equations 10 imputations mice using the stata command mi impute chained Search Results


mic  (New England Biolabs)
99
New England Biolabs mic
The square-shaped interaction patterns in <t>the</t> <t>MAC</t> of T. thermophila are chromosome territories. ( A ) Heatmaps showing the chromosome interactions on the 568 MAC scaffolds (ordered by their locations on the <t>MIC</t> genome) at 3 hpm (whole cells Hi-C data mapped to the MAC scaffolds), and the chromosome interactions of the 83 MAC scaffolds located on the MIC Chromosome 2 at 1.5 hpm, 3 hpm, and 24 hpm. Zoomed-in views of scf_8254803 are shown at the bottom . (hpm) Hours post-mixing. Numbers at the lower left of heatmaps correspond to the maximum signal in the matrix. ( B , C ) The MAC chromosomes (MAC scaffolds with telomere sequences at both ends) and the MAC scaffolds compared to the chromosome interactions on MIC Chromosome 1 at 3 hpm are shown (whole cells Hi-C data mapped to the MIC genome). Regions from 1 Mb to 36.32 Mb ( B ); zoomed in region from 4 Mb to 14 Mb ( C ).
Mic, supplied by New England Biolabs, 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/product/equations+10+imputations+mice+using+the+stata+command+mi+impute+chained/NEBuffer+2/pmc07111529-119-16-34
Average 99 stars, based on 1 article reviews
mic - by Bioz Stars, 2026-09
99/100 stars
  Buy from Supplier
titanium dioxide coated mica pigment  (DIC Corporation)
90
DIC Corporation titanium dioxide coated mica pigment
The square-shaped interaction patterns in <t>the</t> <t>MAC</t> of T. thermophila are chromosome territories. ( A ) Heatmaps showing the chromosome interactions on the 568 MAC scaffolds (ordered by their locations on the <t>MIC</t> genome) at 3 hpm (whole cells Hi-C data mapped to the MAC scaffolds), and the chromosome interactions of the 83 MAC scaffolds located on the MIC Chromosome 2 at 1.5 hpm, 3 hpm, and 24 hpm. Zoomed-in views of scf_8254803 are shown at the bottom . (hpm) Hours post-mixing. Numbers at the lower left of heatmaps correspond to the maximum signal in the matrix. ( B , C ) The MAC chromosomes (MAC scaffolds with telomere sequences at both ends) and the MAC scaffolds compared to the chromosome interactions on MIC Chromosome 1 at 3 hpm are shown (whole cells Hi-C data mapped to the MIC genome). Regions from 1 Mb to 36.32 Mb ( B ); zoomed in region from 4 Mb to 14 Mb ( C ).
Titanium Dioxide Coated Mica Pigment, supplied by DIC 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/product/equations+10+imputations+mice+using+the+stata+command+mi+impute+chained/mica+coated+with+titanium+dioxide+sunmica+fine+white+2800102/us10689529-254-20-28
Average 90 stars, based on 1 article reviews
titanium dioxide coated mica pigment - by Bioz Stars, 2026-09
90/100 stars
  Buy from Supplier
mouse monoclonal anti mbp  (New England Biolabs)
96
New England Biolabs mouse monoclonal anti mbp
PP1β dephosphorylates MKLP1 at S708 in cytokinesis. a HeLa Kyoto cells were treated with control or MYPT1 siRNA for 48 h and stained to detect the indicated epitopes. Cells were staged as in Fig. . Insets indicate 3× magnification of the midbody. Scale bars, 10 µm. b Quantification of total and pS708 MKLP1 in control and MYPT1 siRNA cells. The boxes indicate the first quartile to the third quartile, the horizontal lines the median and the whiskers the minimum or maximum. AU, arbitrary unit; n = 32 independent control cells and n = 35 MYPT1 siRNA independent cells for MKLP1 stained cells; n = 38 independent control cells and n = 42 MYPT1 siRNA independent cells for MKLP1-pS708 stained cells; p values from student’s T-test. c HeLa stably expressing GFP-MKLP1 were treated with control or MYPT1 siRNA, synchronized in telophase and GFP pull-down protein extracts analyzed by western blot. The numbers indicate the sizes of the molecular mass marker. d Schematic diagram of MKLP1 protein. The Aurora B phosphorylation site and the VQF PP1-binding site are indicated. e <t>MBP-tagged</t> MKLP1, MKLP1 AQA or MBP alone were co-expressed in yeast and used for MBP pull-down assay. Extracts and pull downs were analyzed by western blot to <t>detect</t> <t>GST</t> and MBP. Numbers indicate the size of the protein ladder. f In vitro phosphatase assay of GST-tagged WT and AQA MKLP1. The reactions were incubated with either MBP-tagged PP1β or a catalytically dead version for the times indicated at the top and analyzed by western blot using antibodies against MKLP1 pS708 and GST. g Graph showing the normalization of MKLP1 pS708 values against the amounts of GST-MKLP1 620–858 . h HeLa Kyoto cells stably expressing GFP-MKLP1, GFP-MKLP1 AQA or no transgene were treated with either control or MKLP1 3′UTR siRNA were stained to detect the indicated epitopes. Scale bars, 10 µm. i Quantification of multinucleate cells from the experiments shown in h . More than 500 independent cells were counted in n ≥ 3 independent experiments. Bars indicate standard errors. * p < 0.05, ** p < 0.01, *** p < 0.001 (Mann–Whitney U test). Source data for Fig. , e–g and i are provided as a Source Data file
Mouse Monoclonal Anti Mbp, supplied by New England Biolabs, 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/product/equations+10+imputations+mice+using+the+stata+command+mi+impute+chained/Anti-MBP+Monoclonal+Antibody/pmc06778137-282-305-308
Average 96 stars, based on 1 article reviews
mouse monoclonal anti mbp - by Bioz Stars, 2026-09
96/100 stars
  Buy from Supplier
c57bl 6jrcchsd mice  (Envigo)
99
Envigo c57bl 6jrcchsd mice
PP1β dephosphorylates MKLP1 at S708 in cytokinesis. a HeLa Kyoto cells were treated with control or MYPT1 siRNA for 48 h and stained to detect the indicated epitopes. Cells were staged as in Fig. . Insets indicate 3× magnification of the midbody. Scale bars, 10 µm. b Quantification of total and pS708 MKLP1 in control and MYPT1 siRNA cells. The boxes indicate the first quartile to the third quartile, the horizontal lines the median and the whiskers the minimum or maximum. AU, arbitrary unit; n = 32 independent control cells and n = 35 MYPT1 siRNA independent cells for MKLP1 stained cells; n = 38 independent control cells and n = 42 MYPT1 siRNA independent cells for MKLP1-pS708 stained cells; p values from student’s T-test. c HeLa stably expressing GFP-MKLP1 were treated with control or MYPT1 siRNA, synchronized in telophase and GFP pull-down protein extracts analyzed by western blot. The numbers indicate the sizes of the molecular mass marker. d Schematic diagram of MKLP1 protein. The Aurora B phosphorylation site and the VQF PP1-binding site are indicated. e <t>MBP-tagged</t> MKLP1, MKLP1 AQA or MBP alone were co-expressed in yeast and used for MBP pull-down assay. Extracts and pull downs were analyzed by western blot to <t>detect</t> <t>GST</t> and MBP. Numbers indicate the size of the protein ladder. f In vitro phosphatase assay of GST-tagged WT and AQA MKLP1. The reactions were incubated with either MBP-tagged PP1β or a catalytically dead version for the times indicated at the top and analyzed by western blot using antibodies against MKLP1 pS708 and GST. g Graph showing the normalization of MKLP1 pS708 values against the amounts of GST-MKLP1 620–858 . h HeLa Kyoto cells stably expressing GFP-MKLP1, GFP-MKLP1 AQA or no transgene were treated with either control or MKLP1 3′UTR siRNA were stained to detect the indicated epitopes. Scale bars, 10 µm. i Quantification of multinucleate cells from the experiments shown in h . More than 500 independent cells were counted in n ≥ 3 independent experiments. Bars indicate standard errors. * p < 0.05, ** p < 0.01, *** p < 0.001 (Mann–Whitney U test). Source data for Fig. , e–g and i are provided as a Source Data file
C57bl 6jrcchsd Mice, supplied by Envigo, 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/product/equations+10+imputations+mice+using+the+stata+command+mi+impute+chained/C57BL%2F6+aged+inbred+mice/pm37551888-146-4-7
Average 99 stars, based on 1 article reviews
c57bl 6jrcchsd mice - by Bioz Stars, 2026-09
99/100 stars
  Buy from Supplier
icam 1 mouse monoclonal igg  (Santa Cruz Biotechnology)
96
Santa Cruz Biotechnology icam 1 mouse monoclonal igg
PP1β dephosphorylates MKLP1 at S708 in cytokinesis. a HeLa Kyoto cells were treated with control or MYPT1 siRNA for 48 h and stained to detect the indicated epitopes. Cells were staged as in Fig. . Insets indicate 3× magnification of the midbody. Scale bars, 10 µm. b Quantification of total and pS708 MKLP1 in control and MYPT1 siRNA cells. The boxes indicate the first quartile to the third quartile, the horizontal lines the median and the whiskers the minimum or maximum. AU, arbitrary unit; n = 32 independent control cells and n = 35 MYPT1 siRNA independent cells for MKLP1 stained cells; n = 38 independent control cells and n = 42 MYPT1 siRNA independent cells for MKLP1-pS708 stained cells; p values from student’s T-test. c HeLa stably expressing GFP-MKLP1 were treated with control or MYPT1 siRNA, synchronized in telophase and GFP pull-down protein extracts analyzed by western blot. The numbers indicate the sizes of the molecular mass marker. d Schematic diagram of MKLP1 protein. The Aurora B phosphorylation site and the VQF PP1-binding site are indicated. e <t>MBP-tagged</t> MKLP1, MKLP1 AQA or MBP alone were co-expressed in yeast and used for MBP pull-down assay. Extracts and pull downs were analyzed by western blot to <t>detect</t> <t>GST</t> and MBP. Numbers indicate the size of the protein ladder. f In vitro phosphatase assay of GST-tagged WT and AQA MKLP1. The reactions were incubated with either MBP-tagged PP1β or a catalytically dead version for the times indicated at the top and analyzed by western blot using antibodies against MKLP1 pS708 and GST. g Graph showing the normalization of MKLP1 pS708 values against the amounts of GST-MKLP1 620–858 . h HeLa Kyoto cells stably expressing GFP-MKLP1, GFP-MKLP1 AQA or no transgene were treated with either control or MKLP1 3′UTR siRNA were stained to detect the indicated epitopes. Scale bars, 10 µm. i Quantification of multinucleate cells from the experiments shown in h . More than 500 independent cells were counted in n ≥ 3 independent experiments. Bars indicate standard errors. * p < 0.05, ** p < 0.01, *** p < 0.001 (Mann–Whitney U test). Source data for Fig. , e–g and i are provided as a Source Data file
Icam 1 Mouse Monoclonal Igg, supplied by Santa Cruz Biotechnology, 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/product/equations+10+imputations+mice+using+the+stata+command+mi+impute+chained/ICAM-1+Antibody/10__1515_slash_tjb___2021___0248-72-8-12
Average 96 stars, based on 1 article reviews
icam 1 mouse monoclonal igg - by Bioz Stars, 2026-09
96/100 stars
  Buy from Supplier
f4 80 macrophage staining  (Bio-Rad)
96
Bio-Rad f4 80 macrophage staining
PP1β dephosphorylates MKLP1 at S708 in cytokinesis. a HeLa Kyoto cells were treated with control or MYPT1 siRNA for 48 h and stained to detect the indicated epitopes. Cells were staged as in Fig. . Insets indicate 3× magnification of the midbody. Scale bars, 10 µm. b Quantification of total and pS708 MKLP1 in control and MYPT1 siRNA cells. The boxes indicate the first quartile to the third quartile, the horizontal lines the median and the whiskers the minimum or maximum. AU, arbitrary unit; n = 32 independent control cells and n = 35 MYPT1 siRNA independent cells for MKLP1 stained cells; n = 38 independent control cells and n = 42 MYPT1 siRNA independent cells for MKLP1-pS708 stained cells; p values from student’s T-test. c HeLa stably expressing GFP-MKLP1 were treated with control or MYPT1 siRNA, synchronized in telophase and GFP pull-down protein extracts analyzed by western blot. The numbers indicate the sizes of the molecular mass marker. d Schematic diagram of MKLP1 protein. The Aurora B phosphorylation site and the VQF PP1-binding site are indicated. e <t>MBP-tagged</t> MKLP1, MKLP1 AQA or MBP alone were co-expressed in yeast and used for MBP pull-down assay. Extracts and pull downs were analyzed by western blot to <t>detect</t> <t>GST</t> and MBP. Numbers indicate the size of the protein ladder. f In vitro phosphatase assay of GST-tagged WT and AQA MKLP1. The reactions were incubated with either MBP-tagged PP1β or a catalytically dead version for the times indicated at the top and analyzed by western blot using antibodies against MKLP1 pS708 and GST. g Graph showing the normalization of MKLP1 pS708 values against the amounts of GST-MKLP1 620–858 . h HeLa Kyoto cells stably expressing GFP-MKLP1, GFP-MKLP1 AQA or no transgene were treated with either control or MKLP1 3′UTR siRNA were stained to detect the indicated epitopes. Scale bars, 10 µm. i Quantification of multinucleate cells from the experiments shown in h . More than 500 independent cells were counted in n ≥ 3 independent experiments. Bars indicate standard errors. * p < 0.05, ** p < 0.01, *** p < 0.001 (Mann–Whitney U test). Source data for Fig. , e–g and i are provided as a Source Data file
F4 80 Macrophage Staining, 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
https://www.bioz.com/product/equations+10+imputations+mice+using+the+stata+command+mi+impute+chained/Rat+anti+Mouse+F4%2F80/pmc09808650-141-11-19
Average 96 stars, based on 1 article reviews
f4 80 macrophage staining - by Bioz Stars, 2026-09
96/100 stars
  Buy from Supplier
pcmv6 mouse boule deletion plasmids  (OriGene)
90
OriGene pcmv6 mouse boule deletion plasmids
PP1β dephosphorylates MKLP1 at S708 in cytokinesis. a HeLa Kyoto cells were treated with control or MYPT1 siRNA for 48 h and stained to detect the indicated epitopes. Cells were staged as in Fig. . Insets indicate 3× magnification of the midbody. Scale bars, 10 µm. b Quantification of total and pS708 MKLP1 in control and MYPT1 siRNA cells. The boxes indicate the first quartile to the third quartile, the horizontal lines the median and the whiskers the minimum or maximum. AU, arbitrary unit; n = 32 independent control cells and n = 35 MYPT1 siRNA independent cells for MKLP1 stained cells; n = 38 independent control cells and n = 42 MYPT1 siRNA independent cells for MKLP1-pS708 stained cells; p values from student’s T-test. c HeLa stably expressing GFP-MKLP1 were treated with control or MYPT1 siRNA, synchronized in telophase and GFP pull-down protein extracts analyzed by western blot. The numbers indicate the sizes of the molecular mass marker. d Schematic diagram of MKLP1 protein. The Aurora B phosphorylation site and the VQF PP1-binding site are indicated. e <t>MBP-tagged</t> MKLP1, MKLP1 AQA or MBP alone were co-expressed in yeast and used for MBP pull-down assay. Extracts and pull downs were analyzed by western blot to <t>detect</t> <t>GST</t> and MBP. Numbers indicate the size of the protein ladder. f In vitro phosphatase assay of GST-tagged WT and AQA MKLP1. The reactions were incubated with either MBP-tagged PP1β or a catalytically dead version for the times indicated at the top and analyzed by western blot using antibodies against MKLP1 pS708 and GST. g Graph showing the normalization of MKLP1 pS708 values against the amounts of GST-MKLP1 620–858 . h HeLa Kyoto cells stably expressing GFP-MKLP1, GFP-MKLP1 AQA or no transgene were treated with either control or MKLP1 3′UTR siRNA were stained to detect the indicated epitopes. Scale bars, 10 µm. i Quantification of multinucleate cells from the experiments shown in h . More than 500 independent cells were counted in n ≥ 3 independent experiments. Bars indicate standard errors. * p < 0.05, ** p < 0.01, *** p < 0.001 (Mann–Whitney U test). Source data for Fig. , e–g and i are provided as a Source Data file
Pcmv6 Mouse Boule Deletion Plasmids, supplied by OriGene, 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/equations+10+imputations+mice+using+the+stata+command+mi+impute+chained/SOX10+(BC002824)+Human+Untagged+Clone/pmc09376728-126-31-55
Average 90 stars, based on 1 article reviews
pcmv6 mouse boule deletion plasmids - by Bioz Stars, 2026-09
90/100 stars
  Buy from Supplier
dpbs 4 u mouse rnase inhibitor  (New England Biolabs)
99
New England Biolabs dpbs 4 u mouse rnase inhibitor
PP1β dephosphorylates MKLP1 at S708 in cytokinesis. a HeLa Kyoto cells were treated with control or MYPT1 siRNA for 48 h and stained to detect the indicated epitopes. Cells were staged as in Fig. . Insets indicate 3× magnification of the midbody. Scale bars, 10 µm. b Quantification of total and pS708 MKLP1 in control and MYPT1 siRNA cells. The boxes indicate the first quartile to the third quartile, the horizontal lines the median and the whiskers the minimum or maximum. AU, arbitrary unit; n = 32 independent control cells and n = 35 MYPT1 siRNA independent cells for MKLP1 stained cells; n = 38 independent control cells and n = 42 MYPT1 siRNA independent cells for MKLP1-pS708 stained cells; p values from student’s T-test. c HeLa stably expressing GFP-MKLP1 were treated with control or MYPT1 siRNA, synchronized in telophase and GFP pull-down protein extracts analyzed by western blot. The numbers indicate the sizes of the molecular mass marker. d Schematic diagram of MKLP1 protein. The Aurora B phosphorylation site and the VQF PP1-binding site are indicated. e <t>MBP-tagged</t> MKLP1, MKLP1 AQA or MBP alone were co-expressed in yeast and used for MBP pull-down assay. Extracts and pull downs were analyzed by western blot to <t>detect</t> <t>GST</t> and MBP. Numbers indicate the size of the protein ladder. f In vitro phosphatase assay of GST-tagged WT and AQA MKLP1. The reactions were incubated with either MBP-tagged PP1β or a catalytically dead version for the times indicated at the top and analyzed by western blot using antibodies against MKLP1 pS708 and GST. g Graph showing the normalization of MKLP1 pS708 values against the amounts of GST-MKLP1 620–858 . h HeLa Kyoto cells stably expressing GFP-MKLP1, GFP-MKLP1 AQA or no transgene were treated with either control or MKLP1 3′UTR siRNA were stained to detect the indicated epitopes. Scale bars, 10 µm. i Quantification of multinucleate cells from the experiments shown in h . More than 500 independent cells were counted in n ≥ 3 independent experiments. Bars indicate standard errors. * p < 0.05, ** p < 0.01, *** p < 0.001 (Mann–Whitney U test). Source data for Fig. , e–g and i are provided as a Source Data file
Dpbs 4 U Mouse Rnase Inhibitor, supplied by New England Biolabs, 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/product/equations+10+imputations+mice+using+the+stata+command+mi+impute+chained/RNase+Inhibitor/bio_rxiv__2020__05__19__104117-122-28-34
Average 99 stars, based on 1 article reviews
dpbs 4 u mouse rnase inhibitor - by Bioz Stars, 2026-09
99/100 stars
  Buy from Supplier
anti mbp antibody  (New England Biolabs)
96
New England Biolabs anti mbp antibody
WRKY40 interacts with XopS in planta and in vitro. A, Subcellular localization of XopS-GFP and Nb WRKY40-GFP. GFP fusion proteins or free GFP under control of the CaMV35S promoter were expressed transiently in leaves of N. benthamiana using Agrobacterium- infiltration. The localization of transiently expressed proteins (left) was determined with confocal laser scanning microscopy 24 hpi. Scale bars represent 20 µm. DIC, Differential Interference Contrast. A representative image from 10 randomly chosen regions of interest of infiltrated leaves is shown. The experiment was carried out at least 3 times with similar results. Protein expression was verified by immunoblotting using an anti-GFP antibody (right). Amido black staining of RubisCo served as a loading control. B, Co-IP of either free GFP or XopS-GFP with Nb WRKY40-HA or Nb WRKY8-HA. Proteins were transiently co-expressed in leaves of N. benthamiana using Agrobacterium -infiltration. After 24 h, total protein extracts (Input) were subjected to IP (IP:GFP) with GFP-Trap beads, followed by immunoblotting using either anti-GFP or anti-HA antibodies. Amido black staining of RubisCo served as a loading control for input samples. The experiment was carried out at least 2 times with similar results. C, In vitro pull-down assay showing physical interaction of XopS with Nb WRKY40. <t>MBP,</t> MBP- Nb WRKY40, MBP- Nb WRKY8, GST, and GST-XopS were expressed in E. coli. Pull-down was performed by affinity purification of MBP-tagged proteins using amylose resin. MBP alone and GST alone were used as negative controls. Pull-down experiments with MBP- Nb WRKY8 were additionally performed to confirm specificity of interaction between Nb WRKY40 and XopS. Indicated recombinant proteins were detected before (Input 10%) and after affinity purification (IP:MBP) by immunoblotting using <t>anti-MBP</t> or anti-GST antibodies. The experiment was carried out twice with similar results.
Anti Mbp Antibody, supplied by New England Biolabs, 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/product/equations+10+imputations+mice+using+the+stata+command+mi+impute+chained/Anti-MBP+Monoclonal+Antibody/pmc09048924-385-53-56
Average 96 stars, based on 1 article reviews
anti mbp antibody - by Bioz Stars, 2026-09
96/100 stars
  Buy from Supplier
mouse anti-human cd81 primary antibody  (Becton Dickinson)
90
Becton Dickinson mouse anti-human cd81 primary antibody
Expression of tetraspanins CD9 and <t>CD81</t> during osteoclast differentiation and HIV infection. The expression level of CD9 and CD81 was measured using flow cytometry (mean fluorescence intensity per cell, or MFI) at 6 days post-infection (dpi) using both HIV inoculums. The results are representative of two independent experiments performed using cells from different donors (A) . Osteoclasts and their precursors at 6 dpi of HIV infection with the low-inoculum (upper panel) and control (non-infected) (lower panel) were stained with DAPI (for cell nuclei), PE (for HIV-p24 capsid antigen), FITC (for CD81), and merged using immunofluorescence staining and deconvolution microscopy to examine changes in the cellular localization of tetraspanins during maturation and HIV infection (x400) (B) . Osteoclasts and their precursors at 6 dpi of HIV infection with the low-inoculum showing CD81 expression (green) and HIV-infected giant multinuclear cells (red, with nuclei in blue). (C) Yellow arrows show perinuclear structures resembling viral-containing compartments (VCC). Scale bars: 20 μm. *<0.05 indicates a statistically significant difference.
Mouse Anti Human Cd81 Primary Antibody, supplied by Becton Dickinson, 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/equations+10+imputations+mice+using+the+stata+command+mi+impute+chained/anti+cd81/pmc10315468-87-21-27
Average 90 stars, based on 1 article reviews
mouse anti-human cd81 primary antibody - by Bioz Stars, 2026-09
90/100 stars
  Buy from Supplier
mouse genomic dna  (New England Biolabs)
99
New England Biolabs mouse genomic dna
Expression of tetraspanins CD9 and <t>CD81</t> during osteoclast differentiation and HIV infection. The expression level of CD9 and CD81 was measured using flow cytometry (mean fluorescence intensity per cell, or MFI) at 6 days post-infection (dpi) using both HIV inoculums. The results are representative of two independent experiments performed using cells from different donors (A) . Osteoclasts and their precursors at 6 dpi of HIV infection with the low-inoculum (upper panel) and control (non-infected) (lower panel) were stained with DAPI (for cell nuclei), PE (for HIV-p24 capsid antigen), FITC (for CD81), and merged using immunofluorescence staining and deconvolution microscopy to examine changes in the cellular localization of tetraspanins during maturation and HIV infection (x400) (B) . Osteoclasts and their precursors at 6 dpi of HIV infection with the low-inoculum showing CD81 expression (green) and HIV-infected giant multinuclear cells (red, with nuclei in blue). (C) Yellow arrows show perinuclear structures resembling viral-containing compartments (VCC). Scale bars: 20 μm. *<0.05 indicates a statistically significant difference.
Mouse Genomic Dna, supplied by New England Biolabs, 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/product/equations+10+imputations+mice+using+the+stata+command+mi+impute+chained/HindIII/pm08574847-231-0-32
Average 99 stars, based on 1 article reviews
mouse genomic dna - by Bioz Stars, 2026-09
99/100 stars
  Buy from Supplier
anti mouse igg magnetic beads  (New England Biolabs)
95
New England Biolabs anti mouse igg magnetic beads
Expression of tetraspanins CD9 and <t>CD81</t> during osteoclast differentiation and HIV infection. The expression level of CD9 and CD81 was measured using flow cytometry (mean fluorescence intensity per cell, or MFI) at 6 days post-infection (dpi) using both HIV inoculums. The results are representative of two independent experiments performed using cells from different donors (A) . Osteoclasts and their precursors at 6 dpi of HIV infection with the low-inoculum (upper panel) and control (non-infected) (lower panel) were stained with DAPI (for cell nuclei), PE (for HIV-p24 capsid antigen), FITC (for CD81), and merged using immunofluorescence staining and deconvolution microscopy to examine changes in the cellular localization of tetraspanins during maturation and HIV infection (x400) (B) . Osteoclasts and their precursors at 6 dpi of HIV infection with the low-inoculum showing CD81 expression (green) and HIV-infected giant multinuclear cells (red, with nuclei in blue). (C) Yellow arrows show perinuclear structures resembling viral-containing compartments (VCC). Scale bars: 20 μm. *<0.05 indicates a statistically significant difference.
Anti Mouse Igg Magnetic Beads, supplied by New England Biolabs, 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/equations+10+imputations+mice+using+the+stata+command+mi+impute+chained/Anti-MBP+Magnetic+Beads/pmc06090163-148-17-23
Average 95 stars, based on 1 article reviews
anti mouse igg magnetic beads - by Bioz Stars, 2026-09
95/100 stars
  Buy from Supplier

Image Search Results


The square-shaped interaction patterns in the MAC of T. thermophila are chromosome territories. ( A ) Heatmaps showing the chromosome interactions on the 568 MAC scaffolds (ordered by their locations on the MIC genome) at 3 hpm (whole cells Hi-C data mapped to the MAC scaffolds), and the chromosome interactions of the 83 MAC scaffolds located on the MIC Chromosome 2 at 1.5 hpm, 3 hpm, and 24 hpm. Zoomed-in views of scf_8254803 are shown at the bottom . (hpm) Hours post-mixing. Numbers at the lower left of heatmaps correspond to the maximum signal in the matrix. ( B , C ) The MAC chromosomes (MAC scaffolds with telomere sequences at both ends) and the MAC scaffolds compared to the chromosome interactions on MIC Chromosome 1 at 3 hpm are shown (whole cells Hi-C data mapped to the MIC genome). Regions from 1 Mb to 36.32 Mb ( B ); zoomed in region from 4 Mb to 14 Mb ( C ).

Journal: Genome Research

Article Title: Rearrangement of macronucleus chromosomes correspond to TAD-like structures of micronucleus chromosomes in Tetrahymena thermophila

doi: 10.1101/gr.241687.118

Figure Lengend Snippet: The square-shaped interaction patterns in the MAC of T. thermophila are chromosome territories. ( A ) Heatmaps showing the chromosome interactions on the 568 MAC scaffolds (ordered by their locations on the MIC genome) at 3 hpm (whole cells Hi-C data mapped to the MAC scaffolds), and the chromosome interactions of the 83 MAC scaffolds located on the MIC Chromosome 2 at 1.5 hpm, 3 hpm, and 24 hpm. Zoomed-in views of scf_8254803 are shown at the bottom . (hpm) Hours post-mixing. Numbers at the lower left of heatmaps correspond to the maximum signal in the matrix. ( B , C ) The MAC chromosomes (MAC scaffolds with telomere sequences at both ends) and the MAC scaffolds compared to the chromosome interactions on MIC Chromosome 1 at 3 hpm are shown (whole cells Hi-C data mapped to the MIC genome). Regions from 1 Mb to 36.32 Mb ( B ); zoomed in region from 4 Mb to 14 Mb ( C ).

Article Snippet: Then, we centrifuged at 780 g for 10 min at 4°C, transferred the solution which contains MIC to a new tube (the pellet which contains MAC was also collected and washed twice with 1× NEBuffer 2.1), centrifuged the tubes with MIC again at 780 g for 10 min at 4°C, repeated this step 3–4 times and checked by DAPI stain to see if the MIC was pure.

Techniques: Hi-C

Boundaries of TAD-like structures in the MIC are consistent with CBS sites. ( A ) The schematic diagram shows the development of MAC and MIC from the same zygotic nuclei during conjugation. ( B ) The location of CBS sites, boundaries, and TAD-like structures compared to the heatmaps on the Chromosome 4 (2.5 Mb to 10.5 Mb) at 3 hpm. ( C ) The bar plot shows percentage of CBS sites localized to the boundaries of the TAD-like structures (10 kb) or 20 kb around the boundaries (total 50 kb). ( D ) Heatmaps showing averaged Hi-C interaction counts (Smc1-HA HiChIP, 1.5 hpm) around the boundaries of TAD-like structures. ( E ) Heatmaps showing averaged Hi-C interaction counts (Smc1-HA HiChIP, 1.5 hpm) around the CBS sites.

Journal: Genome Research

Article Title: Rearrangement of macronucleus chromosomes correspond to TAD-like structures of micronucleus chromosomes in Tetrahymena thermophila

doi: 10.1101/gr.241687.118

Figure Lengend Snippet: Boundaries of TAD-like structures in the MIC are consistent with CBS sites. ( A ) The schematic diagram shows the development of MAC and MIC from the same zygotic nuclei during conjugation. ( B ) The location of CBS sites, boundaries, and TAD-like structures compared to the heatmaps on the Chromosome 4 (2.5 Mb to 10.5 Mb) at 3 hpm. ( C ) The bar plot shows percentage of CBS sites localized to the boundaries of the TAD-like structures (10 kb) or 20 kb around the boundaries (total 50 kb). ( D ) Heatmaps showing averaged Hi-C interaction counts (Smc1-HA HiChIP, 1.5 hpm) around the boundaries of TAD-like structures. ( E ) Heatmaps showing averaged Hi-C interaction counts (Smc1-HA HiChIP, 1.5 hpm) around the CBS sites.

Article Snippet: Then, we centrifuged at 780 g for 10 min at 4°C, transferred the solution which contains MIC to a new tube (the pellet which contains MAC was also collected and washed twice with 1× NEBuffer 2.1), centrifuged the tubes with MIC again at 780 g for 10 min at 4°C, repeated this step 3–4 times and checked by DAPI stain to see if the MIC was pure.

Techniques: Conjugation Assay, Hi-C, HiChIP

The MAC chromosomes are related to the MIC TAD-like structures during conjugation. ( A ) The heatmap regions (Chromosome 1: 3.2 Mb to 7.2 Mb) of the MIC (Smc1-HA HiChIP at 3 hpm, upper ) and the MAC (whole cells Hi-C at 3 hpm, below ) compared to the CBS sites on the MIC and the MAC scaffolds are plotted. ( B ) The heatmap showing the Hi-C interactions on six of the MAC scaffolds at 3 hpm (whole cells Hi-C data mapped to the MAC scaffolds). ( C ) The heatmap showing the Hi-C interactions on the MIC Chromosome 4 (4.11 Mb to 8.14 Mb) at 3 hpm (whole cells Hi-C data mapped to the MIC genome). ( D ) The heatmap showing the Hi-C interactions on the MIC Chromosome 4 (4.11 Mb to 8.14 Mb) at 3 hpm (Smc1-HA HiChIP data mapped to the MIC genome). ( E ) A model for the MAC chromosomes development during the conjugation of T. thermophila . The TAD-like structures established in the zygotic nuclei were followed by chromosome breakage at CBS sites.

Journal: Genome Research

Article Title: Rearrangement of macronucleus chromosomes correspond to TAD-like structures of micronucleus chromosomes in Tetrahymena thermophila

doi: 10.1101/gr.241687.118

Figure Lengend Snippet: The MAC chromosomes are related to the MIC TAD-like structures during conjugation. ( A ) The heatmap regions (Chromosome 1: 3.2 Mb to 7.2 Mb) of the MIC (Smc1-HA HiChIP at 3 hpm, upper ) and the MAC (whole cells Hi-C at 3 hpm, below ) compared to the CBS sites on the MIC and the MAC scaffolds are plotted. ( B ) The heatmap showing the Hi-C interactions on six of the MAC scaffolds at 3 hpm (whole cells Hi-C data mapped to the MAC scaffolds). ( C ) The heatmap showing the Hi-C interactions on the MIC Chromosome 4 (4.11 Mb to 8.14 Mb) at 3 hpm (whole cells Hi-C data mapped to the MIC genome). ( D ) The heatmap showing the Hi-C interactions on the MIC Chromosome 4 (4.11 Mb to 8.14 Mb) at 3 hpm (Smc1-HA HiChIP data mapped to the MIC genome). ( E ) A model for the MAC chromosomes development during the conjugation of T. thermophila . The TAD-like structures established in the zygotic nuclei were followed by chromosome breakage at CBS sites.

Article Snippet: Then, we centrifuged at 780 g for 10 min at 4°C, transferred the solution which contains MIC to a new tube (the pellet which contains MAC was also collected and washed twice with 1× NEBuffer 2.1), centrifuged the tubes with MIC again at 780 g for 10 min at 4°C, repeated this step 3–4 times and checked by DAPI stain to see if the MIC was pure.

Techniques: Conjugation Assay, HiChIP, Hi-C

PP1β dephosphorylates MKLP1 at S708 in cytokinesis. a HeLa Kyoto cells were treated with control or MYPT1 siRNA for 48 h and stained to detect the indicated epitopes. Cells were staged as in Fig. . Insets indicate 3× magnification of the midbody. Scale bars, 10 µm. b Quantification of total and pS708 MKLP1 in control and MYPT1 siRNA cells. The boxes indicate the first quartile to the third quartile, the horizontal lines the median and the whiskers the minimum or maximum. AU, arbitrary unit; n = 32 independent control cells and n = 35 MYPT1 siRNA independent cells for MKLP1 stained cells; n = 38 independent control cells and n = 42 MYPT1 siRNA independent cells for MKLP1-pS708 stained cells; p values from student’s T-test. c HeLa stably expressing GFP-MKLP1 were treated with control or MYPT1 siRNA, synchronized in telophase and GFP pull-down protein extracts analyzed by western blot. The numbers indicate the sizes of the molecular mass marker. d Schematic diagram of MKLP1 protein. The Aurora B phosphorylation site and the VQF PP1-binding site are indicated. e MBP-tagged MKLP1, MKLP1 AQA or MBP alone were co-expressed in yeast and used for MBP pull-down assay. Extracts and pull downs were analyzed by western blot to detect GST and MBP. Numbers indicate the size of the protein ladder. f In vitro phosphatase assay of GST-tagged WT and AQA MKLP1. The reactions were incubated with either MBP-tagged PP1β or a catalytically dead version for the times indicated at the top and analyzed by western blot using antibodies against MKLP1 pS708 and GST. g Graph showing the normalization of MKLP1 pS708 values against the amounts of GST-MKLP1 620–858 . h HeLa Kyoto cells stably expressing GFP-MKLP1, GFP-MKLP1 AQA or no transgene were treated with either control or MKLP1 3′UTR siRNA were stained to detect the indicated epitopes. Scale bars, 10 µm. i Quantification of multinucleate cells from the experiments shown in h . More than 500 independent cells were counted in n ≥ 3 independent experiments. Bars indicate standard errors. * p < 0.05, ** p < 0.01, *** p < 0.001 (Mann–Whitney U test). Source data for Fig. , e–g and i are provided as a Source Data file

Journal: Nature Communications

Article Title: The midbody interactome reveals unexpected roles for PP1 phosphatases in cytokinesis

doi: 10.1038/s41467-019-12507-9

Figure Lengend Snippet: PP1β dephosphorylates MKLP1 at S708 in cytokinesis. a HeLa Kyoto cells were treated with control or MYPT1 siRNA for 48 h and stained to detect the indicated epitopes. Cells were staged as in Fig. . Insets indicate 3× magnification of the midbody. Scale bars, 10 µm. b Quantification of total and pS708 MKLP1 in control and MYPT1 siRNA cells. The boxes indicate the first quartile to the third quartile, the horizontal lines the median and the whiskers the minimum or maximum. AU, arbitrary unit; n = 32 independent control cells and n = 35 MYPT1 siRNA independent cells for MKLP1 stained cells; n = 38 independent control cells and n = 42 MYPT1 siRNA independent cells for MKLP1-pS708 stained cells; p values from student’s T-test. c HeLa stably expressing GFP-MKLP1 were treated with control or MYPT1 siRNA, synchronized in telophase and GFP pull-down protein extracts analyzed by western blot. The numbers indicate the sizes of the molecular mass marker. d Schematic diagram of MKLP1 protein. The Aurora B phosphorylation site and the VQF PP1-binding site are indicated. e MBP-tagged MKLP1, MKLP1 AQA or MBP alone were co-expressed in yeast and used for MBP pull-down assay. Extracts and pull downs were analyzed by western blot to detect GST and MBP. Numbers indicate the size of the protein ladder. f In vitro phosphatase assay of GST-tagged WT and AQA MKLP1. The reactions were incubated with either MBP-tagged PP1β or a catalytically dead version for the times indicated at the top and analyzed by western blot using antibodies against MKLP1 pS708 and GST. g Graph showing the normalization of MKLP1 pS708 values against the amounts of GST-MKLP1 620–858 . h HeLa Kyoto cells stably expressing GFP-MKLP1, GFP-MKLP1 AQA or no transgene were treated with either control or MKLP1 3′UTR siRNA were stained to detect the indicated epitopes. Scale bars, 10 µm. i Quantification of multinucleate cells from the experiments shown in h . More than 500 independent cells were counted in n ≥ 3 independent experiments. Bars indicate standard errors. * p < 0.05, ** p < 0.01, *** p < 0.001 (Mann–Whitney U test). Source data for Fig. , e–g and i are provided as a Source Data file

Article Snippet: The following antibodies and dilutions for western blot (WB) and immunofluorescence (IF) were used in this study: mouse monoclonal anti α-tubulin (clone DM1A, Sigma, T9026 dilutions for WB 1:20,000, for IF 1:2000), rabbit polyclonal anti-β-tubulin (Abcam, ab6046 dilutions for WB 1:5000, for IF 1:400), mouse monoclonal anti-cyclin B1 (clone GNS1, Santa Cruz, sc-245 dilution for WB 1:2000), mouse monoclonal anti-PP1α (clone G-4, Santa Cruz, sc-271762 dilutions for WB 1:1000, for IF 1:50), mouse monoclonal anti-PP1β (clone A-6, Santa Cruz, sc-365678 dilutions for WB 1:10,000, for IF 1:50), mouse monoclonal anti-PP1γ (clone A-4, Santa Cruz, sc-515943 dilutions for WB 1:2000, for IF 1:50), mouse monoclonal anti-CIT-K (BD Transduction Laboratories, 611377 dilutions for WB 1:1500, for IF 1:250), mouse monoclonal anti-MYPT1 (clone C-6, Santa Cruz, sc-514261 dilutions for WB 1:1500, for IF 1:50), rabbit polyclonal anti-Aurora A (Abcam, ab1287 dilution for WB 1:4000), rabbit polyclonal anti-TPX2 (Novus Biologicals, NB500-179 dilution for WB 1:1000), rabbit polyclonal anti-KIF14 (Bethyl Laboratories A300-233A dilution for WB 1:2000) rabbit polyclonal anti-MKLP1 (clone N19, Santa Cruz Biotechnology, sc-867, dilutions for WB 1:3000, for IF 1:500), rabbit polyclonal anti-phospho MKLP1 pS708 (dilutions for WB 1:2000, for IF 1:200), rabbit polyclonal anti-tri-phospho CHMP4C pS210 pS214 pS215 (dilution for WB 1:400), mouse monoclonal anti-Aurora B (clone AIM-1, BD Transduction Laboratories, 611082 dilutions for WB 1:2000, for IF 1:100), mouse monoclonal anti-PRC1 (clone C-1, Santa Cruz, sc-376983 dilutions for WB 1:5000, for IF 1:100), rabbit monoclonal anti-phospho PRC1 pT481 (Abcam, ab62366 dilution for WB 1:12,000), rabbit polyclonal anti-phospho-histone H3 pS10 (Merck, 06-570 dilution for WB 1:10,000), rabbit polyclonal anti-mono-phospho MRLC pS19 (Cell Signaling Technology, 3671, dilutions for WB 1:1000, for IF 1:50), rabbit polyclonal anti-di-phospho MRLC pT18 pS19 (Cell Signaling Technology, 3674, dilutions for WB 1:1000, for IF 1:100), goat polyclonal anti-RacGAP1 (Abcam, ab2270 dilution for WB 1:1000), mouse monoclonal anti-GST (Abcam, ab92 dilution for WB 1:20,000), mouse monoclonal anti-MBP (NEB, E8032 dilution for WB 1:10,000).

Techniques: Staining, Stable Transfection, Expressing, Western Blot, Marker, Binding Assay, Pull Down Assay, In Vitro, Phosphatase Assay, Incubation, MANN-WHITNEY

WRKY40 interacts with XopS in planta and in vitro. A, Subcellular localization of XopS-GFP and Nb WRKY40-GFP. GFP fusion proteins or free GFP under control of the CaMV35S promoter were expressed transiently in leaves of N. benthamiana using Agrobacterium- infiltration. The localization of transiently expressed proteins (left) was determined with confocal laser scanning microscopy 24 hpi. Scale bars represent 20 µm. DIC, Differential Interference Contrast. A representative image from 10 randomly chosen regions of interest of infiltrated leaves is shown. The experiment was carried out at least 3 times with similar results. Protein expression was verified by immunoblotting using an anti-GFP antibody (right). Amido black staining of RubisCo served as a loading control. B, Co-IP of either free GFP or XopS-GFP with Nb WRKY40-HA or Nb WRKY8-HA. Proteins were transiently co-expressed in leaves of N. benthamiana using Agrobacterium -infiltration. After 24 h, total protein extracts (Input) were subjected to IP (IP:GFP) with GFP-Trap beads, followed by immunoblotting using either anti-GFP or anti-HA antibodies. Amido black staining of RubisCo served as a loading control for input samples. The experiment was carried out at least 2 times with similar results. C, In vitro pull-down assay showing physical interaction of XopS with Nb WRKY40. MBP, MBP- Nb WRKY40, MBP- Nb WRKY8, GST, and GST-XopS were expressed in E. coli. Pull-down was performed by affinity purification of MBP-tagged proteins using amylose resin. MBP alone and GST alone were used as negative controls. Pull-down experiments with MBP- Nb WRKY8 were additionally performed to confirm specificity of interaction between Nb WRKY40 and XopS. Indicated recombinant proteins were detected before (Input 10%) and after affinity purification (IP:MBP) by immunoblotting using anti-MBP or anti-GST antibodies. The experiment was carried out twice with similar results.

Journal: The Plant Cell

Article Title: The Xanthomonas type-III effector XopS stabilizes Ca WRKY40a to regulate defense responses and stomatal immunity in pepper ( Capsicum annuum )

doi: 10.1093/plcell/koac032

Figure Lengend Snippet: WRKY40 interacts with XopS in planta and in vitro. A, Subcellular localization of XopS-GFP and Nb WRKY40-GFP. GFP fusion proteins or free GFP under control of the CaMV35S promoter were expressed transiently in leaves of N. benthamiana using Agrobacterium- infiltration. The localization of transiently expressed proteins (left) was determined with confocal laser scanning microscopy 24 hpi. Scale bars represent 20 µm. DIC, Differential Interference Contrast. A representative image from 10 randomly chosen regions of interest of infiltrated leaves is shown. The experiment was carried out at least 3 times with similar results. Protein expression was verified by immunoblotting using an anti-GFP antibody (right). Amido black staining of RubisCo served as a loading control. B, Co-IP of either free GFP or XopS-GFP with Nb WRKY40-HA or Nb WRKY8-HA. Proteins were transiently co-expressed in leaves of N. benthamiana using Agrobacterium -infiltration. After 24 h, total protein extracts (Input) were subjected to IP (IP:GFP) with GFP-Trap beads, followed by immunoblotting using either anti-GFP or anti-HA antibodies. Amido black staining of RubisCo served as a loading control for input samples. The experiment was carried out at least 2 times with similar results. C, In vitro pull-down assay showing physical interaction of XopS with Nb WRKY40. MBP, MBP- Nb WRKY40, MBP- Nb WRKY8, GST, and GST-XopS were expressed in E. coli. Pull-down was performed by affinity purification of MBP-tagged proteins using amylose resin. MBP alone and GST alone were used as negative controls. Pull-down experiments with MBP- Nb WRKY8 were additionally performed to confirm specificity of interaction between Nb WRKY40 and XopS. Indicated recombinant proteins were detected before (Input 10%) and after affinity purification (IP:MBP) by immunoblotting using anti-MBP or anti-GST antibodies. The experiment was carried out twice with similar results.

Article Snippet: Recombinant MBP- Nb WRKY40, MBP- Nb WRKY8, or MBP alone from E. coli lysates were immobilized on amylose resins (NEB), incubated for 1 h at 4°C with purified GST-XopS or GST alone, eluted, and analyzed by immunoblotting using either anti-GST antibody (1:1,000, horseradish peroxidase-conjugated; Santa Cruz Biotechnology Inc.; cat. no. sc-138 HRP) or anti-MBP antibody (1:10,000; NEB, cat. no. E8032S; used with 1:10,000 secondary horseradish peroxidase-conjugated anti-mouse antibody; ThermoFisher; cat. no. 31430).

Techniques: In Vitro, Confocal Laser Scanning Microscopy, Expressing, Western Blot, Staining, Co-Immunoprecipitation Assay, Pull Down Assay, Affinity Purification, Recombinant

Expression of tetraspanins CD9 and CD81 during osteoclast differentiation and HIV infection. The expression level of CD9 and CD81 was measured using flow cytometry (mean fluorescence intensity per cell, or MFI) at 6 days post-infection (dpi) using both HIV inoculums. The results are representative of two independent experiments performed using cells from different donors (A) . Osteoclasts and their precursors at 6 dpi of HIV infection with the low-inoculum (upper panel) and control (non-infected) (lower panel) were stained with DAPI (for cell nuclei), PE (for HIV-p24 capsid antigen), FITC (for CD81), and merged using immunofluorescence staining and deconvolution microscopy to examine changes in the cellular localization of tetraspanins during maturation and HIV infection (x400) (B) . Osteoclasts and their precursors at 6 dpi of HIV infection with the low-inoculum showing CD81 expression (green) and HIV-infected giant multinuclear cells (red, with nuclei in blue). (C) Yellow arrows show perinuclear structures resembling viral-containing compartments (VCC). Scale bars: 20 μm. *<0.05 indicates a statistically significant difference.

Journal: Frontiers in Immunology

Article Title: Massively HIV-1-infected macrophages exhibit a severely hampered ability to differentiate into osteoclasts

doi: 10.3389/fimmu.2023.1206099

Figure Lengend Snippet: Expression of tetraspanins CD9 and CD81 during osteoclast differentiation and HIV infection. The expression level of CD9 and CD81 was measured using flow cytometry (mean fluorescence intensity per cell, or MFI) at 6 days post-infection (dpi) using both HIV inoculums. The results are representative of two independent experiments performed using cells from different donors (A) . Osteoclasts and their precursors at 6 dpi of HIV infection with the low-inoculum (upper panel) and control (non-infected) (lower panel) were stained with DAPI (for cell nuclei), PE (for HIV-p24 capsid antigen), FITC (for CD81), and merged using immunofluorescence staining and deconvolution microscopy to examine changes in the cellular localization of tetraspanins during maturation and HIV infection (x400) (B) . Osteoclasts and their precursors at 6 dpi of HIV infection with the low-inoculum showing CD81 expression (green) and HIV-infected giant multinuclear cells (red, with nuclei in blue). (C) Yellow arrows show perinuclear structures resembling viral-containing compartments (VCC). Scale bars: 20 μm. *<0.05 indicates a statistically significant difference.

Article Snippet: On day 9 post-seeding cells were fixed with PFA 4% for 10 min at room temperature and were first incubated with mouse anti-human CD81 primary antibody (cat555675, BD Biosciences, United States) diluted in Perm Wash (cat554723, BD Biosciences, United States) for 60 min at 4°C, and then with Alexa Fluor 488 goat anti-mouse IgG H&L secondary antibody (ab150117) for 45 min at 4°C.

Techniques: Expressing, Infection, Flow Cytometry, Fluorescence, Staining, Immunofluorescence, Microscopy