not covered by SRA reads are reported in red. Amino acid identity percentage considering covered regions (in bold) or the entire deposited sequences (in brackets) are reported in the lower panel. Identical sequences were collapsed into a single representative. The full comparison of all deposited affi ACE2 sequences is reported in .
Affi Rm Vpiii, supplied by BD Diagnostics, 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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Image Search Results


(a) Amino acid differences of RaTG13/SARS-CoV-2 RBD and affi ACE2/hACE2. Proteins are depicted in ribbon, with the RBD/ACE2 binding interface at 8 Å in yellow and red transparent surface, respectively. Amino acid differences are depicted as spheres colored according to the distance from the binding interface: RBD and ACE2 mutations below 8 Å are in yellow and red, mutations above 8 Å in purple and cyan, respectively. (b) Identification of affi ACE2 allele associated to RaTG13. The regions of affi ACE2 mRNA covered by SRA reads from dataset SRR11085797 are depicted as yellow bars in the upper panel. Polymorphic sites and relative frequencies were generated with WebLogo . Sites not covered by SRA reads are reported in red. Amino acid identity percentage considering covered regions (in bold) or the entire deposited sequences (in brackets) are reported in the lower panel. Identical sequences were collapsed into a single representative. The full comparison of all deposited affi ACE2 sequences is reported in .

Journal: bioRxiv

Article Title: SARS-CoV-2 Spike Affinity and Dynamics Exclude the Strict Requirement of an Intermediate Host

doi: 10.1101/2021.08.11.455960

Figure Lengend Snippet: (a) Amino acid differences of RaTG13/SARS-CoV-2 RBD and affi ACE2/hACE2. Proteins are depicted in ribbon, with the RBD/ACE2 binding interface at 8 Å in yellow and red transparent surface, respectively. Amino acid differences are depicted as spheres colored according to the distance from the binding interface: RBD and ACE2 mutations below 8 Å are in yellow and red, mutations above 8 Å in purple and cyan, respectively. (b) Identification of affi ACE2 allele associated to RaTG13. The regions of affi ACE2 mRNA covered by SRA reads from dataset SRR11085797 are depicted as yellow bars in the upper panel. Polymorphic sites and relative frequencies were generated with WebLogo . Sites not covered by SRA reads are reported in red. Amino acid identity percentage considering covered regions (in bold) or the entire deposited sequences (in brackets) are reported in the lower panel. Identical sequences were collapsed into a single representative. The full comparison of all deposited affi ACE2 sequences is reported in .

Article Snippet: hACE2 or affi ACE2 were immobilized on a CMD200M SPR chip (XanTec bioanalytics GmbH) using a mixed solution of 200 mM 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide hydrochloride (EDC) and 50 mM N-hydroxysuccinimide (NHS) in a Biacore T-200 SPR instrument (GE Healthcare), reaching 1000 response units (RU).

Techniques: Binding Assay, Generated

(a) Surface plasmon resonance measurements. Blank subtracted sensograms (black curves) of the RaTG13 and SARS-CoV-2 RBDs on immobilized hACE2 and affi ACE2. A 1:1 binding model was used for data fitting. Shown data are the mean of four replicates. (b) Structure comparison of SARS-CoV-2 (PDB ID: 6M17) and RaTG13 (reported here) RBD/hACE2 complexes. Whole structures are depicted in ribbon, hACE2, RaTG13 RBD and SARS-CoV-2 RBD are colored in shades of blue, pink and green, respectively. The side chain of RaTG13/SARS-CoV-2 mutations are reported in licorice.

Journal: bioRxiv

Article Title: SARS-CoV-2 Spike Affinity and Dynamics Exclude the Strict Requirement of an Intermediate Host

doi: 10.1101/2021.08.11.455960

Figure Lengend Snippet: (a) Surface plasmon resonance measurements. Blank subtracted sensograms (black curves) of the RaTG13 and SARS-CoV-2 RBDs on immobilized hACE2 and affi ACE2. A 1:1 binding model was used for data fitting. Shown data are the mean of four replicates. (b) Structure comparison of SARS-CoV-2 (PDB ID: 6M17) and RaTG13 (reported here) RBD/hACE2 complexes. Whole structures are depicted in ribbon, hACE2, RaTG13 RBD and SARS-CoV-2 RBD are colored in shades of blue, pink and green, respectively. The side chain of RaTG13/SARS-CoV-2 mutations are reported in licorice.

Article Snippet: hACE2 or affi ACE2 were immobilized on a CMD200M SPR chip (XanTec bioanalytics GmbH) using a mixed solution of 200 mM 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide hydrochloride (EDC) and 50 mM N-hydroxysuccinimide (NHS) in a Biacore T-200 SPR instrument (GE Healthcare), reaching 1000 response units (RU).

Techniques: SPR Assay, Binding Assay

In the upper panel is reported a representative structure of the complex after having reached the equilibrium. ACE2, RBD and spike reminder are depicted in green, red and white, respectively. In the lower panel is reported the RMSD (root mean square deviation) of the entire complex (heavy atoms only) along the 200 ns unbiased MD simulation.

Journal: bioRxiv

Article Title: SARS-CoV-2 Spike Affinity and Dynamics Exclude the Strict Requirement of an Intermediate Host

doi: 10.1101/2021.08.11.455960

Figure Lengend Snippet: In the upper panel is reported a representative structure of the complex after having reached the equilibrium. ACE2, RBD and spike reminder are depicted in green, red and white, respectively. In the lower panel is reported the RMSD (root mean square deviation) of the entire complex (heavy atoms only) along the 200 ns unbiased MD simulation.

Article Snippet: hACE2 or affi ACE2 were immobilized on a CMD200M SPR chip (XanTec bioanalytics GmbH) using a mixed solution of 200 mM 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide hydrochloride (EDC) and 50 mM N-hydroxysuccinimide (NHS) in a Biacore T-200 SPR instrument (GE Healthcare), reaching 1000 response units (RU).

Techniques:

Final frames of the SMD simulations at the target Φ angle (60° and −15°). The final Ψ angle necessary to accommodate RBDs rotation is reported for each protomer. The starting conformation is represented in transparent surface, the final conformations in ribbon. The spike protomers are colored in yellow, cyan and red, ACE2 molecules in green.

Journal: bioRxiv

Article Title: SARS-CoV-2 Spike Affinity and Dynamics Exclude the Strict Requirement of an Intermediate Host

doi: 10.1101/2021.08.11.455960

Figure Lengend Snippet: Final frames of the SMD simulations at the target Φ angle (60° and −15°). The final Ψ angle necessary to accommodate RBDs rotation is reported for each protomer. The starting conformation is represented in transparent surface, the final conformations in ribbon. The spike protomers are colored in yellow, cyan and red, ACE2 molecules in green.

Article Snippet: hACE2 or affi ACE2 were immobilized on a CMD200M SPR chip (XanTec bioanalytics GmbH) using a mixed solution of 200 mM 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide hydrochloride (EDC) and 50 mM N-hydroxysuccinimide (NHS) in a Biacore T-200 SPR instrument (GE Healthcare), reaching 1000 response units (RU).

Techniques: