1.7-256 plane grating spectrometer Search Results


anti sqrdl novus  (Proteintech)
94
Proteintech anti sqrdl novus
Restricted changes in the brain mitochondrial proteome induced by Parl deficiency explain the Complex III and CoQ defects ( A ) Volcano plot showing differentially regulated proteins in Parl -/- brain mitochondria. purified from 5 week-old WT and Parl -/- brains (n=3) analyzed by mass spectrometry. Significantly differentially regulated proteins are distributed outside the volcano cutoff of fold changes >2 and p value <0.05. Significantly differentially expressed mitochondrial proteins are plotted in red. Previously reported Parl substrates that did not reach statistical significance are plotted in black. The non-mitochondrial proteins Trabd, Bcap31, Bcan, Eif1a, and Setdb, appeared similarly expressed as from the validation experiment in Fig.5B and therefore were not included in the graph. ( B ) Validation of the mass spectrometry results and of previously reported Parl substrates <t>Stard7,</t> <t>Clpb,</t> Htra2, Opa1. Twenty μg of mitochondria isolated from brain of WT, Parl -/- , and Parl Nes-Cre , were analyzed by SDS page followed by immunoblotting. The white arrows indicate the mature (processed) form of the protein, the black arrows indicate unprocessed forms, the grey arrows indicate alternatively processed forms in Parl -/- mitochondria. The asterisk indicates bands of uncertain significance. ( C ) Time course of the protein expression of Ttc19, CoQ biosynthesis proteins and <t>Sqrdl</t> in WT and Parl -/- brains. 20 μg of total brain lysates from WT, Parl -/- sacrificed at 1, 3, 5, and 7 weeks of age (n=3), were analyzed by SDS page followed by immunoblotting. The graph bars indicate the quantifications of the western blot results, normalized with the loading control Hsp60 and expressed as % relative to the WT. The original western blots are shown in SI Appendix , Fig.S5. ( D ) Generation of Ttc19 -/- mice by Crisper/Cas9 technology. Ttc19 -/- mice have a 5 base pairs deletion in the first exon. ( E ) Immunoblot analysis of brain and muscle mitochondria (20 μg) with anti Ttc19 and anti Coq4 antibodies. Hsp60 is the loading control. ( F ) Concentration of total CoQ Q (Q 9 +Q 10 ) were measured by HPLC in brain tissue from7 weeks old WT and Ttc19 -/- mice (n=5 for each genotype). ( G ) Ratio between reduced and oxidized CoQ from 7 weeks old WT and Ttc19 -/- mice from the experiment in F. The bar graphs indicate the average ± SD. Statistical significance has been calculated by two sided student t test: ****=p<0,0001.
Anti Sqrdl Novus, supplied by Proteintech, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/1%2E7-256+plane+grating+spectrometer/SQRDL+Antibody/bio_rxiv__368654-276-83-86
Average 94 stars, based on 1 article reviews
anti sqrdl novus - by Bioz Stars, 2026-10
94/100 stars
  Buy from Supplier

Image Search Results


Restricted changes in the brain mitochondrial proteome induced by Parl deficiency explain the Complex III and CoQ defects ( A ) Volcano plot showing differentially regulated proteins in Parl -/- brain mitochondria. purified from 5 week-old WT and Parl -/- brains (n=3) analyzed by mass spectrometry. Significantly differentially regulated proteins are distributed outside the volcano cutoff of fold changes >2 and p value <0.05. Significantly differentially expressed mitochondrial proteins are plotted in red. Previously reported Parl substrates that did not reach statistical significance are plotted in black. The non-mitochondrial proteins Trabd, Bcap31, Bcan, Eif1a, and Setdb, appeared similarly expressed as from the validation experiment in Fig.5B and therefore were not included in the graph. ( B ) Validation of the mass spectrometry results and of previously reported Parl substrates Stard7, Clpb, Htra2, Opa1. Twenty μg of mitochondria isolated from brain of WT, Parl -/- , and Parl Nes-Cre , were analyzed by SDS page followed by immunoblotting. The white arrows indicate the mature (processed) form of the protein, the black arrows indicate unprocessed forms, the grey arrows indicate alternatively processed forms in Parl -/- mitochondria. The asterisk indicates bands of uncertain significance. ( C ) Time course of the protein expression of Ttc19, CoQ biosynthesis proteins and Sqrdl in WT and Parl -/- brains. 20 μg of total brain lysates from WT, Parl -/- sacrificed at 1, 3, 5, and 7 weeks of age (n=3), were analyzed by SDS page followed by immunoblotting. The graph bars indicate the quantifications of the western blot results, normalized with the loading control Hsp60 and expressed as % relative to the WT. The original western blots are shown in SI Appendix , Fig.S5. ( D ) Generation of Ttc19 -/- mice by Crisper/Cas9 technology. Ttc19 -/- mice have a 5 base pairs deletion in the first exon. ( E ) Immunoblot analysis of brain and muscle mitochondria (20 μg) with anti Ttc19 and anti Coq4 antibodies. Hsp60 is the loading control. ( F ) Concentration of total CoQ Q (Q 9 +Q 10 ) were measured by HPLC in brain tissue from7 weeks old WT and Ttc19 -/- mice (n=5 for each genotype). ( G ) Ratio between reduced and oxidized CoQ from 7 weeks old WT and Ttc19 -/- mice from the experiment in F. The bar graphs indicate the average ± SD. Statistical significance has been calculated by two sided student t test: ****=p<0,0001.

Journal: bioRxiv

Article Title: Parl Deficiency in Mouse Causes Coenzyme Q Depletion, Complex III Defects, and Leigh-like Syndrome

doi: 10.1101/368654

Figure Lengend Snippet: Restricted changes in the brain mitochondrial proteome induced by Parl deficiency explain the Complex III and CoQ defects ( A ) Volcano plot showing differentially regulated proteins in Parl -/- brain mitochondria. purified from 5 week-old WT and Parl -/- brains (n=3) analyzed by mass spectrometry. Significantly differentially regulated proteins are distributed outside the volcano cutoff of fold changes >2 and p value <0.05. Significantly differentially expressed mitochondrial proteins are plotted in red. Previously reported Parl substrates that did not reach statistical significance are plotted in black. The non-mitochondrial proteins Trabd, Bcap31, Bcan, Eif1a, and Setdb, appeared similarly expressed as from the validation experiment in Fig.5B and therefore were not included in the graph. ( B ) Validation of the mass spectrometry results and of previously reported Parl substrates Stard7, Clpb, Htra2, Opa1. Twenty μg of mitochondria isolated from brain of WT, Parl -/- , and Parl Nes-Cre , were analyzed by SDS page followed by immunoblotting. The white arrows indicate the mature (processed) form of the protein, the black arrows indicate unprocessed forms, the grey arrows indicate alternatively processed forms in Parl -/- mitochondria. The asterisk indicates bands of uncertain significance. ( C ) Time course of the protein expression of Ttc19, CoQ biosynthesis proteins and Sqrdl in WT and Parl -/- brains. 20 μg of total brain lysates from WT, Parl -/- sacrificed at 1, 3, 5, and 7 weeks of age (n=3), were analyzed by SDS page followed by immunoblotting. The graph bars indicate the quantifications of the western blot results, normalized with the loading control Hsp60 and expressed as % relative to the WT. The original western blots are shown in SI Appendix , Fig.S5. ( D ) Generation of Ttc19 -/- mice by Crisper/Cas9 technology. Ttc19 -/- mice have a 5 base pairs deletion in the first exon. ( E ) Immunoblot analysis of brain and muscle mitochondria (20 μg) with anti Ttc19 and anti Coq4 antibodies. Hsp60 is the loading control. ( F ) Concentration of total CoQ Q (Q 9 +Q 10 ) were measured by HPLC in brain tissue from7 weeks old WT and Ttc19 -/- mice (n=5 for each genotype). ( G ) Ratio between reduced and oxidized CoQ from 7 weeks old WT and Ttc19 -/- mice from the experiment in F. The bar graphs indicate the average ± SD. Statistical significance has been calculated by two sided student t test: ****=p<0,0001.

Article Snippet: The following commercial available antibodies were employed: anti GFAP, Agilent (DAKO), anti IBA1 (WAKO), anti NeuN (EMD Millipore), anti-Ndufs3 (Abcam), anti-Cytocrome c (BD Phamingen), anti-Aif1 (Santa Cruz), anti-Tubulin (Abcam), anti-Caspase 3 (Cell Signaling), anti activated caspase 3 (Cell signaling), anti-Parp1 (Cell Signaling), anti-Actin (Sigma), anti-Hsp60 (BD Biosciences), ant-Uqcrfs1 (Abcam), anti-Cox4 (Abcam), anti-Sdh (Abcam), anti-Atpb (Abcam), anti-Tomm20 (Santa Cruz), anti-Vdac1 (Abcam), anti-Pink1 (Cayman), anti-Pgam5 (Sigma), anti-Ttc19 (Sigma), anti-Coq3 (Santa Cruz), anti-Coq4 (Proteintech), anti-Coq5 (Proteintech), anti-Coq6 (Proteintech), anti-Coq7 (Santa Cruz), anti-Coq9 (Santa-Cruz), anti-PDSS2 (Santa Cruz), anti-Sqrdl (Novus), anti-Ghitm (Proteintech), anti-Clpb (Proteintech), anti-Stard7 (Proteintech), anti-Smac/Diablo (Cell Signaling), anti Htra2 (R&D system), anti-Opa1 (BD Biosciences).

Techniques: Purification, Mass Spectrometry, Isolation, SDS Page, Western Blot, Expressing, Concentration Assay