fttc anti–rat cd3 antibody Search Results


th17 cell staining kit fttc-anti-mouse-cd3e  (Becton Dickinson)
90
Becton Dickinson th17 cell staining kit fttc-anti-mouse-cd3e
Each group hepatic tissues Treg, <t> Th17 </t> cell levels (%).
Th17 Cell Staining Kit Fttc Anti Mouse Cd3e, 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/fttc+anti%E2%80%93rat+cd3+antibody/cytofix+cytoperm/pmc04419233-80-1-22
Average 90 stars, based on 1 article reviews
th17 cell staining kit fttc-anti-mouse-cd3e - by Bioz Stars, 2026-09
90/100 stars
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anti acetylated lysine antibody  (Cell Signaling Technology Inc)
96
Cell Signaling Technology Inc anti acetylated lysine antibody
MK-STYX decreases the phosphorylation of HDAC6. ( A ) Twenty-four hours post-transfection cells were serum starved (− serum) or not (+ serum), lysed 24 h thereafter, and immunoblotted. Anti-phospho-HDAC6 antibody showed that MK-STYX decreased HDAC6 phosphorylation in non-serum starved cells relative to the cells overexpressing green fluorescence protein (GFP). However, MK-STYX increased HDAC6 phosphorylation in cells depleted of serum relative to GFP-expressing cells. These blots were stripped and probed for HDAC6 as a loading control. The blot was also stripped and probed with anti-GFP antibody to detect GFP (~27 kDa) or anti-STYXL1 (MK-STYX). Anti-STYXL1 antibody showed overexpressed GFP-MK-STYX (~67 kDa; indicated by the black arrow) relative to GFP (control vector) and non-transfected cells to confirm transfection. Three biologically independent replicate experiments were performed. ( B ) Samples were also used to detect effects of MK-STYX on tyrosine phosphorylation of proteins in the presence and absence of serum with the anti-phosphotyrosine antibody (clone 4G10). Cells expressing GFP-MK-STYX showed decreased phosphorylation relative to the controls in the presence of serum. The blot was stripped and probed with anti-GADPH (glyceraldehyde-3-diphosphatedehydrogenase; 37 kDa) antibody for a loading control. ( C ) Samples were also analyzed for acetylation with anti-lysine acetylation antibody to determine any effects of MK-STYX on <t>acetylated</t> proteins. In the presence or absence of serum, acetylation was decreased in cells expressing MK-STYX relative to control cells. The blot was stripped and probed with anti-GAPDH for a loading control. Three biologically independent replicates were performed.
Anti Acetylated Lysine Antibody, supplied by Cell Signaling Technology Inc, 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/fttc+anti%E2%80%93rat+cd3+antibody/Acetylated-Lysine+Antibody/pmc06470616-133-35-37
Average 96 stars, based on 1 article reviews
anti acetylated lysine antibody - by Bioz Stars, 2026-09
96/100 stars
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anti gapdh  (Cell Signaling Technology Inc)
99
Cell Signaling Technology Inc anti gapdh
MK-STYX decreases the phosphorylation of HDAC6. ( A ) Twenty-four hours post-transfection cells were serum starved (− serum) or not (+ serum), lysed 24 h thereafter, and immunoblotted. Anti-phospho-HDAC6 antibody showed that MK-STYX decreased HDAC6 phosphorylation in non-serum starved cells relative to the cells overexpressing green fluorescence protein (GFP). However, MK-STYX increased HDAC6 phosphorylation in cells depleted of serum relative to GFP-expressing cells. These blots were stripped and probed for HDAC6 as a loading control. The blot was also stripped and probed with anti-GFP antibody to detect GFP (~27 kDa) or anti-STYXL1 (MK-STYX). Anti-STYXL1 antibody showed overexpressed GFP-MK-STYX (~67 kDa; indicated by the black arrow) relative to GFP (control vector) and non-transfected cells to confirm transfection. Three biologically independent replicate experiments were performed. ( B ) Samples were also used to detect effects of MK-STYX on tyrosine phosphorylation of proteins in the presence and absence of serum with the anti-phosphotyrosine antibody (clone 4G10). Cells expressing GFP-MK-STYX showed decreased phosphorylation relative to the controls in the presence of serum. The blot was stripped and probed with anti-GADPH (glyceraldehyde-3-diphosphatedehydrogenase; 37 kDa) antibody for a loading control. ( C ) Samples were also analyzed for acetylation with anti-lysine acetylation antibody to determine any effects of MK-STYX on <t>acetylated</t> proteins. In the presence or absence of serum, acetylation was decreased in cells expressing MK-STYX relative to control cells. The blot was stripped and probed with anti-GAPDH for a loading control. Three biologically independent replicates were performed.
Anti Gapdh, supplied by Cell Signaling Technology Inc, 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/fttc+anti%E2%80%93rat+cd3+antibody/GAPDH+XP+Rabbit+mAb/pmc06470616-133-80-81
Average 99 stars, based on 1 article reviews
anti gapdh - by Bioz Stars, 2026-09
99/100 stars
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rabbit monoclonal cell signaling technology  (Cell Signaling Technology Inc)
95
Cell Signaling Technology Inc rabbit monoclonal cell signaling technology
MK-STYX decreases the phosphorylation of HDAC6. ( A ) Twenty-four hours post-transfection cells were serum starved (− serum) or not (+ serum), lysed 24 h thereafter, and immunoblotted. Anti-phospho-HDAC6 antibody showed that MK-STYX decreased HDAC6 phosphorylation in non-serum starved cells relative to the cells overexpressing green fluorescence protein (GFP). However, MK-STYX increased HDAC6 phosphorylation in cells depleted of serum relative to GFP-expressing cells. These blots were stripped and probed for HDAC6 as a loading control. The blot was also stripped and probed with anti-GFP antibody to detect GFP (~27 kDa) or anti-STYXL1 (MK-STYX). Anti-STYXL1 antibody showed overexpressed GFP-MK-STYX (~67 kDa; indicated by the black arrow) relative to GFP (control vector) and non-transfected cells to confirm transfection. Three biologically independent replicate experiments were performed. ( B ) Samples were also used to detect effects of MK-STYX on tyrosine phosphorylation of proteins in the presence and absence of serum with the anti-phosphotyrosine antibody (clone 4G10). Cells expressing GFP-MK-STYX showed decreased phosphorylation relative to the controls in the presence of serum. The blot was stripped and probed with anti-GADPH (glyceraldehyde-3-diphosphatedehydrogenase; 37 kDa) antibody for a loading control. ( C ) Samples were also analyzed for acetylation with anti-lysine acetylation antibody to determine any effects of MK-STYX on <t>acetylated</t> proteins. In the presence or absence of serum, acetylation was decreased in cells expressing MK-STYX relative to control cells. The blot was stripped and probed with anti-GAPDH for a loading control. Three biologically independent replicates were performed.
Rabbit Monoclonal Cell Signaling Technology, supplied by Cell Signaling Technology Inc, 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/fttc+anti%E2%80%93rat+cd3+antibody/Tau+XP+Rabbit+mAb/10__7554_slash_elife__44219-412-170-172
Average 95 stars, based on 1 article reviews
rabbit monoclonal cell signaling technology - by Bioz Stars, 2026-09
95/100 stars
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Image Search Results


Each group hepatic tissues Treg, Th17 cell levels (%).

Journal: Evidence-based Complementary and Alternative Medicine : eCAM

Article Title: Chinese Medicine Bu Xu Hua Yu Recipe for the Regulation of Treg/Th17 Ratio Imbalance in Autoimmune Hepatitis

doi: 10.1155/2015/461294

Figure Lengend Snippet: Each group hepatic tissues Treg, Th17 cell levels (%).

Article Snippet: The Th17 cell staining kit (PE Rat Anti-Mouse IL-17A, APC IFN- γ Anti-Mouse, FTTC-anti-mouse-CD3e, and PerCP Rat Anti-Mouse CD4) was obtained from BD Company.

Techniques:

Treg/Th17 cell ratio for each group.

Journal: Evidence-based Complementary and Alternative Medicine : eCAM

Article Title: Chinese Medicine Bu Xu Hua Yu Recipe for the Regulation of Treg/Th17 Ratio Imbalance in Autoimmune Hepatitis

doi: 10.1155/2015/461294

Figure Lengend Snippet: Treg/Th17 cell ratio for each group.

Article Snippet: The Th17 cell staining kit (PE Rat Anti-Mouse IL-17A, APC IFN- γ Anti-Mouse, FTTC-anti-mouse-CD3e, and PerCP Rat Anti-Mouse CD4) was obtained from BD Company.

Techniques:

The percentage of Th17 cells and Treg cells and the ratio of the two types of cells.

Journal: Evidence-based Complementary and Alternative Medicine : eCAM

Article Title: Chinese Medicine Bu Xu Hua Yu Recipe for the Regulation of Treg/Th17 Ratio Imbalance in Autoimmune Hepatitis

doi: 10.1155/2015/461294

Figure Lengend Snippet: The percentage of Th17 cells and Treg cells and the ratio of the two types of cells.

Article Snippet: The Th17 cell staining kit (PE Rat Anti-Mouse IL-17A, APC IFN- γ Anti-Mouse, FTTC-anti-mouse-CD3e, and PerCP Rat Anti-Mouse CD4) was obtained from BD Company.

Techniques:

MK-STYX decreases the phosphorylation of HDAC6. ( A ) Twenty-four hours post-transfection cells were serum starved (− serum) or not (+ serum), lysed 24 h thereafter, and immunoblotted. Anti-phospho-HDAC6 antibody showed that MK-STYX decreased HDAC6 phosphorylation in non-serum starved cells relative to the cells overexpressing green fluorescence protein (GFP). However, MK-STYX increased HDAC6 phosphorylation in cells depleted of serum relative to GFP-expressing cells. These blots were stripped and probed for HDAC6 as a loading control. The blot was also stripped and probed with anti-GFP antibody to detect GFP (~27 kDa) or anti-STYXL1 (MK-STYX). Anti-STYXL1 antibody showed overexpressed GFP-MK-STYX (~67 kDa; indicated by the black arrow) relative to GFP (control vector) and non-transfected cells to confirm transfection. Three biologically independent replicate experiments were performed. ( B ) Samples were also used to detect effects of MK-STYX on tyrosine phosphorylation of proteins in the presence and absence of serum with the anti-phosphotyrosine antibody (clone 4G10). Cells expressing GFP-MK-STYX showed decreased phosphorylation relative to the controls in the presence of serum. The blot was stripped and probed with anti-GADPH (glyceraldehyde-3-diphosphatedehydrogenase; 37 kDa) antibody for a loading control. ( C ) Samples were also analyzed for acetylation with anti-lysine acetylation antibody to determine any effects of MK-STYX on acetylated proteins. In the presence or absence of serum, acetylation was decreased in cells expressing MK-STYX relative to control cells. The blot was stripped and probed with anti-GAPDH for a loading control. Three biologically independent replicates were performed.

Journal: International Journal of Molecular Sciences

Article Title: Pseudophosphatase MK-STYX Alters Histone Deacetylase 6 Cytoplasmic Localization, Decreases Its Phosphorylation, and Increases Detyrosination of Tubulin

doi: 10.3390/ijms20061455

Figure Lengend Snippet: MK-STYX decreases the phosphorylation of HDAC6. ( A ) Twenty-four hours post-transfection cells were serum starved (− serum) or not (+ serum), lysed 24 h thereafter, and immunoblotted. Anti-phospho-HDAC6 antibody showed that MK-STYX decreased HDAC6 phosphorylation in non-serum starved cells relative to the cells overexpressing green fluorescence protein (GFP). However, MK-STYX increased HDAC6 phosphorylation in cells depleted of serum relative to GFP-expressing cells. These blots were stripped and probed for HDAC6 as a loading control. The blot was also stripped and probed with anti-GFP antibody to detect GFP (~27 kDa) or anti-STYXL1 (MK-STYX). Anti-STYXL1 antibody showed overexpressed GFP-MK-STYX (~67 kDa; indicated by the black arrow) relative to GFP (control vector) and non-transfected cells to confirm transfection. Three biologically independent replicate experiments were performed. ( B ) Samples were also used to detect effects of MK-STYX on tyrosine phosphorylation of proteins in the presence and absence of serum with the anti-phosphotyrosine antibody (clone 4G10). Cells expressing GFP-MK-STYX showed decreased phosphorylation relative to the controls in the presence of serum. The blot was stripped and probed with anti-GADPH (glyceraldehyde-3-diphosphatedehydrogenase; 37 kDa) antibody for a loading control. ( C ) Samples were also analyzed for acetylation with anti-lysine acetylation antibody to determine any effects of MK-STYX on acetylated proteins. In the presence or absence of serum, acetylation was decreased in cells expressing MK-STYX relative to control cells. The blot was stripped and probed with anti-GAPDH for a loading control. Three biologically independent replicates were performed.

Article Snippet: The following antibodies were used: Anti-phospho-HDAC6 (pSer22) antibody (Sigma-Aldrich, Burlington, MA, USA; SAB4504190;); anti-HDAC6 (Cell Signaling, Danvers, MA, USA; 7558); anti-GFP antibody (Thermo Fisher, Grand Island, NY, USA c; MA5-15256); anti-phosphotyrosine, clone 4G10 (Millipore; 05-321); anti-acetylated-lysine antibody (Cell Signaling; 9441); anti-STYXL1 antibody (Sigma-Aldrich; S9823); anti-β-tubulin polyclonal antibody (Thermo Fisher; PA1-21153); monoclonal acetylated microtubule antibody (Sigma, Burlington, MA, USA; T7451); anti-tubulin, detyrosinated antibody (Sigma; AB3201); anti-monoclonal anti-mCherry antibody (SAB2702291); monoclonal anti-FLAG M2-FTTC, Clone M2 antibody (Sigma-Aldrich; F4049); monoclonal anti-β-tubulin-FITC (Sigma-Aldrich; F2043); anti-GAPDH (Cell Signaling; 5174).

Techniques: Phospho-proteomics, Transfection, Fluorescence, Expressing, Control, Plasmid Preparation

MK-STYX increases acetylated and detyrosinated tubulin. Cells were transfected with expression plasmids for mCherry or mCherry-MK-STYX. Twenty-four hours post-transfection, cells treated with nocodazole or not were lysed and analyzed by immunoblotting. We examined cells expressing mCherry constructs by fluorescence microscopy to confirm transfection. ( A ) Blots were probed with anti-acetylated tubulin and showed that acetylated tubulin (55 kDa) is significantly decreased (paired t -test; p < 0.05) in the presence of nocodazole in control cells (mCherry-expressing) relative to cells expressing mCherry-MK-STYX. Cells overexpressing MK-STYX sustain acetylated tubulin in the presence of nocodazole. The blots were stripped and probed for tubulin as the loading control; they were also stripped and probed with anti-mCherry to confirm expression of mCherry (27 kDa) and mCherry-MK-STYX (67 kDa). ( B ) Lysates were also analyzed for detyrosinated tubulin (55 kDa) by detection with anti-detyrosinated tubulin. A significant increase (paired t -test; p < 0.05) in detyrosinated tubulin was observed in mCherry-MK-STYX-expressing cells in the absence of nocodazole, whereas detyrosination was decreased in cells expressing mCherry-MK-STYX in the presence of nocodazole. Blots were stripped and probed with anti-tubulin antibody for a loading control, then stripped a second time and probed with anti-mCherry antibody to confirm transfection. The error bars are ±SEM; three biologically independent replicate experiments were performed.

Journal: International Journal of Molecular Sciences

Article Title: Pseudophosphatase MK-STYX Alters Histone Deacetylase 6 Cytoplasmic Localization, Decreases Its Phosphorylation, and Increases Detyrosination of Tubulin

doi: 10.3390/ijms20061455

Figure Lengend Snippet: MK-STYX increases acetylated and detyrosinated tubulin. Cells were transfected with expression plasmids for mCherry or mCherry-MK-STYX. Twenty-four hours post-transfection, cells treated with nocodazole or not were lysed and analyzed by immunoblotting. We examined cells expressing mCherry constructs by fluorescence microscopy to confirm transfection. ( A ) Blots were probed with anti-acetylated tubulin and showed that acetylated tubulin (55 kDa) is significantly decreased (paired t -test; p < 0.05) in the presence of nocodazole in control cells (mCherry-expressing) relative to cells expressing mCherry-MK-STYX. Cells overexpressing MK-STYX sustain acetylated tubulin in the presence of nocodazole. The blots were stripped and probed for tubulin as the loading control; they were also stripped and probed with anti-mCherry to confirm expression of mCherry (27 kDa) and mCherry-MK-STYX (67 kDa). ( B ) Lysates were also analyzed for detyrosinated tubulin (55 kDa) by detection with anti-detyrosinated tubulin. A significant increase (paired t -test; p < 0.05) in detyrosinated tubulin was observed in mCherry-MK-STYX-expressing cells in the absence of nocodazole, whereas detyrosination was decreased in cells expressing mCherry-MK-STYX in the presence of nocodazole. Blots were stripped and probed with anti-tubulin antibody for a loading control, then stripped a second time and probed with anti-mCherry antibody to confirm transfection. The error bars are ±SEM; three biologically independent replicate experiments were performed.

Article Snippet: The following antibodies were used: Anti-phospho-HDAC6 (pSer22) antibody (Sigma-Aldrich, Burlington, MA, USA; SAB4504190;); anti-HDAC6 (Cell Signaling, Danvers, MA, USA; 7558); anti-GFP antibody (Thermo Fisher, Grand Island, NY, USA c; MA5-15256); anti-phosphotyrosine, clone 4G10 (Millipore; 05-321); anti-acetylated-lysine antibody (Cell Signaling; 9441); anti-STYXL1 antibody (Sigma-Aldrich; S9823); anti-β-tubulin polyclonal antibody (Thermo Fisher; PA1-21153); monoclonal acetylated microtubule antibody (Sigma, Burlington, MA, USA; T7451); anti-tubulin, detyrosinated antibody (Sigma; AB3201); anti-monoclonal anti-mCherry antibody (SAB2702291); monoclonal anti-FLAG M2-FTTC, Clone M2 antibody (Sigma-Aldrich; F4049); monoclonal anti-β-tubulin-FITC (Sigma-Aldrich; F2043); anti-GAPDH (Cell Signaling; 5174).

Techniques: Transfection, Expressing, Western Blot, Construct, Fluorescence, Microscopy, Control