diffuse reflectance infrared spectroscopy tensor 27 Search Results


alox15a trilencer 27  (OriGene)
90
OriGene alox15a trilencer 27
AKBA elevates 12/15‐LOX products involving 15‐LOX‐1 in M2‐MDM. A,B) MDMs (2 × 10 6 cells mL −1 ) differentiated from human monocytes for 6 days with M‐CSF were transfected with non‐target or <t>ALOX15A</t> siRNA during polarization with IL‐4 (20 ng mL −1 ) for 48 h. A) Western blot analysis of 15‐LOX‐1; β ‐actin served as reference protein for normalization after densitometric analysis, n = 4; Student´s unpaired t ‐test. B) LM profile of ALOX15A siRNA‐treated M2‐MDMs after exposure to AKBA (10 µ m ) for 180 min, n = 4. Data are shown as bubble blot in % of non‐target siRNA of LM summarized in groups: 12/15‐LOX products include 17‐HDHA, 15‐HETE, 15‐HEPE, 14‐HDHA, 12‐HETE, and 12‐HEPE; SPM include PD1, PDX, RvD2, RvD5, and MaR1; 5‐LOX products include t‐LTB 4 , LTB 4 , 5‐HETE, and 5‐HEPE; COX products include PGE 2 , PGD 2 , TXB 2 , and PGF 2 α ; PUFA include AA, EPA, and DHA. C) Kinetic of LM formation in M2‐MDMs after incubation with 10 µ m AKBA or 2.5 µ m A23187 in the presence of AA, EPA, and DHA (1 µ m each). After the indicated time points, formed LM were isolated from the supernatants by SPE and analyzed by UPLC‐MS‐/MS. Data are shown as means ± S.E.M. given in pg/2 × 10 6 cells for representative SPM and for the sum of 5‐LOX products, including t‐LTB 4 , LTB 4 , 5‐HETE, and 5‐HEPE; n = 3 separate donors. D) Subcellular redistribution of 5‐LOX and 15‐LOX‐1 in M2‐MDMs after exposure to AKBA (10 µ m ) or A23187 (2.5 µ m ) for indicated time points. Cells were fixed, permeabilized, and incubated with antibodies against 5‐LOX (red) and 15‐LOX‐1 (cyan‐blue); scale bar = 10 µm. Results shown for one single cell are representative for ≈100 individual cells analyzed in n = 3 independent experiments with separate donors, each. E) M2‐MDMs where co‐incubated with or without 3 µg mL −1 of DHA and EPA, each, and with AKBA (10 µ m ) or vehicle (0.1% DMSO) for 180 min at 37 °C. Formed LM were isolated from supernatants by SPE and analyzed by UPLC‐MS‐MS. Data are means ± S.E.M., given in pg/2 × 10 6 cells, n = 4 independent experiments. For statistical analysis, data were log‐transformed, one‐way analysis of variance (ANOVA) with Tukey's test, ** p < 0.01, *** p < 0.001 vehicle control versus AKBA; # p < 0.05, ## p < 0.01 vehicle + supplement versus AKBA + supplement.
Alox15a Trilencer 27, 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
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c 1h nmr spectra  (Varian Medical)
86
Varian Medical c 1h nmr spectra
AKBA elevates 12/15‐LOX products involving 15‐LOX‐1 in M2‐MDM. A,B) MDMs (2 × 10 6 cells mL −1 ) differentiated from human monocytes for 6 days with M‐CSF were transfected with non‐target or <t>ALOX15A</t> siRNA during polarization with IL‐4 (20 ng mL −1 ) for 48 h. A) Western blot analysis of 15‐LOX‐1; β ‐actin served as reference protein for normalization after densitometric analysis, n = 4; Student´s unpaired t ‐test. B) LM profile of ALOX15A siRNA‐treated M2‐MDMs after exposure to AKBA (10 µ m ) for 180 min, n = 4. Data are shown as bubble blot in % of non‐target siRNA of LM summarized in groups: 12/15‐LOX products include 17‐HDHA, 15‐HETE, 15‐HEPE, 14‐HDHA, 12‐HETE, and 12‐HEPE; SPM include PD1, PDX, RvD2, RvD5, and MaR1; 5‐LOX products include t‐LTB 4 , LTB 4 , 5‐HETE, and 5‐HEPE; COX products include PGE 2 , PGD 2 , TXB 2 , and PGF 2 α ; PUFA include AA, EPA, and DHA. C) Kinetic of LM formation in M2‐MDMs after incubation with 10 µ m AKBA or 2.5 µ m A23187 in the presence of AA, EPA, and DHA (1 µ m each). After the indicated time points, formed LM were isolated from the supernatants by SPE and analyzed by UPLC‐MS‐/MS. Data are shown as means ± S.E.M. given in pg/2 × 10 6 cells for representative SPM and for the sum of 5‐LOX products, including t‐LTB 4 , LTB 4 , 5‐HETE, and 5‐HEPE; n = 3 separate donors. D) Subcellular redistribution of 5‐LOX and 15‐LOX‐1 in M2‐MDMs after exposure to AKBA (10 µ m ) or A23187 (2.5 µ m ) for indicated time points. Cells were fixed, permeabilized, and incubated with antibodies against 5‐LOX (red) and 15‐LOX‐1 (cyan‐blue); scale bar = 10 µm. Results shown for one single cell are representative for ≈100 individual cells analyzed in n = 3 independent experiments with separate donors, each. E) M2‐MDMs where co‐incubated with or without 3 µg mL −1 of DHA and EPA, each, and with AKBA (10 µ m ) or vehicle (0.1% DMSO) for 180 min at 37 °C. Formed LM were isolated from supernatants by SPE and analyzed by UPLC‐MS‐MS. Data are means ± S.E.M., given in pg/2 × 10 6 cells, n = 4 independent experiments. For statistical analysis, data were log‐transformed, one‐way analysis of variance (ANOVA) with Tukey's test, ** p < 0.01, *** p < 0.001 vehicle control versus AKBA; # p < 0.05, ## p < 0.01 vehicle + supplement versus AKBA + supplement.
C 1h Nmr Spectra, supplied by Varian Medical, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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tg/ms/ftir system netzsch tg 209 f1 iris  (NETZSCH)
90
NETZSCH tg/ms/ftir system netzsch tg 209 f1 iris
AKBA elevates 12/15‐LOX products involving 15‐LOX‐1 in M2‐MDM. A,B) MDMs (2 × 10 6 cells mL −1 ) differentiated from human monocytes for 6 days with M‐CSF were transfected with non‐target or <t>ALOX15A</t> siRNA during polarization with IL‐4 (20 ng mL −1 ) for 48 h. A) Western blot analysis of 15‐LOX‐1; β ‐actin served as reference protein for normalization after densitometric analysis, n = 4; Student´s unpaired t ‐test. B) LM profile of ALOX15A siRNA‐treated M2‐MDMs after exposure to AKBA (10 µ m ) for 180 min, n = 4. Data are shown as bubble blot in % of non‐target siRNA of LM summarized in groups: 12/15‐LOX products include 17‐HDHA, 15‐HETE, 15‐HEPE, 14‐HDHA, 12‐HETE, and 12‐HEPE; SPM include PD1, PDX, RvD2, RvD5, and MaR1; 5‐LOX products include t‐LTB 4 , LTB 4 , 5‐HETE, and 5‐HEPE; COX products include PGE 2 , PGD 2 , TXB 2 , and PGF 2 α ; PUFA include AA, EPA, and DHA. C) Kinetic of LM formation in M2‐MDMs after incubation with 10 µ m AKBA or 2.5 µ m A23187 in the presence of AA, EPA, and DHA (1 µ m each). After the indicated time points, formed LM were isolated from the supernatants by SPE and analyzed by UPLC‐MS‐/MS. Data are shown as means ± S.E.M. given in pg/2 × 10 6 cells for representative SPM and for the sum of 5‐LOX products, including t‐LTB 4 , LTB 4 , 5‐HETE, and 5‐HEPE; n = 3 separate donors. D) Subcellular redistribution of 5‐LOX and 15‐LOX‐1 in M2‐MDMs after exposure to AKBA (10 µ m ) or A23187 (2.5 µ m ) for indicated time points. Cells were fixed, permeabilized, and incubated with antibodies against 5‐LOX (red) and 15‐LOX‐1 (cyan‐blue); scale bar = 10 µm. Results shown for one single cell are representative for ≈100 individual cells analyzed in n = 3 independent experiments with separate donors, each. E) M2‐MDMs where co‐incubated with or without 3 µg mL −1 of DHA and EPA, each, and with AKBA (10 µ m ) or vehicle (0.1% DMSO) for 180 min at 37 °C. Formed LM were isolated from supernatants by SPE and analyzed by UPLC‐MS‐MS. Data are means ± S.E.M., given in pg/2 × 10 6 cells, n = 4 independent experiments. For statistical analysis, data were log‐transformed, one‐way analysis of variance (ANOVA) with Tukey's test, ** p < 0.01, *** p < 0.001 vehicle control versus AKBA; # p < 0.05, ## p < 0.01 vehicle + supplement versus AKBA + supplement.
Tg/Ms/Ftir System Netzsch Tg 209 F1 Iris, supplied by NETZSCH, 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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page 18 27 mass spectrometry ms analysis puri ed proteins  (Sartorius AG)
99
Sartorius AG page 18 27 mass spectrometry ms analysis puri ed proteins
AKBA elevates 12/15‐LOX products involving 15‐LOX‐1 in M2‐MDM. A,B) MDMs (2 × 10 6 cells mL −1 ) differentiated from human monocytes for 6 days with M‐CSF were transfected with non‐target or <t>ALOX15A</t> siRNA during polarization with IL‐4 (20 ng mL −1 ) for 48 h. A) Western blot analysis of 15‐LOX‐1; β ‐actin served as reference protein for normalization after densitometric analysis, n = 4; Student´s unpaired t ‐test. B) LM profile of ALOX15A siRNA‐treated M2‐MDMs after exposure to AKBA (10 µ m ) for 180 min, n = 4. Data are shown as bubble blot in % of non‐target siRNA of LM summarized in groups: 12/15‐LOX products include 17‐HDHA, 15‐HETE, 15‐HEPE, 14‐HDHA, 12‐HETE, and 12‐HEPE; SPM include PD1, PDX, RvD2, RvD5, and MaR1; 5‐LOX products include t‐LTB 4 , LTB 4 , 5‐HETE, and 5‐HEPE; COX products include PGE 2 , PGD 2 , TXB 2 , and PGF 2 α ; PUFA include AA, EPA, and DHA. C) Kinetic of LM formation in M2‐MDMs after incubation with 10 µ m AKBA or 2.5 µ m A23187 in the presence of AA, EPA, and DHA (1 µ m each). After the indicated time points, formed LM were isolated from the supernatants by SPE and analyzed by UPLC‐MS‐/MS. Data are shown as means ± S.E.M. given in pg/2 × 10 6 cells for representative SPM and for the sum of 5‐LOX products, including t‐LTB 4 , LTB 4 , 5‐HETE, and 5‐HEPE; n = 3 separate donors. D) Subcellular redistribution of 5‐LOX and 15‐LOX‐1 in M2‐MDMs after exposure to AKBA (10 µ m ) or A23187 (2.5 µ m ) for indicated time points. Cells were fixed, permeabilized, and incubated with antibodies against 5‐LOX (red) and 15‐LOX‐1 (cyan‐blue); scale bar = 10 µm. Results shown for one single cell are representative for ≈100 individual cells analyzed in n = 3 independent experiments with separate donors, each. E) M2‐MDMs where co‐incubated with or without 3 µg mL −1 of DHA and EPA, each, and with AKBA (10 µ m ) or vehicle (0.1% DMSO) for 180 min at 37 °C. Formed LM were isolated from supernatants by SPE and analyzed by UPLC‐MS‐MS. Data are means ± S.E.M., given in pg/2 × 10 6 cells, n = 4 independent experiments. For statistical analysis, data were log‐transformed, one‐way analysis of variance (ANOVA) with Tukey's test, ** p < 0.01, *** p < 0.001 vehicle control versus AKBA; # p < 0.05, ## p < 0.01 vehicle + supplement versus AKBA + supplement.
Page 18 27 Mass Spectrometry Ms Analysis Puri Ed Proteins, supplied by Sartorius AG, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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anti lys63 antibodies 27  (Tocris)
96
Tocris anti lys63 antibodies 27
FIGURE 3. Lys11, Lys48, and <t>Lys63,</t> but not Lys29 linkages accumulate in frontal cortex of AD or AD/LBD specimens. A–H, pathological staining of -synuclein (Lewy body), amyloid peptide (plaques), Tau (neurofibrillary tangles), and Lys63-linked polyUb in control and AD/LBD cases, respectively. Wide-field images were captured with a 10 objective, except a 40 objective was used for D and H. Scale bar is 150 m for all panels but D and H (20 m). I, elevated level of Ub in AD/LBD cases in Western blotting. J, analysis of four abundant polyUb linkages in total frontal cortex lysate of the matched control (n 12), pure AD (n 12), and AD/LBD cases (n 12) by LC-MS. The asterisk indicates p value 0.05 according to Student’s t test.
Anti Lys63 Antibodies 27, supplied by Tocris, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1h nmr  (Varian Medical)
86
Varian Medical 1h nmr
FIGURE 3. Lys11, Lys48, and <t>Lys63,</t> but not Lys29 linkages accumulate in frontal cortex of AD or AD/LBD specimens. A–H, pathological staining of -synuclein (Lewy body), amyloid peptide (plaques), Tau (neurofibrillary tangles), and Lys63-linked polyUb in control and AD/LBD cases, respectively. Wide-field images were captured with a 10 objective, except a 40 objective was used for D and H. Scale bar is 150 m for all panels but D and H (20 m). I, elevated level of Ub in AD/LBD cases in Western blotting. J, analysis of four abundant polyUb linkages in total frontal cortex lysate of the matched control (n 12), pure AD (n 12), and AD/LBD cases (n 12) by LC-MS. The asterisk indicates p value 0.05 according to Student’s t test.
1h Nmr, supplied by Varian Medical, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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tensor 27 spectrometer  (Bruker Corporation)
95
Bruker Corporation tensor 27 spectrometer
FIGURE 3. Lys11, Lys48, and <t>Lys63,</t> but not Lys29 linkages accumulate in frontal cortex of AD or AD/LBD specimens. A–H, pathological staining of -synuclein (Lewy body), amyloid peptide (plaques), Tau (neurofibrillary tangles), and Lys63-linked polyUb in control and AD/LBD cases, respectively. Wide-field images were captured with a 10 objective, except a 40 objective was used for D and H. Scale bar is 150 m for all panels but D and H (20 m). I, elevated level of Ub in AD/LBD cases in Western blotting. J, analysis of four abundant polyUb linkages in total frontal cortex lysate of the matched control (n 12), pure AD (n 12), and AD/LBD cases (n 12) by LC-MS. The asterisk indicates p value 0.05 according to Student’s t test.
Tensor 27 Spectrometer, supplied by Bruker Corporation, 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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ftir spectrometer  (Bruker Corporation)
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Bruker Corporation ftir spectrometer
FIGURE 3. Lys11, Lys48, and <t>Lys63,</t> but not Lys29 linkages accumulate in frontal cortex of AD or AD/LBD specimens. A–H, pathological staining of -synuclein (Lewy body), amyloid peptide (plaques), Tau (neurofibrillary tangles), and Lys63-linked polyUb in control and AD/LBD cases, respectively. Wide-field images were captured with a 10 objective, except a 40 objective was used for D and H. Scale bar is 150 m for all panels but D and H (20 m). I, elevated level of Ub in AD/LBD cases in Western blotting. J, analysis of four abundant polyUb linkages in total frontal cortex lysate of the matched control (n 12), pure AD (n 12), and AD/LBD cases (n 12) by LC-MS. The asterisk indicates p value 0.05 according to Student’s t test.
Ftir Spectrometer, supplied by Bruker Corporation, 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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human coq9  (Proteintech)
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Proteintech human coq9
Genotype and Source of Yeast Strains.
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nist ms search 2.0 software  (National Institute of Standards and Technology)
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Genotype and Source of Yeast Strains.
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diffusir  (PIKE Technologies)
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Genotype and Source of Yeast Strains.
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Genotype and Source of Yeast Strains.
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Image Search Results


AKBA elevates 12/15‐LOX products involving 15‐LOX‐1 in M2‐MDM. A,B) MDMs (2 × 10 6 cells mL −1 ) differentiated from human monocytes for 6 days with M‐CSF were transfected with non‐target or ALOX15A siRNA during polarization with IL‐4 (20 ng mL −1 ) for 48 h. A) Western blot analysis of 15‐LOX‐1; β ‐actin served as reference protein for normalization after densitometric analysis, n = 4; Student´s unpaired t ‐test. B) LM profile of ALOX15A siRNA‐treated M2‐MDMs after exposure to AKBA (10 µ m ) for 180 min, n = 4. Data are shown as bubble blot in % of non‐target siRNA of LM summarized in groups: 12/15‐LOX products include 17‐HDHA, 15‐HETE, 15‐HEPE, 14‐HDHA, 12‐HETE, and 12‐HEPE; SPM include PD1, PDX, RvD2, RvD5, and MaR1; 5‐LOX products include t‐LTB 4 , LTB 4 , 5‐HETE, and 5‐HEPE; COX products include PGE 2 , PGD 2 , TXB 2 , and PGF 2 α ; PUFA include AA, EPA, and DHA. C) Kinetic of LM formation in M2‐MDMs after incubation with 10 µ m AKBA or 2.5 µ m A23187 in the presence of AA, EPA, and DHA (1 µ m each). After the indicated time points, formed LM were isolated from the supernatants by SPE and analyzed by UPLC‐MS‐/MS. Data are shown as means ± S.E.M. given in pg/2 × 10 6 cells for representative SPM and for the sum of 5‐LOX products, including t‐LTB 4 , LTB 4 , 5‐HETE, and 5‐HEPE; n = 3 separate donors. D) Subcellular redistribution of 5‐LOX and 15‐LOX‐1 in M2‐MDMs after exposure to AKBA (10 µ m ) or A23187 (2.5 µ m ) for indicated time points. Cells were fixed, permeabilized, and incubated with antibodies against 5‐LOX (red) and 15‐LOX‐1 (cyan‐blue); scale bar = 10 µm. Results shown for one single cell are representative for ≈100 individual cells analyzed in n = 3 independent experiments with separate donors, each. E) M2‐MDMs where co‐incubated with or without 3 µg mL −1 of DHA and EPA, each, and with AKBA (10 µ m ) or vehicle (0.1% DMSO) for 180 min at 37 °C. Formed LM were isolated from supernatants by SPE and analyzed by UPLC‐MS‐MS. Data are means ± S.E.M., given in pg/2 × 10 6 cells, n = 4 independent experiments. For statistical analysis, data were log‐transformed, one‐way analysis of variance (ANOVA) with Tukey's test, ** p < 0.01, *** p < 0.001 vehicle control versus AKBA; # p < 0.05, ## p < 0.01 vehicle + supplement versus AKBA + supplement.

Journal: Advanced Science

Article Title: Allosteric Activation of 15‐Lipoxygenase‐1 by Boswellic Acid Induces the Lipid Mediator Class Switch to Promote Resolution of Inflammation

doi: 10.1002/advs.202205604

Figure Lengend Snippet: AKBA elevates 12/15‐LOX products involving 15‐LOX‐1 in M2‐MDM. A,B) MDMs (2 × 10 6 cells mL −1 ) differentiated from human monocytes for 6 days with M‐CSF were transfected with non‐target or ALOX15A siRNA during polarization with IL‐4 (20 ng mL −1 ) for 48 h. A) Western blot analysis of 15‐LOX‐1; β ‐actin served as reference protein for normalization after densitometric analysis, n = 4; Student´s unpaired t ‐test. B) LM profile of ALOX15A siRNA‐treated M2‐MDMs after exposure to AKBA (10 µ m ) for 180 min, n = 4. Data are shown as bubble blot in % of non‐target siRNA of LM summarized in groups: 12/15‐LOX products include 17‐HDHA, 15‐HETE, 15‐HEPE, 14‐HDHA, 12‐HETE, and 12‐HEPE; SPM include PD1, PDX, RvD2, RvD5, and MaR1; 5‐LOX products include t‐LTB 4 , LTB 4 , 5‐HETE, and 5‐HEPE; COX products include PGE 2 , PGD 2 , TXB 2 , and PGF 2 α ; PUFA include AA, EPA, and DHA. C) Kinetic of LM formation in M2‐MDMs after incubation with 10 µ m AKBA or 2.5 µ m A23187 in the presence of AA, EPA, and DHA (1 µ m each). After the indicated time points, formed LM were isolated from the supernatants by SPE and analyzed by UPLC‐MS‐/MS. Data are shown as means ± S.E.M. given in pg/2 × 10 6 cells for representative SPM and for the sum of 5‐LOX products, including t‐LTB 4 , LTB 4 , 5‐HETE, and 5‐HEPE; n = 3 separate donors. D) Subcellular redistribution of 5‐LOX and 15‐LOX‐1 in M2‐MDMs after exposure to AKBA (10 µ m ) or A23187 (2.5 µ m ) for indicated time points. Cells were fixed, permeabilized, and incubated with antibodies against 5‐LOX (red) and 15‐LOX‐1 (cyan‐blue); scale bar = 10 µm. Results shown for one single cell are representative for ≈100 individual cells analyzed in n = 3 independent experiments with separate donors, each. E) M2‐MDMs where co‐incubated with or without 3 µg mL −1 of DHA and EPA, each, and with AKBA (10 µ m ) or vehicle (0.1% DMSO) for 180 min at 37 °C. Formed LM were isolated from supernatants by SPE and analyzed by UPLC‐MS‐MS. Data are means ± S.E.M., given in pg/2 × 10 6 cells, n = 4 independent experiments. For statistical analysis, data were log‐transformed, one‐way analysis of variance (ANOVA) with Tukey's test, ** p < 0.01, *** p < 0.001 vehicle control versus AKBA; # p < 0.05, ## p < 0.01 vehicle + supplement versus AKBA + supplement.

Article Snippet: Freshly isolated monocytes were differentiated with M‐CSF (20 ng mL −1 ) to MDM M‐CSF and then subjected to electroporation using Neon Transfection System 100 μL Kit (Thermo Fisher Scientific) as described by Jordan et al. [ ] In brief, MDM M‐CSF (1.5 × 10 6 ) were resuspended in 1 mL of PBS and 20 μ m of human non‐targeting siRNA (Thermo Fisher Scientific; D‐001810‐01‐05) or 20 μ m of ALOX15A Trilencer‐27 Human siRNA (OriGene, SR300171) were added to the cells prior to electroporation.

Techniques: Transfection, Western Blot, Incubation, Isolation, Tandem Mass Spectroscopy, Transformation Assay, Control

FIGURE 3. Lys11, Lys48, and Lys63, but not Lys29 linkages accumulate in frontal cortex of AD or AD/LBD specimens. A–H, pathological staining of -synuclein (Lewy body), amyloid peptide (plaques), Tau (neurofibrillary tangles), and Lys63-linked polyUb in control and AD/LBD cases, respectively. Wide-field images were captured with a 10 objective, except a 40 objective was used for D and H. Scale bar is 150 m for all panels but D and H (20 m). I, elevated level of Ub in AD/LBD cases in Western blotting. J, analysis of four abundant polyUb linkages in total frontal cortex lysate of the matched control (n 12), pure AD (n 12), and AD/LBD cases (n 12) by LC-MS. The asterisk indicates p value 0.05 according to Student’s t test.

Journal: Journal of Biological Chemistry

Article Title: Polyubiquitin Linkage Profiles in Three Models of Proteolytic Stress Suggest the Etiology of Alzheimer Disease

doi: 10.1074/jbc.m110.149633

Figure Lengend Snippet: FIGURE 3. Lys11, Lys48, and Lys63, but not Lys29 linkages accumulate in frontal cortex of AD or AD/LBD specimens. A–H, pathological staining of -synuclein (Lewy body), amyloid peptide (plaques), Tau (neurofibrillary tangles), and Lys63-linked polyUb in control and AD/LBD cases, respectively. Wide-field images were captured with a 10 objective, except a 40 objective was used for D and H. Scale bar is 150 m for all panels but D and H (20 m). I, elevated level of Ub in AD/LBD cases in Western blotting. J, analysis of four abundant polyUb linkages in total frontal cortex lysate of the matched control (n 12), pure AD (n 12), and AD/LBD cases (n 12) by LC-MS. The asterisk indicates p value 0.05 according to Student’s t test.

Article Snippet: Reagents—Reagents used in this study included antibodies against actin (catalog no. sc-1615, Santa Cruz Biotechnology, Santa Cruz, CA), ubiquitin (catalog no. mAb1510, Chemicon Millipore, Billerica, MA), Lys63 polyUb monoclonal Ab (HWA4C4, eBioscience, San Diego, CA); LC3 (catalog no. NB100-2331, Novus Biologicals, Littleton, CO); humanized anti-Lys48 and anti-Lys63 antibodies (27) (a kind gift of V.Dixit); MG-132 and epoxomicin (Boston Biochem., Cambridge, MA); riluzole (Tocris, Ellisville, MO); and 6-aminonicotinamide and bafilomycin A1 (Sigma).

Techniques: Staining, Control, Western Blot, Liquid Chromatography with Mass Spectroscopy

FIGURE 4. Proteasome deficiency increases all detected polyUb linkages, but Lys63 shows a delayed response. A, Western blot of Ub when HEK293 cells were treated with 10 M epoxomicin. B, Ub linkage profile in a time course during epoxomicin treatment. The signal of Lys6 linkages was weak compared with others and might be subject to more variation. Rpn2 and E1 were also quantified as two internal loading controls. C, Ub linkage profile in cells treated with 10 M MG-132. D, PolyUb linkage profile using mouse primary neuronal culture.

Journal: Journal of Biological Chemistry

Article Title: Polyubiquitin Linkage Profiles in Three Models of Proteolytic Stress Suggest the Etiology of Alzheimer Disease

doi: 10.1074/jbc.m110.149633

Figure Lengend Snippet: FIGURE 4. Proteasome deficiency increases all detected polyUb linkages, but Lys63 shows a delayed response. A, Western blot of Ub when HEK293 cells were treated with 10 M epoxomicin. B, Ub linkage profile in a time course during epoxomicin treatment. The signal of Lys6 linkages was weak compared with others and might be subject to more variation. Rpn2 and E1 were also quantified as two internal loading controls. C, Ub linkage profile in cells treated with 10 M MG-132. D, PolyUb linkage profile using mouse primary neuronal culture.

Article Snippet: Reagents—Reagents used in this study included antibodies against actin (catalog no. sc-1615, Santa Cruz Biotechnology, Santa Cruz, CA), ubiquitin (catalog no. mAb1510, Chemicon Millipore, Billerica, MA), Lys63 polyUb monoclonal Ab (HWA4C4, eBioscience, San Diego, CA); LC3 (catalog no. NB100-2331, Novus Biologicals, Littleton, CO); humanized anti-Lys48 and anti-Lys63 antibodies (27) (a kind gift of V.Dixit); MG-132 and epoxomicin (Boston Biochem., Cambridge, MA); riluzole (Tocris, Ellisville, MO); and 6-aminonicotinamide and bafilomycin A1 (Sigma).

Techniques: Western Blot

FIGURE 5. Lys48 and Lys63 linkages accumulate in inclusions (or inclusion- like structures) after proteasome inhibition. A, Lys48 polyUb was imaged by immunofluorescent staining at 0, 4, and 10 h of MG-132 treatment (10 M). B, Lys63 polyUb (green) was analyzed together with LC3 (red) under the same conditions. The scale bars represent a distance of 10 M.

Journal: Journal of Biological Chemistry

Article Title: Polyubiquitin Linkage Profiles in Three Models of Proteolytic Stress Suggest the Etiology of Alzheimer Disease

doi: 10.1074/jbc.m110.149633

Figure Lengend Snippet: FIGURE 5. Lys48 and Lys63 linkages accumulate in inclusions (or inclusion- like structures) after proteasome inhibition. A, Lys48 polyUb was imaged by immunofluorescent staining at 0, 4, and 10 h of MG-132 treatment (10 M). B, Lys63 polyUb (green) was analyzed together with LC3 (red) under the same conditions. The scale bars represent a distance of 10 M.

Article Snippet: Reagents—Reagents used in this study included antibodies against actin (catalog no. sc-1615, Santa Cruz Biotechnology, Santa Cruz, CA), ubiquitin (catalog no. mAb1510, Chemicon Millipore, Billerica, MA), Lys63 polyUb monoclonal Ab (HWA4C4, eBioscience, San Diego, CA); LC3 (catalog no. NB100-2331, Novus Biologicals, Littleton, CO); humanized anti-Lys48 and anti-Lys63 antibodies (27) (a kind gift of V.Dixit); MG-132 and epoxomicin (Boston Biochem., Cambridge, MA); riluzole (Tocris, Ellisville, MO); and 6-aminonicotinamide and bafilomycin A1 (Sigma).

Techniques: Inhibition, Staining

FIGURE 6. Lysosomal deficiency increases Lys63 linkages and other polyUb linkages. A, Ub linkage profile of bafilomycin A1-treated (200 nM) HEK293 cells, shown as mean and S.E. Statistical significance (asterisk) was analyzed between the untreated samples and other samples based on Stu- dent’s t test (p 0.05). B, Ub linkage profile of bafilomycin A1-treated primary neurons in a similar time course. C, immunofluorescence of Lys48, Lys63 polyUb chains, and LC3 with varying bafilomycin A1 (200 nM) treatment time. The nuclei are shown by DAPI staining. Lysosome inhibition appeared to increase the size of LC3/Lys48/Lys63-positive structures in HEK293 cells over time. The scale bars represent a distance of 10 M.

Journal: Journal of Biological Chemistry

Article Title: Polyubiquitin Linkage Profiles in Three Models of Proteolytic Stress Suggest the Etiology of Alzheimer Disease

doi: 10.1074/jbc.m110.149633

Figure Lengend Snippet: FIGURE 6. Lysosomal deficiency increases Lys63 linkages and other polyUb linkages. A, Ub linkage profile of bafilomycin A1-treated (200 nM) HEK293 cells, shown as mean and S.E. Statistical significance (asterisk) was analyzed between the untreated samples and other samples based on Stu- dent’s t test (p 0.05). B, Ub linkage profile of bafilomycin A1-treated primary neurons in a similar time course. C, immunofluorescence of Lys48, Lys63 polyUb chains, and LC3 with varying bafilomycin A1 (200 nM) treatment time. The nuclei are shown by DAPI staining. Lysosome inhibition appeared to increase the size of LC3/Lys48/Lys63-positive structures in HEK293 cells over time. The scale bars represent a distance of 10 M.

Article Snippet: Reagents—Reagents used in this study included antibodies against actin (catalog no. sc-1615, Santa Cruz Biotechnology, Santa Cruz, CA), ubiquitin (catalog no. mAb1510, Chemicon Millipore, Billerica, MA), Lys63 polyUb monoclonal Ab (HWA4C4, eBioscience, San Diego, CA); LC3 (catalog no. NB100-2331, Novus Biologicals, Littleton, CO); humanized anti-Lys48 and anti-Lys63 antibodies (27) (a kind gift of V.Dixit); MG-132 and epoxomicin (Boston Biochem., Cambridge, MA); riluzole (Tocris, Ellisville, MO); and 6-aminonicotinamide and bafilomycin A1 (Sigma).

Techniques: Immunofluorescence, Staining, Inhibition

Genotype and Source of Yeast Strains.

Journal: Frontiers in Physiology

Article Title: Human COQ9 Rescues a coq9 Yeast Mutant by Enhancing Coenzyme Q Biosynthesis from 4-Hydroxybenzoic Acid and Stabilizing the CoQ-Synthome

doi: 10.3389/fphys.2017.00463

Figure Lengend Snippet: Genotype and Source of Yeast Strains.

Article Snippet: Human COQ9 , 1:1000 , Proteintech Group, Inc..

Techniques:

Description and Source of Antibodies.

Journal: Frontiers in Physiology

Article Title: Human COQ9 Rescues a coq9 Yeast Mutant by Enhancing Coenzyme Q Biosynthesis from 4-Hydroxybenzoic Acid and Stabilizing the CoQ-Synthome

doi: 10.3389/fphys.2017.00463

Figure Lengend Snippet: Description and Source of Antibodies.

Article Snippet: Human COQ9 , 1:1000 , Proteintech Group, Inc..

Techniques:

Expression of human COQ9 or over-expression of COQ8 rescues the growth of the temperature-sensitive coq9 mutant on a non-fermentable carbon source. W303Δ9K was transformed with TS19 and one of the following plasmids: empty vector pRS426 (EV), multi-copy yeast COQ8 ( mcCOQ8 ), single-copy human COQ9 ( scHCOQ9 ), and multi-copy human COQ9 ( mcHCOQ9 ). Yeast strains were cultured in SD-Leu-Ura media overnight at 25°C. W3031B (WT), W303Δ9K, W303Δ9K: COQ9 , and W303Δ9K:TS19 were used as controls and grown in YPG and SD-Leu respectively. Cell cultures were diluted to 0.2 A 600 nm /ml and 2 μl of 1:5 serial dilutions were spotted onto SD-Ura-Leu or YPG plate media and incubated at either 25°C or 37°C for 3 days.

Journal: Frontiers in Physiology

Article Title: Human COQ9 Rescues a coq9 Yeast Mutant by Enhancing Coenzyme Q Biosynthesis from 4-Hydroxybenzoic Acid and Stabilizing the CoQ-Synthome

doi: 10.3389/fphys.2017.00463

Figure Lengend Snippet: Expression of human COQ9 or over-expression of COQ8 rescues the growth of the temperature-sensitive coq9 mutant on a non-fermentable carbon source. W303Δ9K was transformed with TS19 and one of the following plasmids: empty vector pRS426 (EV), multi-copy yeast COQ8 ( mcCOQ8 ), single-copy human COQ9 ( scHCOQ9 ), and multi-copy human COQ9 ( mcHCOQ9 ). Yeast strains were cultured in SD-Leu-Ura media overnight at 25°C. W3031B (WT), W303Δ9K, W303Δ9K: COQ9 , and W303Δ9K:TS19 were used as controls and grown in YPG and SD-Leu respectively. Cell cultures were diluted to 0.2 A 600 nm /ml and 2 μl of 1:5 serial dilutions were spotted onto SD-Ura-Leu or YPG plate media and incubated at either 25°C or 37°C for 3 days.

Article Snippet: Human COQ9 , 1:1000 , Proteintech Group, Inc..

Techniques: Expressing, Over Expression, Mutagenesis, Transformation Assay, Plasmid Preparation, Cell Culture, Incubation

Expression of human COQ9 or over-expression of COQ8 increases the content of Q 6 and DMQ 6 in W303Δ9K expressing the temperature-sensitive plasmid TS19. W303Δ9K was transformed with TS19 and one of the following plasmids: empty vector pRS426 (EV), multi-copy yeast COQ8 ( mcCOQ8 ), single-copy of human COQ9 ( scHCOQ9 ), and multi-copy of human COQ9 ( mcHCOQ9 ). One colony of each type of yeast transformant was seeded in selective media, SD-Ura-Leu, and grown overnight. The cell culture was diluted to 0.1A 600 nm /ml in 20 ml of fresh SD-Ura-Leu containing 10 μg/ml 13 C 6 -pABA (A–C) or 10 μg/ml 13 C 6 -4HB (D–F) dissolved in 2 μl ethanol/ml medium and grown at 25 or 37°C for 12.5 h. Final cell density was between 3 and 5 A 600 nm /ml. Yeast cells (corresponding to a total of 50 A 600 nm ) were collected as pellets, from which lipids were extracted and analyzed by RP-HPLC-MS/MS. Each bar represents a total four measurements from two independent samples each with two injections. Black bars represent the amount of 12 C-Q 6 , red bars represent 13 C 6 -Q 6 and 13 C 6 -DMQ 6 labeled by 13 C 6 -pABA and blue bars represent 13 C 6 -Q 6 and 13 C 6 -DMQ 6 labeled by 13 C 6 -4HB. The amounts of the 12 C- and 13 C 6 -compounds represent the sum of reduced and oxidized forms. Both Q 6 and 13 C 6 -DMQ 6 levels were higher in W303Δ9K:TS19 harboring human COQ9 homolog or over-expression of COQ8 as compared to W303Δ9K:TS19 harboring empty vector as determined by the Student's two-tailed t -test. The * symbols represent samples at 25°C compared to W303Δ9K:TS19+EV at 25°C; ** p < 0.01, *** p < 0.001. The + symbols represent samples at 37°C compared to W303Δ9K:TS19+EV at 37°C; + p < 0.05, ‡ p < 0.01, p < 0.001. When there is no significant change, ns was used to designate “non-significant.”

Journal: Frontiers in Physiology

Article Title: Human COQ9 Rescues a coq9 Yeast Mutant by Enhancing Coenzyme Q Biosynthesis from 4-Hydroxybenzoic Acid and Stabilizing the CoQ-Synthome

doi: 10.3389/fphys.2017.00463

Figure Lengend Snippet: Expression of human COQ9 or over-expression of COQ8 increases the content of Q 6 and DMQ 6 in W303Δ9K expressing the temperature-sensitive plasmid TS19. W303Δ9K was transformed with TS19 and one of the following plasmids: empty vector pRS426 (EV), multi-copy yeast COQ8 ( mcCOQ8 ), single-copy of human COQ9 ( scHCOQ9 ), and multi-copy of human COQ9 ( mcHCOQ9 ). One colony of each type of yeast transformant was seeded in selective media, SD-Ura-Leu, and grown overnight. The cell culture was diluted to 0.1A 600 nm /ml in 20 ml of fresh SD-Ura-Leu containing 10 μg/ml 13 C 6 -pABA (A–C) or 10 μg/ml 13 C 6 -4HB (D–F) dissolved in 2 μl ethanol/ml medium and grown at 25 or 37°C for 12.5 h. Final cell density was between 3 and 5 A 600 nm /ml. Yeast cells (corresponding to a total of 50 A 600 nm ) were collected as pellets, from which lipids were extracted and analyzed by RP-HPLC-MS/MS. Each bar represents a total four measurements from two independent samples each with two injections. Black bars represent the amount of 12 C-Q 6 , red bars represent 13 C 6 -Q 6 and 13 C 6 -DMQ 6 labeled by 13 C 6 -pABA and blue bars represent 13 C 6 -Q 6 and 13 C 6 -DMQ 6 labeled by 13 C 6 -4HB. The amounts of the 12 C- and 13 C 6 -compounds represent the sum of reduced and oxidized forms. Both Q 6 and 13 C 6 -DMQ 6 levels were higher in W303Δ9K:TS19 harboring human COQ9 homolog or over-expression of COQ8 as compared to W303Δ9K:TS19 harboring empty vector as determined by the Student's two-tailed t -test. The * symbols represent samples at 25°C compared to W303Δ9K:TS19+EV at 25°C; ** p < 0.01, *** p < 0.001. The + symbols represent samples at 37°C compared to W303Δ9K:TS19+EV at 37°C; + p < 0.05, ‡ p < 0.01, p < 0.001. When there is no significant change, ns was used to designate “non-significant.”

Article Snippet: Human COQ9 , 1:1000 , Proteintech Group, Inc..

Techniques: Expressing, Over Expression, Plasmid Preparation, Transformation Assay, Cell Culture, Tandem Mass Spectroscopy, Labeling, Two Tailed Test

Expression of human COQ9 stabilizes yeast Coq polypeptides in the temperature-sensitive coq9 mutant at permissive temperature. W303Δ9K harboring the temperature-sensitive plasmid TS19 (Δ9K:TS19) were transformed with multi-copy human COQ9 (Δ9K:TS19+ mcHCOQ9 ). Yeast strains W3031B (WT), Δ9K:TS19, and Δ9K:TS19+ mcHCOQ9 were grown for 18.5 h at either 25 or 37°C. Mitochondria were then purified from these yeast cultures. Mitochondria were also isolated from the null control strains BY4741ΔCOQ9 (Δ9), W303ΔCOQ4 (Δ4) (A) , W303ΔCOQ7 (Δ7) (B) , and W303ΔCOQ6 (Δ6) (C) after yeast were grown overnight at 30°C. Purified mitochondria (15 μg protein) were separated by SDS-PAGE and analyzed by Western blot. Immunoblots were performed with antibodies against the designated polypeptides: Coq4, Coq6, Coq7, Coq9, human COQ9, and Atp2. M denotes the molecular weight marker.

Journal: Frontiers in Physiology

Article Title: Human COQ9 Rescues a coq9 Yeast Mutant by Enhancing Coenzyme Q Biosynthesis from 4-Hydroxybenzoic Acid and Stabilizing the CoQ-Synthome

doi: 10.3389/fphys.2017.00463

Figure Lengend Snippet: Expression of human COQ9 stabilizes yeast Coq polypeptides in the temperature-sensitive coq9 mutant at permissive temperature. W303Δ9K harboring the temperature-sensitive plasmid TS19 (Δ9K:TS19) were transformed with multi-copy human COQ9 (Δ9K:TS19+ mcHCOQ9 ). Yeast strains W3031B (WT), Δ9K:TS19, and Δ9K:TS19+ mcHCOQ9 were grown for 18.5 h at either 25 or 37°C. Mitochondria were then purified from these yeast cultures. Mitochondria were also isolated from the null control strains BY4741ΔCOQ9 (Δ9), W303ΔCOQ4 (Δ4) (A) , W303ΔCOQ7 (Δ7) (B) , and W303ΔCOQ6 (Δ6) (C) after yeast were grown overnight at 30°C. Purified mitochondria (15 μg protein) were separated by SDS-PAGE and analyzed by Western blot. Immunoblots were performed with antibodies against the designated polypeptides: Coq4, Coq6, Coq7, Coq9, human COQ9, and Atp2. M denotes the molecular weight marker.

Article Snippet: Human COQ9 , 1:1000 , Proteintech Group, Inc..

Techniques: Expressing, Mutagenesis, Plasmid Preparation, Transformation Assay, Purification, Isolation, Control, SDS Page, Western Blot, Molecular Weight, Marker

The human Coq9 polypeptide associates with yeast Coq6. Mitochondria were isolated from CNAP6 and CNAP6: mcHCOQ9 . Purified mitochondria (13 mg) were solubilized and co-precipitation was then performed on the solubilized mitochondria with Ni-NTA resin. Flow-through (FT), wash (W1 and W2), eluate (E1 and E2), and beads from co-precipitation were collected. 0.17% of the FT, 0.25% of W1, 0.25% of W2, 1% of E1, 0.5% of E2, and 1.25% of Ni-NTA resin were analyzed by SDS-PAGE followed by immunoblotting with antibodies against yeast Coq9, Coq6, human COQ9, and Atp2. Purified mitochondria (15 μg) from CNAP6: mcHCOQ9 were included as control.

Journal: Frontiers in Physiology

Article Title: Human COQ9 Rescues a coq9 Yeast Mutant by Enhancing Coenzyme Q Biosynthesis from 4-Hydroxybenzoic Acid and Stabilizing the CoQ-Synthome

doi: 10.3389/fphys.2017.00463

Figure Lengend Snippet: The human Coq9 polypeptide associates with yeast Coq6. Mitochondria were isolated from CNAP6 and CNAP6: mcHCOQ9 . Purified mitochondria (13 mg) were solubilized and co-precipitation was then performed on the solubilized mitochondria with Ni-NTA resin. Flow-through (FT), wash (W1 and W2), eluate (E1 and E2), and beads from co-precipitation were collected. 0.17% of the FT, 0.25% of W1, 0.25% of W2, 1% of E1, 0.5% of E2, and 1.25% of Ni-NTA resin were analyzed by SDS-PAGE followed by immunoblotting with antibodies against yeast Coq9, Coq6, human COQ9, and Atp2. Purified mitochondria (15 μg) from CNAP6: mcHCOQ9 were included as control.

Article Snippet: Human COQ9 , 1:1000 , Proteintech Group, Inc..

Techniques: Isolation, Purification, SDS Page, Western Blot, Control