prism software, version 8.2 Search Results


cd45 2 percp cy5 5 thermofisher  (Thermo Fisher)
94
Thermo Fisher cd45 2 percp cy5 5 thermofisher
(A) Contour plots show Cxcr5 vs. PD1 expression at d7 p.i. on gp66-specific host cells (left) and Smarta donor cells (right two plots) from <t>CD45</t> congenic WT recipients of Zbtb7bPD or control Smarta T cells. Contour plots are representative of 2 experiments totaling n=6 (Ctrl) or 7 (Zbtb7bPD) mice, summarized in graph (right). (B) Numbers of host Tfh and GC B cells in experiments shown in (A). (C, D) Adoptively transferred Smarta cells were analyzed as in (A) at d3 p.i. (C) Contour plots (top) are representative of 4 experiments; graphs (bottom) show percent and absolute numbers of Cxcr5+ cells from one representative experiment with 3 mice of each genotype. (D) Graphs show MFI of intra-cellular Nur77, and surface CD69 and PD-1 expression on Smarta cells at d3 p.i. (left) and on indicated CD4+ T cell subsets from uninfected wild-type mice as a reference (right). (E) Mixed chimeras made from either Zbtb7bAD or control (‘tester’, <t>CD45.2)</t> and wild-type CD45.1 competitor bone marrow were assessed for Tfh and GC B differentiation. Graphs show numbers of cells of tester origin (Zbtb7bAD or control as indicated): (left) total (bottom) and Cxcr5+PD-1hi Tfh (top) gp66-specific CD4+ T cells, (right) total (bottom) and Fas+GL7+IgDlo B220+ GC B (top) B cells. Data is from 2 independent experiments including a total of 5 chimera each with control or Zbtb7bAD tester marrow; ****p<0.0001, **P< 0.003, *P<0.02 (Student t-test).
Cd45 2 Percp Cy5 5 Thermofisher, supplied by Thermo Fisher, 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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Average 94 stars, based on 1 article reviews
cd45 2 percp cy5 5 thermofisher - by Bioz Stars, 2026-03
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labsolutions software  (Shimadzu Corporation)
99
Shimadzu Corporation labsolutions software
(A) Contour plots show Cxcr5 vs. PD1 expression at d7 p.i. on gp66-specific host cells (left) and Smarta donor cells (right two plots) from <t>CD45</t> congenic WT recipients of Zbtb7bPD or control Smarta T cells. Contour plots are representative of 2 experiments totaling n=6 (Ctrl) or 7 (Zbtb7bPD) mice, summarized in graph (right). (B) Numbers of host Tfh and GC B cells in experiments shown in (A). (C, D) Adoptively transferred Smarta cells were analyzed as in (A) at d3 p.i. (C) Contour plots (top) are representative of 4 experiments; graphs (bottom) show percent and absolute numbers of Cxcr5+ cells from one representative experiment with 3 mice of each genotype. (D) Graphs show MFI of intra-cellular Nur77, and surface CD69 and PD-1 expression on Smarta cells at d3 p.i. (left) and on indicated CD4+ T cell subsets from uninfected wild-type mice as a reference (right). (E) Mixed chimeras made from either Zbtb7bAD or control (‘tester’, <t>CD45.2)</t> and wild-type CD45.1 competitor bone marrow were assessed for Tfh and GC B differentiation. Graphs show numbers of cells of tester origin (Zbtb7bAD or control as indicated): (left) total (bottom) and Cxcr5+PD-1hi Tfh (top) gp66-specific CD4+ T cells, (right) total (bottom) and Fas+GL7+IgDlo B220+ GC B (top) B cells. Data is from 2 independent experiments including a total of 5 chimera each with control or Zbtb7bAD tester marrow; ****p<0.0001, **P< 0.003, *P<0.02 (Student t-test).
Labsolutions Software, supplied by Shimadzu Corporation, 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/result/labsolutions software/product/Shimadzu Corporation
Average 99 stars, based on 1 article reviews
labsolutions software - by Bioz Stars, 2026-03
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pipeline software v1.82  (Illumina Inc)
90
Illumina Inc pipeline software v1.82
(A) Contour plots show Cxcr5 vs. PD1 expression at d7 p.i. on gp66-specific host cells (left) and Smarta donor cells (right two plots) from <t>CD45</t> congenic WT recipients of Zbtb7bPD or control Smarta T cells. Contour plots are representative of 2 experiments totaling n=6 (Ctrl) or 7 (Zbtb7bPD) mice, summarized in graph (right). (B) Numbers of host Tfh and GC B cells in experiments shown in (A). (C, D) Adoptively transferred Smarta cells were analyzed as in (A) at d3 p.i. (C) Contour plots (top) are representative of 4 experiments; graphs (bottom) show percent and absolute numbers of Cxcr5+ cells from one representative experiment with 3 mice of each genotype. (D) Graphs show MFI of intra-cellular Nur77, and surface CD69 and PD-1 expression on Smarta cells at d3 p.i. (left) and on indicated CD4+ T cell subsets from uninfected wild-type mice as a reference (right). (E) Mixed chimeras made from either Zbtb7bAD or control (‘tester’, <t>CD45.2)</t> and wild-type CD45.1 competitor bone marrow were assessed for Tfh and GC B differentiation. Graphs show numbers of cells of tester origin (Zbtb7bAD or control as indicated): (left) total (bottom) and Cxcr5+PD-1hi Tfh (top) gp66-specific CD4+ T cells, (right) total (bottom) and Fas+GL7+IgDlo B220+ GC B (top) B cells. Data is from 2 independent experiments including a total of 5 chimera each with control or Zbtb7bAD tester marrow; ****p<0.0001, **P< 0.003, *P<0.02 (Student t-test).
Pipeline Software V1.82, supplied by Illumina 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/result/pipeline software v1.82/product/Illumina Inc
Average 90 stars, based on 1 article reviews
pipeline software v1.82 - by Bioz Stars, 2026-03
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pipeline software version 1.82  (Illumina Inc)
90
Illumina Inc pipeline software version 1.82
(A) Contour plots show Cxcr5 vs. PD1 expression at d7 p.i. on gp66-specific host cells (left) and Smarta donor cells (right two plots) from <t>CD45</t> congenic WT recipients of Zbtb7bPD or control Smarta T cells. Contour plots are representative of 2 experiments totaling n=6 (Ctrl) or 7 (Zbtb7bPD) mice, summarized in graph (right). (B) Numbers of host Tfh and GC B cells in experiments shown in (A). (C, D) Adoptively transferred Smarta cells were analyzed as in (A) at d3 p.i. (C) Contour plots (top) are representative of 4 experiments; graphs (bottom) show percent and absolute numbers of Cxcr5+ cells from one representative experiment with 3 mice of each genotype. (D) Graphs show MFI of intra-cellular Nur77, and surface CD69 and PD-1 expression on Smarta cells at d3 p.i. (left) and on indicated CD4+ T cell subsets from uninfected wild-type mice as a reference (right). (E) Mixed chimeras made from either Zbtb7bAD or control (‘tester’, <t>CD45.2)</t> and wild-type CD45.1 competitor bone marrow were assessed for Tfh and GC B differentiation. Graphs show numbers of cells of tester origin (Zbtb7bAD or control as indicated): (left) total (bottom) and Cxcr5+PD-1hi Tfh (top) gp66-specific CD4+ T cells, (right) total (bottom) and Fas+GL7+IgDlo B220+ GC B (top) B cells. Data is from 2 independent experiments including a total of 5 chimera each with control or Zbtb7bAD tester marrow; ****p<0.0001, **P< 0.003, *P<0.02 (Student t-test).
Pipeline Software Version 1.82, supplied by Illumina 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/result/pipeline software version 1.82/product/Illumina Inc
Average 90 stars, based on 1 article reviews
pipeline software version 1.82 - by Bioz Stars, 2026-03
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image analysis software lucia image v.4.82  (Nikon)
90
Nikon image analysis software lucia image v.4.82
(A) Contour plots show Cxcr5 vs. PD1 expression at d7 p.i. on gp66-specific host cells (left) and Smarta donor cells (right two plots) from <t>CD45</t> congenic WT recipients of Zbtb7bPD or control Smarta T cells. Contour plots are representative of 2 experiments totaling n=6 (Ctrl) or 7 (Zbtb7bPD) mice, summarized in graph (right). (B) Numbers of host Tfh and GC B cells in experiments shown in (A). (C, D) Adoptively transferred Smarta cells were analyzed as in (A) at d3 p.i. (C) Contour plots (top) are representative of 4 experiments; graphs (bottom) show percent and absolute numbers of Cxcr5+ cells from one representative experiment with 3 mice of each genotype. (D) Graphs show MFI of intra-cellular Nur77, and surface CD69 and PD-1 expression on Smarta cells at d3 p.i. (left) and on indicated CD4+ T cell subsets from uninfected wild-type mice as a reference (right). (E) Mixed chimeras made from either Zbtb7bAD or control (‘tester’, <t>CD45.2)</t> and wild-type CD45.1 competitor bone marrow were assessed for Tfh and GC B differentiation. Graphs show numbers of cells of tester origin (Zbtb7bAD or control as indicated): (left) total (bottom) and Cxcr5+PD-1hi Tfh (top) gp66-specific CD4+ T cells, (right) total (bottom) and Fas+GL7+IgDlo B220+ GC B (top) B cells. Data is from 2 independent experiments including a total of 5 chimera each with control or Zbtb7bAD tester marrow; ****p<0.0001, **P< 0.003, *P<0.02 (Student t-test).
Image Analysis Software Lucia Image V.4.82, supplied by Nikon, 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/result/image analysis software lucia image v.4.82/product/Nikon
Average 90 stars, based on 1 article reviews
image analysis software lucia image v.4.82 - by Bioz Stars, 2026-03
90/100 stars
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lucia g software (version 4.82  (Nikon)
90
Nikon lucia g software (version 4.82
(A) Contour plots show Cxcr5 vs. PD1 expression at d7 p.i. on gp66-specific host cells (left) and Smarta donor cells (right two plots) from <t>CD45</t> congenic WT recipients of Zbtb7bPD or control Smarta T cells. Contour plots are representative of 2 experiments totaling n=6 (Ctrl) or 7 (Zbtb7bPD) mice, summarized in graph (right). (B) Numbers of host Tfh and GC B cells in experiments shown in (A). (C, D) Adoptively transferred Smarta cells were analyzed as in (A) at d3 p.i. (C) Contour plots (top) are representative of 4 experiments; graphs (bottom) show percent and absolute numbers of Cxcr5+ cells from one representative experiment with 3 mice of each genotype. (D) Graphs show MFI of intra-cellular Nur77, and surface CD69 and PD-1 expression on Smarta cells at d3 p.i. (left) and on indicated CD4+ T cell subsets from uninfected wild-type mice as a reference (right). (E) Mixed chimeras made from either Zbtb7bAD or control (‘tester’, <t>CD45.2)</t> and wild-type CD45.1 competitor bone marrow were assessed for Tfh and GC B differentiation. Graphs show numbers of cells of tester origin (Zbtb7bAD or control as indicated): (left) total (bottom) and Cxcr5+PD-1hi Tfh (top) gp66-specific CD4+ T cells, (right) total (bottom) and Fas+GL7+IgDlo B220+ GC B (top) B cells. Data is from 2 independent experiments including a total of 5 chimera each with control or Zbtb7bAD tester marrow; ****p<0.0001, **P< 0.003, *P<0.02 (Student t-test).
Lucia G Software (Version 4.82, supplied by Nikon, 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/result/lucia g software (version 4.82/product/Nikon
Average 90 stars, based on 1 article reviews
lucia g software (version 4.82 - by Bioz Stars, 2026-03
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power injector injektron® 82 mrt  (MEDTRON Software Intelligence Corporation)
90
MEDTRON Software Intelligence Corporation power injector injektron® 82 mrt
(A) Contour plots show Cxcr5 vs. PD1 expression at d7 p.i. on gp66-specific host cells (left) and Smarta donor cells (right two plots) from <t>CD45</t> congenic WT recipients of Zbtb7bPD or control Smarta T cells. Contour plots are representative of 2 experiments totaling n=6 (Ctrl) or 7 (Zbtb7bPD) mice, summarized in graph (right). (B) Numbers of host Tfh and GC B cells in experiments shown in (A). (C, D) Adoptively transferred Smarta cells were analyzed as in (A) at d3 p.i. (C) Contour plots (top) are representative of 4 experiments; graphs (bottom) show percent and absolute numbers of Cxcr5+ cells from one representative experiment with 3 mice of each genotype. (D) Graphs show MFI of intra-cellular Nur77, and surface CD69 and PD-1 expression on Smarta cells at d3 p.i. (left) and on indicated CD4+ T cell subsets from uninfected wild-type mice as a reference (right). (E) Mixed chimeras made from either Zbtb7bAD or control (‘tester’, <t>CD45.2)</t> and wild-type CD45.1 competitor bone marrow were assessed for Tfh and GC B differentiation. Graphs show numbers of cells of tester origin (Zbtb7bAD or control as indicated): (left) total (bottom) and Cxcr5+PD-1hi Tfh (top) gp66-specific CD4+ T cells, (right) total (bottom) and Fas+GL7+IgDlo B220+ GC B (top) B cells. Data is from 2 independent experiments including a total of 5 chimera each with control or Zbtb7bAD tester marrow; ****p<0.0001, **P< 0.003, *P<0.02 (Student t-test).
Power Injector Injektron® 82 Mrt, supplied by MEDTRON Software Intelligence Corporation, 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/result/power injector injektron® 82 mrt/product/MEDTRON Software Intelligence Corporation
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power injector injektron® 82 mrt - by Bioz Stars, 2026-03
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casava software v1.82.2  (Illumina Inc)
90
Illumina Inc casava software v1.82.2
(A) Contour plots show Cxcr5 vs. PD1 expression at d7 p.i. on gp66-specific host cells (left) and Smarta donor cells (right two plots) from <t>CD45</t> congenic WT recipients of Zbtb7bPD or control Smarta T cells. Contour plots are representative of 2 experiments totaling n=6 (Ctrl) or 7 (Zbtb7bPD) mice, summarized in graph (right). (B) Numbers of host Tfh and GC B cells in experiments shown in (A). (C, D) Adoptively transferred Smarta cells were analyzed as in (A) at d3 p.i. (C) Contour plots (top) are representative of 4 experiments; graphs (bottom) show percent and absolute numbers of Cxcr5+ cells from one representative experiment with 3 mice of each genotype. (D) Graphs show MFI of intra-cellular Nur77, and surface CD69 and PD-1 expression on Smarta cells at d3 p.i. (left) and on indicated CD4+ T cell subsets from uninfected wild-type mice as a reference (right). (E) Mixed chimeras made from either Zbtb7bAD or control (‘tester’, <t>CD45.2)</t> and wild-type CD45.1 competitor bone marrow were assessed for Tfh and GC B differentiation. Graphs show numbers of cells of tester origin (Zbtb7bAD or control as indicated): (left) total (bottom) and Cxcr5+PD-1hi Tfh (top) gp66-specific CD4+ T cells, (right) total (bottom) and Fas+GL7+IgDlo B220+ GC B (top) B cells. Data is from 2 independent experiments including a total of 5 chimera each with control or Zbtb7bAD tester marrow; ****p<0.0001, **P< 0.003, *P<0.02 (Student t-test).
Casava Software V1.82.2, supplied by Illumina 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/result/casava software v1.82.2/product/Illumina Inc
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casava software v1.82.2 - by Bioz Stars, 2026-03
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n ε acetyl l lysine  (Chem Impex International)
95
Chem Impex International n ε acetyl l lysine
( A ) SDS-PAGE analysis of proteins used in this study. All proteins were expressed and purified as GST-fusion proteins. In terms of YcgC and YcgC S200A the GST-tag was removed by TEV protease during the purification steps. Staining of the gel was done by coomassie brilliant blue (CBB). For molecular masses see figure legend for . ( B ) Analytical size exclusion chromatography on a S200 10/300 GL column shows that YcgC WT and YcgC S200A as well as CobB and the corresponding catalytically inactive variant CobB H110Y display an almost identical elution profile. Moreover, RutR proteins show a nearly identical elution profile in analytical SEC runs indicating that RutR acetylation at K52 and K62 does not interfere with protein folding or its oligomeric state. ( C ) RutR-His 6 AcK52 and AcK62 are quantitatively acetylated. Shown are SDS-PAGE and immunoblot analyses of all RutR-His 6 proteins used in this study. Staining for AcK using an <t>anti-acetyl-L-lysine</t> antibody revealed a strong signal for RutR AcK52 and AcK62, whereas no signal was obtained for RutR WT. As loading control anti-His 6 staining was performed. ( D ) ESI-MS data show the quantitative and homogenous incorporation of acetyl-L-lysine into RutR. Shown is the deconvoluted spectrum on the true mass scale after software transformation yielding one single peak and the corresponding molecular mass as indicated. Expected mass non-acetylated RutR: 24567.5 Da; acetylated RutR: 24609.5 Da.
N ε Acetyl L Lysine, supplied by Chem Impex International, 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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n ε acetyl l lysine - by Bioz Stars, 2026-03
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sas® studio software  (SAS institute)
90
SAS institute sas® studio software
( A ) SDS-PAGE analysis of proteins used in this study. All proteins were expressed and purified as GST-fusion proteins. In terms of YcgC and YcgC S200A the GST-tag was removed by TEV protease during the purification steps. Staining of the gel was done by coomassie brilliant blue (CBB). For molecular masses see figure legend for . ( B ) Analytical size exclusion chromatography on a S200 10/300 GL column shows that YcgC WT and YcgC S200A as well as CobB and the corresponding catalytically inactive variant CobB H110Y display an almost identical elution profile. Moreover, RutR proteins show a nearly identical elution profile in analytical SEC runs indicating that RutR acetylation at K52 and K62 does not interfere with protein folding or its oligomeric state. ( C ) RutR-His 6 AcK52 and AcK62 are quantitatively acetylated. Shown are SDS-PAGE and immunoblot analyses of all RutR-His 6 proteins used in this study. Staining for AcK using an <t>anti-acetyl-L-lysine</t> antibody revealed a strong signal for RutR AcK52 and AcK62, whereas no signal was obtained for RutR WT. As loading control anti-His 6 staining was performed. ( D ) ESI-MS data show the quantitative and homogenous incorporation of acetyl-L-lysine into RutR. Shown is the deconvoluted spectrum on the true mass scale after software transformation yielding one single peak and the corresponding molecular mass as indicated. Expected mass non-acetylated RutR: 24567.5 Da; acetylated RutR: 24609.5 Da.
Sas® Studio Software, supplied by SAS institute, 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/result/sas® studio software/product/SAS institute
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sas® studio software - by Bioz Stars, 2026-03
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on demand for academics software  (SAS institute)
90
SAS institute on demand for academics software
( A ) SDS-PAGE analysis of proteins used in this study. All proteins were expressed and purified as GST-fusion proteins. In terms of YcgC and YcgC S200A the GST-tag was removed by TEV protease during the purification steps. Staining of the gel was done by coomassie brilliant blue (CBB). For molecular masses see figure legend for . ( B ) Analytical size exclusion chromatography on a S200 10/300 GL column shows that YcgC WT and YcgC S200A as well as CobB and the corresponding catalytically inactive variant CobB H110Y display an almost identical elution profile. Moreover, RutR proteins show a nearly identical elution profile in analytical SEC runs indicating that RutR acetylation at K52 and K62 does not interfere with protein folding or its oligomeric state. ( C ) RutR-His 6 AcK52 and AcK62 are quantitatively acetylated. Shown are SDS-PAGE and immunoblot analyses of all RutR-His 6 proteins used in this study. Staining for AcK using an <t>anti-acetyl-L-lysine</t> antibody revealed a strong signal for RutR AcK52 and AcK62, whereas no signal was obtained for RutR WT. As loading control anti-His 6 staining was performed. ( D ) ESI-MS data show the quantitative and homogenous incorporation of acetyl-L-lysine into RutR. Shown is the deconvoluted spectrum on the true mass scale after software transformation yielding one single peak and the corresponding molecular mass as indicated. Expected mass non-acetylated RutR: 24567.5 Da; acetylated RutR: 24609.5 Da.
On Demand For Academics Software, supplied by SAS institute, 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/result/on demand for academics software/product/SAS institute
Average 90 stars, based on 1 article reviews
on demand for academics software - by Bioz Stars, 2026-03
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version 9 0  (STATA Corporation)
96
STATA Corporation version 9 0
( A ) SDS-PAGE analysis of proteins used in this study. All proteins were expressed and purified as GST-fusion proteins. In terms of YcgC and YcgC S200A the GST-tag was removed by TEV protease during the purification steps. Staining of the gel was done by coomassie brilliant blue (CBB). For molecular masses see figure legend for . ( B ) Analytical size exclusion chromatography on a S200 10/300 GL column shows that YcgC WT and YcgC S200A as well as CobB and the corresponding catalytically inactive variant CobB H110Y display an almost identical elution profile. Moreover, RutR proteins show a nearly identical elution profile in analytical SEC runs indicating that RutR acetylation at K52 and K62 does not interfere with protein folding or its oligomeric state. ( C ) RutR-His 6 AcK52 and AcK62 are quantitatively acetylated. Shown are SDS-PAGE and immunoblot analyses of all RutR-His 6 proteins used in this study. Staining for AcK using an <t>anti-acetyl-L-lysine</t> antibody revealed a strong signal for RutR AcK52 and AcK62, whereas no signal was obtained for RutR WT. As loading control anti-His 6 staining was performed. ( D ) ESI-MS data show the quantitative and homogenous incorporation of acetyl-L-lysine into RutR. Shown is the deconvoluted spectrum on the true mass scale after software transformation yielding one single peak and the corresponding molecular mass as indicated. Expected mass non-acetylated RutR: 24567.5 Da; acetylated RutR: 24609.5 Da.
Version 9 0, supplied by STATA Corporation, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/version 9 0/product/STATA Corporation
Average 96 stars, based on 1 article reviews
version 9 0 - by Bioz Stars, 2026-03
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Image Search Results


(A) Contour plots show Cxcr5 vs. PD1 expression at d7 p.i. on gp66-specific host cells (left) and Smarta donor cells (right two plots) from CD45 congenic WT recipients of Zbtb7bPD or control Smarta T cells. Contour plots are representative of 2 experiments totaling n=6 (Ctrl) or 7 (Zbtb7bPD) mice, summarized in graph (right). (B) Numbers of host Tfh and GC B cells in experiments shown in (A). (C, D) Adoptively transferred Smarta cells were analyzed as in (A) at d3 p.i. (C) Contour plots (top) are representative of 4 experiments; graphs (bottom) show percent and absolute numbers of Cxcr5+ cells from one representative experiment with 3 mice of each genotype. (D) Graphs show MFI of intra-cellular Nur77, and surface CD69 and PD-1 expression on Smarta cells at d3 p.i. (left) and on indicated CD4+ T cell subsets from uninfected wild-type mice as a reference (right). (E) Mixed chimeras made from either Zbtb7bAD or control (‘tester’, CD45.2) and wild-type CD45.1 competitor bone marrow were assessed for Tfh and GC B differentiation. Graphs show numbers of cells of tester origin (Zbtb7bAD or control as indicated): (left) total (bottom) and Cxcr5+PD-1hi Tfh (top) gp66-specific CD4+ T cells, (right) total (bottom) and Fas+GL7+IgDlo B220+ GC B (top) B cells. Data is from 2 independent experiments including a total of 5 chimera each with control or Zbtb7bAD tester marrow; ****p<0.0001, **P< 0.003, *P<0.02 (Student t-test).

Journal: Immunity

Article Title: A Thpok-directed transcriptional circuitry promotes Bcl6 and Maf to orchestrate T follicular helper differentiation.

doi: 10.1016/j.immuni.2019.06.023

Figure Lengend Snippet: (A) Contour plots show Cxcr5 vs. PD1 expression at d7 p.i. on gp66-specific host cells (left) and Smarta donor cells (right two plots) from CD45 congenic WT recipients of Zbtb7bPD or control Smarta T cells. Contour plots are representative of 2 experiments totaling n=6 (Ctrl) or 7 (Zbtb7bPD) mice, summarized in graph (right). (B) Numbers of host Tfh and GC B cells in experiments shown in (A). (C, D) Adoptively transferred Smarta cells were analyzed as in (A) at d3 p.i. (C) Contour plots (top) are representative of 4 experiments; graphs (bottom) show percent and absolute numbers of Cxcr5+ cells from one representative experiment with 3 mice of each genotype. (D) Graphs show MFI of intra-cellular Nur77, and surface CD69 and PD-1 expression on Smarta cells at d3 p.i. (left) and on indicated CD4+ T cell subsets from uninfected wild-type mice as a reference (right). (E) Mixed chimeras made from either Zbtb7bAD or control (‘tester’, CD45.2) and wild-type CD45.1 competitor bone marrow were assessed for Tfh and GC B differentiation. Graphs show numbers of cells of tester origin (Zbtb7bAD or control as indicated): (left) total (bottom) and Cxcr5+PD-1hi Tfh (top) gp66-specific CD4+ T cells, (right) total (bottom) and Fas+GL7+IgDlo B220+ GC B (top) B cells. Data is from 2 independent experiments including a total of 5 chimera each with control or Zbtb7bAD tester marrow; ****p<0.0001, **P< 0.003, *P<0.02 (Student t-test).

Article Snippet: ​ REAGENT or RESOURCE SOURCE IDENTIFIER Antibodies Anti-B220-V500 (Clone RA3-6B2) BD Pharmigen Cat# 561227, RRID:AB_10562193 Anti-CXCR5-PE-eFluor 610 (Clone SPRCL5) Thermofisher Cat# 61-7185-82, RRID:AB_2574660 Anti-Thpok-AF647 (Clone T43-94) BD Pharmigen Cat# 565500, RRID:AB_273926 Anti-CD4-BV786 BD Pharmigen Cat# 563727, RRID:AB_2728707 Anti-CD4-PE Thermofisher Cat# 12-0043-85, RRID:AB_465516 Anti-CD40L-PE Thermofisher Cat# 17-1541-82, RRID:AB_795823 Anti-TCRb-e450 Thermofisher Cat# 48-5961-82, RRID:AB_11039532 Anti-Thy1.1-PECy7 Thermofisher Cat# 25-0900-82, RRID:AB_469640 Anti-Thy1.1-e450 Thermofisher Cat# 561406, RRID:AB_10680271 Anti-CD44-e450 Thermofisher Cat# 48-0441-82, RRID:AB_1272246 Anti-CD44-AF700 Thermofisher Cat# 56-0441-82, RRID:AB_494011 Anti-PD-1-PECy7 Thermofisher Cat# 25-9985-82, RRID:AB_10853805 Anti-GL7-e450 Thermofisher Cat# 48-5902-80, RRID:AB_10854881 Anti-IgD-APC Thermofisher Cat# 17-5993-80, RRID:AB_10598656 Anti-Fas-PE Thermofisher Cat# 554258, RRID:AB_395330 Anti-Bcl6-PE Thermofisher Cat# 561522, RRID:AB_10717126 Anti TCF-1 Cell Signaling Technologies Cat# 2203, RRID:AB_2199302 Goat-Anti Rabbit IgG F(ab’)2 Jackson Immunoresearch Laboratories Cat# 111-136-144, RRID:AB_2337987 Anti-CD4-APC-e780 Thermofisher Cat# 47-0042-82, RRID:AB_1272183 Anti-CD8a PerCP-CY5.5 Thermofisher Cat# 45-0081-82, RRID:AB_1107004 Anti-CD45.1-AF780 Thermofisher Cat# 47-0453-82, RRID:AB_1582228 Anti-CD45.2-PerCP-Cy5.5 Thermofisher Cat# 45-0454-82, RRID:AB_953590 Anti-Nur77-PE Thermofisher Cat# 12-5965-80, RRID:AB_1257210 Anti-CD69-PE Thermofisher Cat# 12-0691-82, RRID:AB_465732 Anti-CD45.2- V500 Thermofisher Cat# 562129, RRID:AB_10897142 Anti-CD45.2- BV786 Thermofisher Cat# 563686, RRID:AB_2738375 Anti-IgD-AF647 Biolegend Cat# 405708, RRID:AB_893528 goat anti-IgG-HRP Southern Biotech Cat# 1031-05, RRID:AB_2794307 anti-CD3 (2C11) BioXcell Cat# BE0001-1, RRID:AB_1107634 anti-CD28 (37.51) BioXcell Cat# BE0015-1, RRID:AB_1107624 Bacterial and Virus Strains LCMV Armstrong McGavern Lab Generated in house Biological Samples Toxoplasma gondii M.E.

Techniques: Expressing

KEY RESOURCES TABLE

Journal: Immunity

Article Title: A Thpok-directed transcriptional circuitry promotes Bcl6 and Maf to orchestrate T follicular helper differentiation.

doi: 10.1016/j.immuni.2019.06.023

Figure Lengend Snippet: KEY RESOURCES TABLE

Article Snippet: ​ REAGENT or RESOURCE SOURCE IDENTIFIER Antibodies Anti-B220-V500 (Clone RA3-6B2) BD Pharmigen Cat# 561227, RRID:AB_10562193 Anti-CXCR5-PE-eFluor 610 (Clone SPRCL5) Thermofisher Cat# 61-7185-82, RRID:AB_2574660 Anti-Thpok-AF647 (Clone T43-94) BD Pharmigen Cat# 565500, RRID:AB_273926 Anti-CD4-BV786 BD Pharmigen Cat# 563727, RRID:AB_2728707 Anti-CD4-PE Thermofisher Cat# 12-0043-85, RRID:AB_465516 Anti-CD40L-PE Thermofisher Cat# 17-1541-82, RRID:AB_795823 Anti-TCRb-e450 Thermofisher Cat# 48-5961-82, RRID:AB_11039532 Anti-Thy1.1-PECy7 Thermofisher Cat# 25-0900-82, RRID:AB_469640 Anti-Thy1.1-e450 Thermofisher Cat# 561406, RRID:AB_10680271 Anti-CD44-e450 Thermofisher Cat# 48-0441-82, RRID:AB_1272246 Anti-CD44-AF700 Thermofisher Cat# 56-0441-82, RRID:AB_494011 Anti-PD-1-PECy7 Thermofisher Cat# 25-9985-82, RRID:AB_10853805 Anti-GL7-e450 Thermofisher Cat# 48-5902-80, RRID:AB_10854881 Anti-IgD-APC Thermofisher Cat# 17-5993-80, RRID:AB_10598656 Anti-Fas-PE Thermofisher Cat# 554258, RRID:AB_395330 Anti-Bcl6-PE Thermofisher Cat# 561522, RRID:AB_10717126 Anti TCF-1 Cell Signaling Technologies Cat# 2203, RRID:AB_2199302 Goat-Anti Rabbit IgG F(ab’)2 Jackson Immunoresearch Laboratories Cat# 111-136-144, RRID:AB_2337987 Anti-CD4-APC-e780 Thermofisher Cat# 47-0042-82, RRID:AB_1272183 Anti-CD8a PerCP-CY5.5 Thermofisher Cat# 45-0081-82, RRID:AB_1107004 Anti-CD45.1-AF780 Thermofisher Cat# 47-0453-82, RRID:AB_1582228 Anti-CD45.2-PerCP-Cy5.5 Thermofisher Cat# 45-0454-82, RRID:AB_953590 Anti-Nur77-PE Thermofisher Cat# 12-5965-80, RRID:AB_1257210 Anti-CD69-PE Thermofisher Cat# 12-0691-82, RRID:AB_465732 Anti-CD45.2- V500 Thermofisher Cat# 562129, RRID:AB_10897142 Anti-CD45.2- BV786 Thermofisher Cat# 563686, RRID:AB_2738375 Anti-IgD-AF647 Biolegend Cat# 405708, RRID:AB_893528 goat anti-IgG-HRP Southern Biotech Cat# 1031-05, RRID:AB_2794307 anti-CD3 (2C11) BioXcell Cat# BE0001-1, RRID:AB_1107634 anti-CD28 (37.51) BioXcell Cat# BE0015-1, RRID:AB_1107624 Bacterial and Virus Strains LCMV Armstrong McGavern Lab Generated in house Biological Samples Toxoplasma gondii M.E.

Techniques: Generated, Recombinant, Purification, Staining, Plasmid Preparation, Reporter Assay, Expressing, Transduction, Transgenic Assay, Software

( A ) SDS-PAGE analysis of proteins used in this study. All proteins were expressed and purified as GST-fusion proteins. In terms of YcgC and YcgC S200A the GST-tag was removed by TEV protease during the purification steps. Staining of the gel was done by coomassie brilliant blue (CBB). For molecular masses see figure legend for . ( B ) Analytical size exclusion chromatography on a S200 10/300 GL column shows that YcgC WT and YcgC S200A as well as CobB and the corresponding catalytically inactive variant CobB H110Y display an almost identical elution profile. Moreover, RutR proteins show a nearly identical elution profile in analytical SEC runs indicating that RutR acetylation at K52 and K62 does not interfere with protein folding or its oligomeric state. ( C ) RutR-His 6 AcK52 and AcK62 are quantitatively acetylated. Shown are SDS-PAGE and immunoblot analyses of all RutR-His 6 proteins used in this study. Staining for AcK using an anti-acetyl-L-lysine antibody revealed a strong signal for RutR AcK52 and AcK62, whereas no signal was obtained for RutR WT. As loading control anti-His 6 staining was performed. ( D ) ESI-MS data show the quantitative and homogenous incorporation of acetyl-L-lysine into RutR. Shown is the deconvoluted spectrum on the true mass scale after software transformation yielding one single peak and the corresponding molecular mass as indicated. Expected mass non-acetylated RutR: 24567.5 Da; acetylated RutR: 24609.5 Da.

Journal: eLife

Article Title: Comment on ‘YcgC represents a new protein deacetylase family in prokaryotes’

doi: 10.7554/eLife.37798

Figure Lengend Snippet: ( A ) SDS-PAGE analysis of proteins used in this study. All proteins were expressed and purified as GST-fusion proteins. In terms of YcgC and YcgC S200A the GST-tag was removed by TEV protease during the purification steps. Staining of the gel was done by coomassie brilliant blue (CBB). For molecular masses see figure legend for . ( B ) Analytical size exclusion chromatography on a S200 10/300 GL column shows that YcgC WT and YcgC S200A as well as CobB and the corresponding catalytically inactive variant CobB H110Y display an almost identical elution profile. Moreover, RutR proteins show a nearly identical elution profile in analytical SEC runs indicating that RutR acetylation at K52 and K62 does not interfere with protein folding or its oligomeric state. ( C ) RutR-His 6 AcK52 and AcK62 are quantitatively acetylated. Shown are SDS-PAGE and immunoblot analyses of all RutR-His 6 proteins used in this study. Staining for AcK using an anti-acetyl-L-lysine antibody revealed a strong signal for RutR AcK52 and AcK62, whereas no signal was obtained for RutR WT. As loading control anti-His 6 staining was performed. ( D ) ESI-MS data show the quantitative and homogenous incorporation of acetyl-L-lysine into RutR. Shown is the deconvoluted spectrum on the true mass scale after software transformation yielding one single peak and the corresponding molecular mass as indicated. Expected mass non-acetylated RutR: 24567.5 Da; acetylated RutR: 24609.5 Da.

Article Snippet: After addition of 10 mM N-(ε)-acetyl-L-lysine (Chem-Impex International Inc.) and 20 mM nicotinamide (NAM) cells were grown for further 30 min before protein expression was induced by adding 300 µM IPTG.

Techniques: SDS Page, Purification, Staining, Size-exclusion Chromatography, Variant Assay, Western Blot, Software, Transformation Assay