serine Search Results


elastase  (Athens Research)
94
Athens Research elastase
Elastase, supplied by Athens Research, 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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o benzyl d serine  (Chem Impex International)
95
Chem Impex International o benzyl d serine
O Benzyl D Serine, 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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anti tmprss2  (Proteintech)
93
Proteintech anti tmprss2
Anti Tmprss2, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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ripk1  (Boster Bio)
93
Boster Bio ripk1
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csbyp023924hu  (Cusabio)
93
Cusabio csbyp023924hu
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recombinant protein c inhibitor  (MedChemExpress)
93
MedChemExpress recombinant protein c inhibitor
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met  (Proteintech)
93
Proteintech met
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shmt2  (Proteintech)
93
Proteintech shmt2
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lonp1  (Proteintech)
95
Proteintech lonp1
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anti pai 1 polyclonal antibody  (Boster Bio)
93
Boster Bio anti pai 1 polyclonal antibody
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serine racemase  (Santa Cruz Biotechnology)
93
Santa Cruz Biotechnology serine racemase
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polyclonal rabbit anti ryr2 phospho serine 2808  (Alomone Labs)
90
Alomone Labs polyclonal rabbit anti ryr2 phospho serine 2808
Structural changes consequent to PKP2 deletion. a STORM-acquired images of Cav1.2 ( green ) and <t>RyR2</t> ( purple ) in a single myocyte. b Analysis of RyR2/Cav1.2 overlapping area in transverse ( left ) and longitudinal ( right ) clusters. n = 1335 and 1285 clusters from 30 control and 25 PKP2-cKO cardiomyocytes at 21 dpi, respectively. t -test, * p < 0.05 and ** p < 0.01 vs. control. c 2D-EM image of PKP2-cKO ventricular tissue at 21 dpi showing a dyadic structure. Scale bar = 200 nm. d Boundaries of the jSR ( red ) and T-tubule ( blue ) membranes, detected from the dyad in the dotted square in c . e Acquisition of distances from each point in the T-tuble membrane to its closest neighbor in the jSR ( green lines ). f Close-up of the region inside the dashed square in e . All distances measured within a dyad were averaged to obtain the “average distance” for that dyad (expressed in nm). g Comparison of average data collected from one control ( n = 30 dyads) and 2 PKP2-cKO 21 dpi samples ( n = 41 dyads for both). Student’s t -test * p < 0.001 vs. control. h Spatial orientation of the T-tubular network, obtained from segmentation and analysis of a volume of 15 × 12 × 0.8 µm 3 dimensions obtained by Serial Block-Face Scanning Electron Microscopy analysis. See also Supplementary Video and “Methods”. The angle of the T-tubular skeleton is color-coded ( bottom left ) from −90° in magenta to +90° in red ; relative to the longitudinal axis of the cell ( light blue ; 0°). i Histogram of orientations (from h ), showing a strong preference for zero-degree orientation, as expected from a non-failing heart (see ref. )
Polyclonal Rabbit Anti Ryr2 Phospho Serine 2808, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


Structural changes consequent to PKP2 deletion. a STORM-acquired images of Cav1.2 ( green ) and RyR2 ( purple ) in a single myocyte. b Analysis of RyR2/Cav1.2 overlapping area in transverse ( left ) and longitudinal ( right ) clusters. n = 1335 and 1285 clusters from 30 control and 25 PKP2-cKO cardiomyocytes at 21 dpi, respectively. t -test, * p < 0.05 and ** p < 0.01 vs. control. c 2D-EM image of PKP2-cKO ventricular tissue at 21 dpi showing a dyadic structure. Scale bar = 200 nm. d Boundaries of the jSR ( red ) and T-tubule ( blue ) membranes, detected from the dyad in the dotted square in c . e Acquisition of distances from each point in the T-tuble membrane to its closest neighbor in the jSR ( green lines ). f Close-up of the region inside the dashed square in e . All distances measured within a dyad were averaged to obtain the “average distance” for that dyad (expressed in nm). g Comparison of average data collected from one control ( n = 30 dyads) and 2 PKP2-cKO 21 dpi samples ( n = 41 dyads for both). Student’s t -test * p < 0.001 vs. control. h Spatial orientation of the T-tubular network, obtained from segmentation and analysis of a volume of 15 × 12 × 0.8 µm 3 dimensions obtained by Serial Block-Face Scanning Electron Microscopy analysis. See also Supplementary Video and “Methods”. The angle of the T-tubular skeleton is color-coded ( bottom left ) from −90° in magenta to +90° in red ; relative to the longitudinal axis of the cell ( light blue ; 0°). i Histogram of orientations (from h ), showing a strong preference for zero-degree orientation, as expected from a non-failing heart (see ref. )

Journal: Nature Communications

Article Title: Plakophilin-2 is required for transcription of genes that control calcium cycling and cardiac rhythm

doi: 10.1038/s41467-017-00127-0

Figure Lengend Snippet: Structural changes consequent to PKP2 deletion. a STORM-acquired images of Cav1.2 ( green ) and RyR2 ( purple ) in a single myocyte. b Analysis of RyR2/Cav1.2 overlapping area in transverse ( left ) and longitudinal ( right ) clusters. n = 1335 and 1285 clusters from 30 control and 25 PKP2-cKO cardiomyocytes at 21 dpi, respectively. t -test, * p < 0.05 and ** p < 0.01 vs. control. c 2D-EM image of PKP2-cKO ventricular tissue at 21 dpi showing a dyadic structure. Scale bar = 200 nm. d Boundaries of the jSR ( red ) and T-tubule ( blue ) membranes, detected from the dyad in the dotted square in c . e Acquisition of distances from each point in the T-tuble membrane to its closest neighbor in the jSR ( green lines ). f Close-up of the region inside the dashed square in e . All distances measured within a dyad were averaged to obtain the “average distance” for that dyad (expressed in nm). g Comparison of average data collected from one control ( n = 30 dyads) and 2 PKP2-cKO 21 dpi samples ( n = 41 dyads for both). Student’s t -test * p < 0.001 vs. control. h Spatial orientation of the T-tubular network, obtained from segmentation and analysis of a volume of 15 × 12 × 0.8 µm 3 dimensions obtained by Serial Block-Face Scanning Electron Microscopy analysis. See also Supplementary Video and “Methods”. The angle of the T-tubular skeleton is color-coded ( bottom left ) from −90° in magenta to +90° in red ; relative to the longitudinal axis of the cell ( light blue ; 0°). i Histogram of orientations (from h ), showing a strong preference for zero-degree orientation, as expected from a non-failing heart (see ref. )

Article Snippet: The following primary antibodies were used: monoclonal mouse anti-PKP2 (K44262M; Biodesign International, Meridian Life Sciences), monoclonal mouse anti-AnkyrinB (N105-17; BioLegend), polyclonal rabbit anti-Cav1.2 (ACC-003; Alomone), polyclonal rabbit anti-CASQ2 (PA1-913; ThermoFisher), monoclonal mouse anti-RyR2 (MA3-916; ThermoFisher), polyclonal rabbit anti-RyR2 phospho serine-2808 and anti-RyR2 phospho serine-2814 (A010-30 and A010-31 respectively; Badrilla), monoclonal mouse anti-TriadinT32 (MA3-927; ThermoFisher), polyclonal rabbit anti-NCX (sc-32881, SantaCruz), polyclonal rabbit anti-SERCA2 (PA5-29380; ThermoFisher), monoclonal mouse anti-phospholamban (sc-393990; SantaCruz), polyclonal rabbit anti-phospholamban phospho serine-16 (sc-12963; SantaCruz) and phospho threonine-17 (sc-17024; SantaCruz), GAPDH (G109A; Fitzerald) monoclonal mouse anti-Cx43 (Clone 4E6.2, Millipore), polyclonal rabbit anti-β-catenin (C2206; Sigma), monoclonal mouse anti-JPH2 (sc-37086, SantaCruz), monoclonal mouse anti-Bin1 (Clone 99D; Sigma), polyclonal rabbit anti-PKC and anti-phospho PKC (#2056 and #9375; Cell Signaling), polyclonal rabbit anti-CaMKII (PA5-22168; ThermoFisher), monoclonal mouse anti-CaMKII phospho threonine-286 (MA1-047; ThermoFisher), polyclonal rabbit Desmocollin-2 (ab72792; Abcam), polyclonal rabbit anti-Nav1.5 (S0819; Sigma).

Techniques: Control, Membrane, Comparison, Blocking Assay, Electron Microscopy