atcb sham Search Results


93
ATCC prevotella denticola atcc 33185
Prevotella Denticola Atcc 33185, supplied by ATCC, 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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93
ATCC atcc 35552
Atcc 35552, supplied by ATCC, 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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95
ATCC finegoldia magna atcc 29 328
Information density values for prokaryotic genomes.
Finegoldia Magna Atcc 29 328, supplied by ATCC, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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92
ATCC ay323524
Representative bacterial species identified in bone samples of BRONJ and control
Ay323524, supplied by ATCC, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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94
ATCC p intermedia atcc 49046
Representative bacterial species identified in bone samples of BRONJ and control
P Intermedia Atcc 49046, supplied by ATCC, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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96
ATCC strains atcc 51191
Representative bacterial species identified in bone samples of BRONJ and control
Strains Atcc 51191, supplied by ATCC, 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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94
ATCC herrer christensen 1980 b variegatus shaw 1985 b tridactylus shaw 1985 e monterogeii c hoffmanni shaw 1969 endotrypanum sp
Representative bacterial species identified in bone samples of BRONJ and control
Herrer Christensen 1980 B Variegatus Shaw 1985 B Tridactylus Shaw 1985 E Monterogeii C Hoffmanni Shaw 1969 Endotrypanum Sp, supplied by ATCC, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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94
ATCC f nucleatum atcc 51190
Representative bacterial species identified in bone samples of BRONJ and control
F Nucleatum Atcc 51190, supplied by ATCC, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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96
ATCC p gingivalis
Representative bacterial species identified in bone samples of BRONJ and control
P Gingivalis, supplied by ATCC, 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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94
ATCC sars cov 2 g614 seed virus
( A ) Binding site locations of selected monoclonal antibodies and ACE2 binding site. Surface regions of the SARS-CoV-2 spike trimer in a top view targeted by eight selected antibodies on the RBD and NTD are highlighted by ellipses. Various domains of one protomer are colored (RBM in magenta, the rest of RBD in red and NTD in blue); the other two protomers in white and gray, respectively. The ACE2 binding site is marked with a yellow dashed line. ( B ) Schematic representation of antibody IgG (heavy and light chains) and FcγRI (α and γ chains) constructs, as well as a diagram for how FcγRI captures an IgG antibody on the surface of membrane based on the crystal structure PDB ID: 4W4O . ( C ) HEK293T cells with or without expressing FcγRI were decorated with eight selected monoclonal antibodies and tested for membrane fusion with the full-length <t>G614</t> S protein expressing cells in our standard cell-cell fusion assay. Cell-cell fusion led to reconstitution of α and μ fragments of β-galactosidase yielding an active enzyme and thus the fusion activity was quantified by a chemiluminescent assay. Cells only and cells expressing FcγRI with no antibody added were negative controls. ( D ) The cell-cell fusion assay was used to analyze seven polyclonal IgG antibodies purified from serum samples of vaccinated convalescent individuals reported previously .
Sars Cov 2 G614 Seed Virus, supplied by ATCC, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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99
ATCC strain baa 308 5 w83
( A ) Binding site locations of selected monoclonal antibodies and ACE2 binding site. Surface regions of the SARS-CoV-2 spike trimer in a top view targeted by eight selected antibodies on the RBD and NTD are highlighted by ellipses. Various domains of one protomer are colored (RBM in magenta, the rest of RBD in red and NTD in blue); the other two protomers in white and gray, respectively. The ACE2 binding site is marked with a yellow dashed line. ( B ) Schematic representation of antibody IgG (heavy and light chains) and FcγRI (α and γ chains) constructs, as well as a diagram for how FcγRI captures an IgG antibody on the surface of membrane based on the crystal structure PDB ID: 4W4O . ( C ) HEK293T cells with or without expressing FcγRI were decorated with eight selected monoclonal antibodies and tested for membrane fusion with the full-length <t>G614</t> S protein expressing cells in our standard cell-cell fusion assay. Cell-cell fusion led to reconstitution of α and μ fragments of β-galactosidase yielding an active enzyme and thus the fusion activity was quantified by a chemiluminescent assay. Cells only and cells expressing FcγRI with no antibody added were negative controls. ( D ) The cell-cell fusion assay was used to analyze seven polyclonal IgG antibodies purified from serum samples of vaccinated convalescent individuals reported previously .
Strain Baa 308 5 W83, supplied by ATCC, 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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d12701  (ATCC)
90
ATCC d12701
( A ) Binding site locations of selected monoclonal antibodies and ACE2 binding site. Surface regions of the SARS-CoV-2 spike trimer in a top view targeted by eight selected antibodies on the RBD and NTD are highlighted by ellipses. Various domains of one protomer are colored (RBM in magenta, the rest of RBD in red and NTD in blue); the other two protomers in white and gray, respectively. The ACE2 binding site is marked with a yellow dashed line. ( B ) Schematic representation of antibody IgG (heavy and light chains) and FcγRI (α and γ chains) constructs, as well as a diagram for how FcγRI captures an IgG antibody on the surface of membrane based on the crystal structure PDB ID: 4W4O . ( C ) HEK293T cells with or without expressing FcγRI were decorated with eight selected monoclonal antibodies and tested for membrane fusion with the full-length <t>G614</t> S protein expressing cells in our standard cell-cell fusion assay. Cell-cell fusion led to reconstitution of α and μ fragments of β-galactosidase yielding an active enzyme and thus the fusion activity was quantified by a chemiluminescent assay. Cells only and cells expressing FcγRI with no antibody added were negative controls. ( D ) The cell-cell fusion assay was used to analyze seven polyclonal IgG antibodies purified from serum samples of vaccinated convalescent individuals reported previously .
D12701, supplied by ATCC, 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


Information density values for prokaryotic genomes.

Journal: Saudi Journal of Biological Sciences

Article Title: Information theoretic perspective on genome clustering

doi: 10.1016/j.sjbs.2020.12.039

Figure Lengend Snippet: Information density values for prokaryotic genomes.

Article Snippet: Finegoldia magna ATCC 29,328 , 1,797,577 , 0.115 , 0.9791886 , 0.9750321 , 0.805 , 0.144 , 0.051 , 0.092 , 0.017 , 0.006.

Techniques:

Representative bacterial species identified in bone samples of BRONJ and control

Journal: Oral Diseases

Article Title: Molecular profiling of oral microbiota in jawbone samples of bisphosphonate‐related osteonecrosis of the jaw

doi: 10.1111/j.1601-0825.2012.01916.x

Figure Lengend Snippet: Representative bacterial species identified in bone samples of BRONJ and control

Article Snippet: Prevotella denticola (T); ATCC 35308; AY323524.

Techniques:

( A ) Binding site locations of selected monoclonal antibodies and ACE2 binding site. Surface regions of the SARS-CoV-2 spike trimer in a top view targeted by eight selected antibodies on the RBD and NTD are highlighted by ellipses. Various domains of one protomer are colored (RBM in magenta, the rest of RBD in red and NTD in blue); the other two protomers in white and gray, respectively. The ACE2 binding site is marked with a yellow dashed line. ( B ) Schematic representation of antibody IgG (heavy and light chains) and FcγRI (α and γ chains) constructs, as well as a diagram for how FcγRI captures an IgG antibody on the surface of membrane based on the crystal structure PDB ID: 4W4O . ( C ) HEK293T cells with or without expressing FcγRI were decorated with eight selected monoclonal antibodies and tested for membrane fusion with the full-length G614 S protein expressing cells in our standard cell-cell fusion assay. Cell-cell fusion led to reconstitution of α and μ fragments of β-galactosidase yielding an active enzyme and thus the fusion activity was quantified by a chemiluminescent assay. Cells only and cells expressing FcγRI with no antibody added were negative controls. ( D ) The cell-cell fusion assay was used to analyze seven polyclonal IgG antibodies purified from serum samples of vaccinated convalescent individuals reported previously .

Journal: bioRxiv

Article Title: Antibody-mediated cell entry of SARS-CoV-2

doi: 10.1101/2023.02.20.529249

Figure Lengend Snippet: ( A ) Binding site locations of selected monoclonal antibodies and ACE2 binding site. Surface regions of the SARS-CoV-2 spike trimer in a top view targeted by eight selected antibodies on the RBD and NTD are highlighted by ellipses. Various domains of one protomer are colored (RBM in magenta, the rest of RBD in red and NTD in blue); the other two protomers in white and gray, respectively. The ACE2 binding site is marked with a yellow dashed line. ( B ) Schematic representation of antibody IgG (heavy and light chains) and FcγRI (α and γ chains) constructs, as well as a diagram for how FcγRI captures an IgG antibody on the surface of membrane based on the crystal structure PDB ID: 4W4O . ( C ) HEK293T cells with or without expressing FcγRI were decorated with eight selected monoclonal antibodies and tested for membrane fusion with the full-length G614 S protein expressing cells in our standard cell-cell fusion assay. Cell-cell fusion led to reconstitution of α and μ fragments of β-galactosidase yielding an active enzyme and thus the fusion activity was quantified by a chemiluminescent assay. Cells only and cells expressing FcγRI with no antibody added were negative controls. ( D ) The cell-cell fusion assay was used to analyze seven polyclonal IgG antibodies purified from serum samples of vaccinated convalescent individuals reported previously .

Article Snippet: The SARS-CoV-2 G614 seed virus (the clinical isolate New York-PV09158/2020; ATCC #NR-53516) was obtained through BEI Resources (Manassas, VA) and amplified in TMPRSS2-E6 cells.

Techniques: Binding Assay, Bioprocessing, Construct, Membrane, Expressing, Cell-Cell Fusion Assay, Activity Assay, Purification

( A ) Schematic representation of the full-length human ACE2 and design of antibody-based expression constructs. Various segments for ACE2 include: catalytic peptidase domain, neck domain; TM, transmembrane anchor; and CT, cytoplasmic tail. Expression constructs of antibody-ACE2 chimera, the Fab heavy chain of an antibody is fused with the neck domain, TM and CT of ACE2, coexpressed with the Fab light chain. A diagram showing how Fab is presented on the cell surfaces by the ACE2 TM anchor. ( B ) HEK293T cells transfected with eight different antibody-ACE2 chimeric constructs were tested for membrane fusion with the full-length S protein (G614 or Omicron subvariant BA.2) expressing cells in the β-galactosidase-based cell-cell fusion assay. The wildtype ACE2 was a positive control; no receptor/no S a negative control. ( C ) Infection of HEK293T cells transfected with either ACE2 or various antibody-ACE2 chimeric constructs by HIV-based pseudotyped viruses using the full-length G614 and BA.1 S constructs in a single cycle. Empty vector was used as a negative control. ( D ) Virus foci in MDCK cells transfected with either ACE2 or various antibody-ACE2 chimeric constructs followed by infection of the authentic SARS-CoV-2 G614 isolate. Empty vector was used as a negative control.

Journal: bioRxiv

Article Title: Antibody-mediated cell entry of SARS-CoV-2

doi: 10.1101/2023.02.20.529249

Figure Lengend Snippet: ( A ) Schematic representation of the full-length human ACE2 and design of antibody-based expression constructs. Various segments for ACE2 include: catalytic peptidase domain, neck domain; TM, transmembrane anchor; and CT, cytoplasmic tail. Expression constructs of antibody-ACE2 chimera, the Fab heavy chain of an antibody is fused with the neck domain, TM and CT of ACE2, coexpressed with the Fab light chain. A diagram showing how Fab is presented on the cell surfaces by the ACE2 TM anchor. ( B ) HEK293T cells transfected with eight different antibody-ACE2 chimeric constructs were tested for membrane fusion with the full-length S protein (G614 or Omicron subvariant BA.2) expressing cells in the β-galactosidase-based cell-cell fusion assay. The wildtype ACE2 was a positive control; no receptor/no S a negative control. ( C ) Infection of HEK293T cells transfected with either ACE2 or various antibody-ACE2 chimeric constructs by HIV-based pseudotyped viruses using the full-length G614 and BA.1 S constructs in a single cycle. Empty vector was used as a negative control. ( D ) Virus foci in MDCK cells transfected with either ACE2 or various antibody-ACE2 chimeric constructs followed by infection of the authentic SARS-CoV-2 G614 isolate. Empty vector was used as a negative control.

Article Snippet: The SARS-CoV-2 G614 seed virus (the clinical isolate New York-PV09158/2020; ATCC #NR-53516) was obtained through BEI Resources (Manassas, VA) and amplified in TMPRSS2-E6 cells.

Techniques: Expressing, Construct, Transfection, Membrane, Cell-Cell Fusion Assay, Positive Control, Negative Control, Infection, Plasmid Preparation, Virus

( A ) Schematic representation of the membrane-bound B cell receptor (BCR) expression constructs and a diagram showing how Fab is presented on the cell surfaces by the BCR TM anchor. ( B ) HEK293T cells transfected with eight different membrane-bound BCR constructs were tested for membrane fusion with the full-length S protein (G614 or Omicron subvariant BA.2) expressing cells in the β-galactosidase-based cell-cell fusion assay. The wildtype ACE2 was a positive control and no receptor/no S a negative control. ( C ) Infection of HEK293T cells transfected with either ACE2 or various BCR constructs by HIV-based pseudotyped viruses using the full-length G614 and Omicron BA.1 S constructs in a single cycle. Empty vector was used as a negative control. ( D ) Virus foci in MDCK cells transfected with either ACE2 or various antibody-ACE2 chimeric constructs followed by infection of the authentic SARS-CoV-2 G614 isolate. Empty vector was used as a negative control.

Journal: bioRxiv

Article Title: Antibody-mediated cell entry of SARS-CoV-2

doi: 10.1101/2023.02.20.529249

Figure Lengend Snippet: ( A ) Schematic representation of the membrane-bound B cell receptor (BCR) expression constructs and a diagram showing how Fab is presented on the cell surfaces by the BCR TM anchor. ( B ) HEK293T cells transfected with eight different membrane-bound BCR constructs were tested for membrane fusion with the full-length S protein (G614 or Omicron subvariant BA.2) expressing cells in the β-galactosidase-based cell-cell fusion assay. The wildtype ACE2 was a positive control and no receptor/no S a negative control. ( C ) Infection of HEK293T cells transfected with either ACE2 or various BCR constructs by HIV-based pseudotyped viruses using the full-length G614 and Omicron BA.1 S constructs in a single cycle. Empty vector was used as a negative control. ( D ) Virus foci in MDCK cells transfected with either ACE2 or various antibody-ACE2 chimeric constructs followed by infection of the authentic SARS-CoV-2 G614 isolate. Empty vector was used as a negative control.

Article Snippet: The SARS-CoV-2 G614 seed virus (the clinical isolate New York-PV09158/2020; ATCC #NR-53516) was obtained through BEI Resources (Manassas, VA) and amplified in TMPRSS2-E6 cells.

Techniques: Membrane, Expressing, Construct, Transfection, Cell-Cell Fusion Assay, Positive Control, Negative Control, Infection, Plasmid Preparation, Virus

( A ) and ( B ) Inhibition of viral infectivity by protease inhibitors. Pseudovirus (G614 S) infection of HEK293T cells transfected with ACE2 or antibody constructs with/without TMPRSS2 were treated with either E-64d (a cathepsin L inhibitor) or Camostat (TMPRSS2 inhibitor). DMSO, organic solvent used to dissolve E-64d. ( C - E ) Antibody neutralization of pseudoviruses containing the G614 S protein was determined using IgG antibodies, C63C8, SP1-77, S2H97 and C63C7 in red; G32B6 and C12A2 in magenta; and C12C9 in blue.

Journal: bioRxiv

Article Title: Antibody-mediated cell entry of SARS-CoV-2

doi: 10.1101/2023.02.20.529249

Figure Lengend Snippet: ( A ) and ( B ) Inhibition of viral infectivity by protease inhibitors. Pseudovirus (G614 S) infection of HEK293T cells transfected with ACE2 or antibody constructs with/without TMPRSS2 were treated with either E-64d (a cathepsin L inhibitor) or Camostat (TMPRSS2 inhibitor). DMSO, organic solvent used to dissolve E-64d. ( C - E ) Antibody neutralization of pseudoviruses containing the G614 S protein was determined using IgG antibodies, C63C8, SP1-77, S2H97 and C63C7 in red; G32B6 and C12A2 in magenta; and C12C9 in blue.

Article Snippet: The SARS-CoV-2 G614 seed virus (the clinical isolate New York-PV09158/2020; ATCC #NR-53516) was obtained through BEI Resources (Manassas, VA) and amplified in TMPRSS2-E6 cells.

Techniques: Inhibition, Infection, Transfection, Construct, Solvent, Neutralization