cis Search Results


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MedChemExpress cisplatin
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Chem Impex International 9fluorenylmethoxycarbonyloxy succinimide fmoc osu
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Proteintech cycline
Fig. 2 NR1D1 induced cell cycle arrest and apoptosis in ovarian cancer cells. A Cell cycle of NR1D1 over-expressed cells was determined by flow cytometry. B The levels of cyclinD and <t>cyclinE</t> were determined by western blot. C Flow cytometry was performed to determine the cell cycle of NR1D1 silenced cells. D Western blot was performed to determine the levels of cyclinD and cyclinE. E Apoptosis of NR1D1 over-expressed cells was determined by flow cytometry. F After transfection with NR1D1 over-expression plasmid, the levels of activated caspase-3 and caspase-9 were determined. The results are presented as mean + SD
Cycline, supplied by Proteintech, 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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Toronto Research Chemicals cis retinyl palmitate
Fig. 2 NR1D1 induced cell cycle arrest and apoptosis in ovarian cancer cells. A Cell cycle of NR1D1 over-expressed cells was determined by flow cytometry. B The levels of cyclinD and <t>cyclinE</t> were determined by western blot. C Flow cytometry was performed to determine the cell cycle of NR1D1 silenced cells. D Western blot was performed to determine the levels of cyclinD and cyclinE. E Apoptosis of NR1D1 over-expressed cells was determined by flow cytometry. F After transfection with NR1D1 over-expression plasmid, the levels of activated caspase-3 and caspase-9 were determined. The results are presented as mean + SD
Cis Retinyl Palmitate, supplied by Toronto Research Chemicals, 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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TargetMol 13 cis retinoic acid
Fig. 2 NR1D1 induced cell cycle arrest and apoptosis in ovarian cancer cells. A Cell cycle of NR1D1 over-expressed cells was determined by flow cytometry. B The levels of cyclinD and <t>cyclinE</t> were determined by western blot. C Flow cytometry was performed to determine the cell cycle of NR1D1 silenced cells. D Western blot was performed to determine the levels of cyclinD and cyclinE. E Apoptosis of NR1D1 over-expressed cells was determined by flow cytometry. F After transfection with NR1D1 over-expression plasmid, the levels of activated caspase-3 and caspase-9 were determined. The results are presented as mean + SD
13 Cis Retinoic Acid, supplied by TargetMol, used in various techniques. Bioz Stars score: 89/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Biosynth Carbosynth cetp
Figure 2. An interinstrument platform comparison <t>of</t> <t>PLTP</t> and <t>CETP</t> tracer enrichment data. (A) PRM scans of the same CETP peptide from the Q Exactive and the Lumos. The relative peak intensities of the fragment ions are conserved between the 2 instruments. The y7 2HM3 (tracer) peak environment is zoomed in. R = 120 K for the Q Exactive and 240 K for the Lumos. (B) Loess regression plots showing that the standard error (gray) of the fitted curves is lower on the Lumos. PLTP data are from alpha1 and CETP from alpha2. Legend: the PRM ions’ m/z values. (C) Box plots depicting the distribution of the enrichment data in B. Each data point is the average enrichment (n = 3 PRM ions’ measurements) per time point. The box plots depict the minimum and maximum values (whiskers), the upper and lower quartiles, and the median. The length of the box represents the interquartile range. The gray lines indicate the relative shift in enrichment value per given time point. Variance was calculated using individual PRM ion enrichment data in B, not the averages.
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MedChemExpress cells
Figure 2. An interinstrument platform comparison <t>of</t> <t>PLTP</t> and <t>CETP</t> tracer enrichment data. (A) PRM scans of the same CETP peptide from the Q Exactive and the Lumos. The relative peak intensities of the fragment ions are conserved between the 2 instruments. The y7 2HM3 (tracer) peak environment is zoomed in. R = 120 K for the Q Exactive and 240 K for the Lumos. (B) Loess regression plots showing that the standard error (gray) of the fitted curves is lower on the Lumos. PLTP data are from alpha1 and CETP from alpha2. Legend: the PRM ions’ m/z values. (C) Box plots depicting the distribution of the enrichment data in B. Each data point is the average enrichment (n = 3 PRM ions’ measurements) per time point. The box plots depict the minimum and maximum values (whiskers), the upper and lower quartiles, and the median. The length of the box represents the interquartile range. The gray lines indicate the relative shift in enrichment value per given time point. Variance was calculated using individual PRM ion enrichment data in B, not the averages.
Cells, supplied by MedChemExpress, 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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Gerstel GmbH cooled injection system
Figure 2. An interinstrument platform comparison <t>of</t> <t>PLTP</t> and <t>CETP</t> tracer enrichment data. (A) PRM scans of the same CETP peptide from the Q Exactive and the Lumos. The relative peak intensities of the fragment ions are conserved between the 2 instruments. The y7 2HM3 (tracer) peak environment is zoomed in. R = 120 K for the Q Exactive and 240 K for the Lumos. (B) Loess regression plots showing that the standard error (gray) of the fitted curves is lower on the Lumos. PLTP data are from alpha1 and CETP from alpha2. Legend: the PRM ions’ m/z values. (C) Box plots depicting the distribution of the enrichment data in B. Each data point is the average enrichment (n = 3 PRM ions’ measurements) per time point. The box plots depict the minimum and maximum values (whiskers), the upper and lower quartiles, and the median. The length of the box represents the interquartile range. The gray lines indicate the relative shift in enrichment value per given time point. Variance was calculated using individual PRM ion enrichment data in B, not the averages.
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Avanti Polar dioleoyl sn glycero 3 phosphocholine dopc
Figure 2. An interinstrument platform comparison <t>of</t> <t>PLTP</t> and <t>CETP</t> tracer enrichment data. (A) PRM scans of the same CETP peptide from the Q Exactive and the Lumos. The relative peak intensities of the fragment ions are conserved between the 2 instruments. The y7 2HM3 (tracer) peak environment is zoomed in. R = 120 K for the Q Exactive and 240 K for the Lumos. (B) Loess regression plots showing that the standard error (gray) of the fitted curves is lower on the Lumos. PLTP data are from alpha1 and CETP from alpha2. Legend: the PRM ions’ m/z values. (C) Box plots depicting the distribution of the enrichment data in B. Each data point is the average enrichment (n = 3 PRM ions’ measurements) per time point. The box plots depict the minimum and maximum values (whiskers), the upper and lower quartiles, and the median. The length of the box represents the interquartile range. The gray lines indicate the relative shift in enrichment value per given time point. Variance was calculated using individual PRM ion enrichment data in B, not the averages.
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Avanti Polar dioleoylsn glycero 3 phosphoethanolamine n
Figure 2. An interinstrument platform comparison <t>of</t> <t>PLTP</t> and <t>CETP</t> tracer enrichment data. (A) PRM scans of the same CETP peptide from the Q Exactive and the Lumos. The relative peak intensities of the fragment ions are conserved between the 2 instruments. The y7 2HM3 (tracer) peak environment is zoomed in. R = 120 K for the Q Exactive and 240 K for the Lumos. (B) Loess regression plots showing that the standard error (gray) of the fitted curves is lower on the Lumos. PLTP data are from alpha1 and CETP from alpha2. Legend: the PRM ions’ m/z values. (C) Box plots depicting the distribution of the enrichment data in B. Each data point is the average enrichment (n = 3 PRM ions’ measurements) per time point. The box plots depict the minimum and maximum values (whiskers), the upper and lower quartiles, and the median. The length of the box represents the interquartile range. The gray lines indicate the relative shift in enrichment value per given time point. Variance was calculated using individual PRM ion enrichment data in B, not the averages.
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Valiant Co Ltd mgso4
Figure 2. An interinstrument platform comparison <t>of</t> <t>PLTP</t> and <t>CETP</t> tracer enrichment data. (A) PRM scans of the same CETP peptide from the Q Exactive and the Lumos. The relative peak intensities of the fragment ions are conserved between the 2 instruments. The y7 2HM3 (tracer) peak environment is zoomed in. R = 120 K for the Q Exactive and 240 K for the Lumos. (B) Loess regression plots showing that the standard error (gray) of the fitted curves is lower on the Lumos. PLTP data are from alpha1 and CETP from alpha2. Legend: the PRM ions’ m/z values. (C) Box plots depicting the distribution of the enrichment data in B. Each data point is the average enrichment (n = 3 PRM ions’ measurements) per time point. The box plots depict the minimum and maximum values (whiskers), the upper and lower quartiles, and the median. The length of the box represents the interquartile range. The gray lines indicate the relative shift in enrichment value per given time point. Variance was calculated using individual PRM ion enrichment data in B, not the averages.
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Valiant Co Ltd purity triolein
Figure 2. An interinstrument platform comparison <t>of</t> <t>PLTP</t> and <t>CETP</t> tracer enrichment data. (A) PRM scans of the same CETP peptide from the Q Exactive and the Lumos. The relative peak intensities of the fragment ions are conserved between the 2 instruments. The y7 2HM3 (tracer) peak environment is zoomed in. R = 120 K for the Q Exactive and 240 K for the Lumos. (B) Loess regression plots showing that the standard error (gray) of the fitted curves is lower on the Lumos. PLTP data are from alpha1 and CETP from alpha2. Legend: the PRM ions’ m/z values. (C) Box plots depicting the distribution of the enrichment data in B. Each data point is the average enrichment (n = 3 PRM ions’ measurements) per time point. The box plots depict the minimum and maximum values (whiskers), the upper and lower quartiles, and the median. The length of the box represents the interquartile range. The gray lines indicate the relative shift in enrichment value per given time point. Variance was calculated using individual PRM ion enrichment data in B, not the averages.
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Image Search Results


Fig. 2 NR1D1 induced cell cycle arrest and apoptosis in ovarian cancer cells. A Cell cycle of NR1D1 over-expressed cells was determined by flow cytometry. B The levels of cyclinD and cyclinE were determined by western blot. C Flow cytometry was performed to determine the cell cycle of NR1D1 silenced cells. D Western blot was performed to determine the levels of cyclinD and cyclinE. E Apoptosis of NR1D1 over-expressed cells was determined by flow cytometry. F After transfection with NR1D1 over-expression plasmid, the levels of activated caspase-3 and caspase-9 were determined. The results are presented as mean + SD

Journal: BMC cancer

Article Title: NR1D1 suppressed the growth of ovarian cancer by abrogating the JAK/STAT3 signaling pathway.

doi: 10.1186/s12885-021-08597-8

Figure Lengend Snippet: Fig. 2 NR1D1 induced cell cycle arrest and apoptosis in ovarian cancer cells. A Cell cycle of NR1D1 over-expressed cells was determined by flow cytometry. B The levels of cyclinD and cyclinE were determined by western blot. C Flow cytometry was performed to determine the cell cycle of NR1D1 silenced cells. D Western blot was performed to determine the levels of cyclinD and cyclinE. E Apoptosis of NR1D1 over-expressed cells was determined by flow cytometry. F After transfection with NR1D1 over-expression plasmid, the levels of activated caspase-3 and caspase-9 were determined. The results are presented as mean + SD

Article Snippet: Following blocking with 5% bovine serum albumin, the membranes were incubated with antibodies against NR1D1 (1:1000; Abclonal, Wuhan, China), cyclinD (1:1000; ABclonal), cyclinE (1:1000; Proteintech, Wuhan, China), SOCS3 (1:1000; ABclonal), JAK-1 (1:1000; Affinity, Changzhou, China), p-JAK1 (Tyr 1034/Tyr 1035; 1:1000; Affinity), JAK2 (1:500; Affinity), p-JAK2 (Tyr 1007/Tyr 1008, 1:1000; Affinity), STAT3 (1:500; Affinity), p-STAT3 (Tyr 705, 1:500; Affinity), β-actin (1:2000; Proteintech) at 4 °C overnight.

Techniques: Flow Cytometry, Western Blot, Transfection, Over Expression, Plasmid Preparation

Figure 2. An interinstrument platform comparison of PLTP and CETP tracer enrichment data. (A) PRM scans of the same CETP peptide from the Q Exactive and the Lumos. The relative peak intensities of the fragment ions are conserved between the 2 instruments. The y7 2HM3 (tracer) peak environment is zoomed in. R = 120 K for the Q Exactive and 240 K for the Lumos. (B) Loess regression plots showing that the standard error (gray) of the fitted curves is lower on the Lumos. PLTP data are from alpha1 and CETP from alpha2. Legend: the PRM ions’ m/z values. (C) Box plots depicting the distribution of the enrichment data in B. Each data point is the average enrichment (n = 3 PRM ions’ measurements) per time point. The box plots depict the minimum and maximum values (whiskers), the upper and lower quartiles, and the median. The length of the box represents the interquartile range. The gray lines indicate the relative shift in enrichment value per given time point. Variance was calculated using individual PRM ion enrichment data in B, not the averages.

Journal: JCI insight

Article Title: Metabolism of PLTP, CETP, and LCAT on multiple HDL sizes using the Orbitrap Fusion Lumos.

doi: 10.1172/jci.insight.143526

Figure Lengend Snippet: Figure 2. An interinstrument platform comparison of PLTP and CETP tracer enrichment data. (A) PRM scans of the same CETP peptide from the Q Exactive and the Lumos. The relative peak intensities of the fragment ions are conserved between the 2 instruments. The y7 2HM3 (tracer) peak environment is zoomed in. R = 120 K for the Q Exactive and 240 K for the Lumos. (B) Loess regression plots showing that the standard error (gray) of the fitted curves is lower on the Lumos. PLTP data are from alpha1 and CETP from alpha2. Legend: the PRM ions’ m/z values. (C) Box plots depicting the distribution of the enrichment data in B. Each data point is the average enrichment (n = 3 PRM ions’ measurements) per time point. The box plots depict the minimum and maximum values (whiskers), the upper and lower quartiles, and the median. The length of the box represents the interquartile range. The gray lines indicate the relative shift in enrichment value per given time point. Variance was calculated using individual PRM ion enrichment data in B, not the averages.

Article Snippet: Each protein was quantified using the following peptide standards: APOA1 (THLAPYSDEL[R-labeled]), APOE (LGPLVEQG[R-labeled]), LCAT (SSGLVSNAPGVQI[R-labeled]), CETP (ASYPDITGE[K-labeled]), and PLTP (AVEPQLQEEE[R-labeled]) (New England Peptides, NEP, Supplemental Table 2).

Techniques: Comparison

Figure 3. Compartmental models and kinetics parameters for PLTP and CETP in the larger alpha HDL size fractions. (A) Compartmental model for PLTP and CETP (the average of n = 6 participants). PLTP flux into alpha1 is approximately 45% from the source (0.010 mg/kg/d) and 55% from the smaller alpha2 (0.012 mg/kg/d). Approximately 75% of PLTP on alpha2 is transferred to alpha0 and alpha1 (0.10 and 0.59 pool/d, respectively) while the remaining 25% is removed from the model system (0.20 pool/d). CETP appears on alpha1 and alpha2 via direct secretion. (B) Enrichment curve fits generated from the models in A, participant 1. (C) FCR and production rate (PR) for PLTP and CETP. Bar graphs represent the mean value for n = 6 participants, error bars represent SD, and open circles represent values per participant.

Journal: JCI insight

Article Title: Metabolism of PLTP, CETP, and LCAT on multiple HDL sizes using the Orbitrap Fusion Lumos.

doi: 10.1172/jci.insight.143526

Figure Lengend Snippet: Figure 3. Compartmental models and kinetics parameters for PLTP and CETP in the larger alpha HDL size fractions. (A) Compartmental model for PLTP and CETP (the average of n = 6 participants). PLTP flux into alpha1 is approximately 45% from the source (0.010 mg/kg/d) and 55% from the smaller alpha2 (0.012 mg/kg/d). Approximately 75% of PLTP on alpha2 is transferred to alpha0 and alpha1 (0.10 and 0.59 pool/d, respectively) while the remaining 25% is removed from the model system (0.20 pool/d). CETP appears on alpha1 and alpha2 via direct secretion. (B) Enrichment curve fits generated from the models in A, participant 1. (C) FCR and production rate (PR) for PLTP and CETP. Bar graphs represent the mean value for n = 6 participants, error bars represent SD, and open circles represent values per participant.

Article Snippet: Each protein was quantified using the following peptide standards: APOA1 (THLAPYSDEL[R-labeled]), APOE (LGPLVEQG[R-labeled]), LCAT (SSGLVSNAPGVQI[R-labeled]), CETP (ASYPDITGE[K-labeled]), and PLTP (AVEPQLQEEE[R-labeled]) (New England Peptides, NEP, Supplemental Table 2).

Techniques: Generated