enzyme subtilisin Search Results


furin cleavage junction  (ProSci Incorporated)
90
ProSci Incorporated furin cleavage junction
FIGURE 1. Flavivirus RVPs containing N-linked glycans at E protein residue 67 infect CD209-expressing cells efficiently. A, Western blot analysis <t>of</t> <t>prM</t> and M content of RVP stocks made by transfection of replicon- containing cells with plasmids encoding the WNV structural proteins, plus pcDNA3 () or pcDNA3.1furin (). B–F, RVPs were made with expression plasmids for flavivirus structural proteins and human <t>furin</t> as in A. Serial dilutions of RVPs were used to infect K562 control cells (closed black diamonds), K562-CD209 cells (open red squares), or K562-CD209L cells (closed blue triangles). Renilla luciferase activity was measured 48 h after infec- tion.B,RVPsweremadewithexpressionplasmidsforDENVcapsidandDENVserotype1(Westpacstrain)prM-E. C–F, RVPs were made with plasmids encoding WNV capsid and wild-type or glycosylation mutant WNV prM-E constructs. Numbers above B–F indicate the locations of N-linked glycosylation sites within the E proteins used. Similar results were seen in more than four separate experiments using independent RVP preparations. The horizontal line on each graph represents the average background luciferase activity for uninfected wells.
Furin Cleavage Junction, supplied by ProSci Incorporated, 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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furin cleavage junction - by Bioz Stars, 2026-10
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subtilisin-enzyme solution (enzyrim osa)  (Bauer Handels)
90
Bauer Handels subtilisin-enzyme solution (enzyrim osa)
FIGURE 1. Flavivirus RVPs containing N-linked glycans at E protein residue 67 infect CD209-expressing cells efficiently. A, Western blot analysis <t>of</t> <t>prM</t> and M content of RVP stocks made by transfection of replicon- containing cells with plasmids encoding the WNV structural proteins, plus pcDNA3 () or pcDNA3.1furin (). B–F, RVPs were made with expression plasmids for flavivirus structural proteins and human <t>furin</t> as in A. Serial dilutions of RVPs were used to infect K562 control cells (closed black diamonds), K562-CD209 cells (open red squares), or K562-CD209L cells (closed blue triangles). Renilla luciferase activity was measured 48 h after infec- tion.B,RVPsweremadewithexpressionplasmidsforDENVcapsidandDENVserotype1(Westpacstrain)prM-E. C–F, RVPs were made with plasmids encoding WNV capsid and wild-type or glycosylation mutant WNV prM-E constructs. Numbers above B–F indicate the locations of N-linked glycosylation sites within the E proteins used. Similar results were seen in more than four separate experiments using independent RVP preparations. The horizontal line on each graph represents the average background luciferase activity for uninfected wells.
Subtilisin Enzyme Solution (Enzyrim Osa), supplied by Bauer Handels, 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
subtilisin-enzyme solution (enzyrim osa) - by Bioz Stars, 2026-10
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subtilisin  (AB Enzymes)
90
AB Enzymes subtilisin
FIGURE 1. Flavivirus RVPs containing N-linked glycans at E protein residue 67 infect CD209-expressing cells efficiently. A, Western blot analysis <t>of</t> <t>prM</t> and M content of RVP stocks made by transfection of replicon- containing cells with plasmids encoding the WNV structural proteins, plus pcDNA3 () or pcDNA3.1furin (). B–F, RVPs were made with expression plasmids for flavivirus structural proteins and human <t>furin</t> as in A. Serial dilutions of RVPs were used to infect K562 control cells (closed black diamonds), K562-CD209 cells (open red squares), or K562-CD209L cells (closed blue triangles). Renilla luciferase activity was measured 48 h after infec- tion.B,RVPsweremadewithexpressionplasmidsforDENVcapsidandDENVserotype1(Westpacstrain)prM-E. C–F, RVPs were made with plasmids encoding WNV capsid and wild-type or glycosylation mutant WNV prM-E constructs. Numbers above B–F indicate the locations of N-linked glycosylation sites within the E proteins used. Similar results were seen in more than four separate experiments using independent RVP preparations. The horizontal line on each graph represents the average background luciferase activity for uninfected wells.
Subtilisin, supplied by AB Enzymes, 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/enzyme+subtilisin/subtilisin/pm29605324-92-21-17
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subtilisin - by Bioz Stars, 2026-10
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subtilisin (ec 3.4.21.62  (AB Enzymes)
90
AB Enzymes subtilisin (ec 3.4.21.62
Composition of the food enzyme.
Subtilisin (Ec 3.4.21.62, supplied by AB Enzymes, 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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free enzyme subtilisin a  (Novozymes limited)
90
Novozymes limited free enzyme subtilisin a
Composition of the food enzyme.
Free Enzyme Subtilisin A, supplied by Novozymes limited, 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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subtilisin  (Enzyme Development Corporation)
90
Enzyme Development Corporation subtilisin
Composition of the food enzyme.
Subtilisin, supplied by Enzyme Development 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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subtilisin novo crystalline bacterial proteinase batch 56-2  (Enzyme Development Corporation)
90
Enzyme Development Corporation subtilisin novo crystalline bacterial proteinase batch 56-2
Composition of the food enzyme.
Subtilisin Novo Crystalline Bacterial Proteinase Batch 56 2, supplied by Enzyme Development 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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food enzyme subtilisin from b. licheniformis  (Novozymes limited)
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Novozymes limited food enzyme subtilisin from b. licheniformis
Composition of the food enzyme.
Food Enzyme Subtilisin From B. Licheniformis, supplied by Novozymes limited, 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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commercial subtilisin enzyme product savinase  (Novozymes limited)
90
Novozymes limited commercial subtilisin enzyme product savinase
Composition of the food enzyme.
Commercial Subtilisin Enzyme Product Savinase, supplied by Novozymes limited, 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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enzyme subtilisin alcalase  (Novozymes limited)
90
Novozymes limited enzyme subtilisin alcalase
Composition of the food enzyme.
Enzyme Subtilisin Alcalase, supplied by Novozymes limited, 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


FIGURE 1. Flavivirus RVPs containing N-linked glycans at E protein residue 67 infect CD209-expressing cells efficiently. A, Western blot analysis of prM and M content of RVP stocks made by transfection of replicon- containing cells with plasmids encoding the WNV structural proteins, plus pcDNA3 () or pcDNA3.1furin (). B–F, RVPs were made with expression plasmids for flavivirus structural proteins and human furin as in A. Serial dilutions of RVPs were used to infect K562 control cells (closed black diamonds), K562-CD209 cells (open red squares), or K562-CD209L cells (closed blue triangles). Renilla luciferase activity was measured 48 h after infec- tion.B,RVPsweremadewithexpressionplasmidsforDENVcapsidandDENVserotype1(Westpacstrain)prM-E. C–F, RVPs were made with plasmids encoding WNV capsid and wild-type or glycosylation mutant WNV prM-E constructs. Numbers above B–F indicate the locations of N-linked glycosylation sites within the E proteins used. Similar results were seen in more than four separate experiments using independent RVP preparations. The horizontal line on each graph represents the average background luciferase activity for uninfected wells.

Journal: Journal of Biological Chemistry

Article Title: The Location of Asparagine-linked Glycans on West Nile Virions Controls Their Interactions with CD209 (Dendritic Cell-specific ICAM-3 Grabbing Nonintegrin)

doi: 10.1074/jbc.m605429200

Figure Lengend Snippet: FIGURE 1. Flavivirus RVPs containing N-linked glycans at E protein residue 67 infect CD209-expressing cells efficiently. A, Western blot analysis of prM and M content of RVP stocks made by transfection of replicon- containing cells with plasmids encoding the WNV structural proteins, plus pcDNA3 () or pcDNA3.1furin (). B–F, RVPs were made with expression plasmids for flavivirus structural proteins and human furin as in A. Serial dilutions of RVPs were used to infect K562 control cells (closed black diamonds), K562-CD209 cells (open red squares), or K562-CD209L cells (closed blue triangles). Renilla luciferase activity was measured 48 h after infec- tion.B,RVPsweremadewithexpressionplasmidsforDENVcapsidandDENVserotype1(Westpacstrain)prM-E. C–F, RVPs were made with plasmids encoding WNV capsid and wild-type or glycosylation mutant WNV prM-E constructs. Numbers above B–F indicate the locations of N-linked glycosylation sites within the E proteins used. Similar results were seen in more than four separate experiments using independent RVP preparations. The horizontal line on each graph represents the average background luciferase activity for uninfected wells.

Article Snippet: Polyclonal rabbit antibodies against prM were generated by ProSci (San Diego) by immunization of rabbits with peptides spanning the following three regions in prM: the N-terminal “pr” region, the furin cleavage junction, and the C-terminal “M” region.

Techniques: Residue, Expressing, Western Blot, Transfection, Control, Luciferase, Activity Assay, Glycoproteomics, Mutagenesis, Construct

Composition of the food enzyme.

Journal: EFSA Journal

Article Title: Safety evaluation of a food enzyme containing bacillolysin and subtilisin activities from the non‐genetically modified Bacillus amyloliquefaciens strain AR ‐383

doi: 10.2903/j.efsa.2024.8779

Figure Lengend Snippet: Composition of the food enzyme.

Article Snippet: The food enzyme with two declared activities, bacillolysin (EC 3.4.24.28) and subtilisin (EC 3.4.21.62), is produced with the non‐genetically modified Bacillus amyloliquefaciens strain AR‐383 by AB Enzymes GmbH.

Techniques: Activity Assay

Journal: EFSA Journal

Article Title: Safety evaluation of a food enzyme containing bacillolysin and subtilisin activities from the non‐genetically modified Bacillus amyloliquefaciens strain AR ‐383

doi: 10.2903/j.efsa.2024.8779

Figure Lengend Snippet:

Article Snippet: The food enzyme with two declared activities, bacillolysin (EC 3.4.24.28) and subtilisin (EC 3.4.21.62), is produced with the non‐genetically modified Bacillus amyloliquefaciens strain AR‐383 by AB Enzymes GmbH.

Techniques: