phospho pkc Search Results


pkc δ thr507  (Elabscience Biotechnology)
96
Elabscience Biotechnology pkc δ thr507
The inhibition of EGFR/PKC-δ/NF-κB proteins phosphorylation and induction of apoptosis-related proteins by imipramine in CL1-5-F4/ NF-κB-luc2 bearing tumor. (A–C) The protein expression from IHC of EGFR (Try 1068), PKC-δ (Thr507), NF-κB (Ser536), cleaved caspase-3, -8, -9, MMP-9, XIAP, MCL-1 and their quantification bar chart are presented. (D, E) The tumor ex vivo Western blotting from each mice of cleaved caspase-3, -8, -9 and PARP-1 is presented. ( ** p < 0.01 vs . vehicle; scale bar =100 μm).
Pkc δ Thr507, supplied by Elabscience Biotechnology, 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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Average 96 stars, based on 1 article reviews
pkc δ thr507 - by Bioz Stars, 2026-09
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rabbit anti pkcε pser substrate  (Cell Signaling Technology Inc)
96
Cell Signaling Technology Inc rabbit anti pkcε pser substrate
The inhibition of EGFR/PKC-δ/NF-κB proteins phosphorylation and induction of apoptosis-related proteins by imipramine in CL1-5-F4/ NF-κB-luc2 bearing tumor. (A–C) The protein expression from IHC of EGFR (Try 1068), PKC-δ (Thr507), NF-κB (Ser536), cleaved caspase-3, -8, -9, MMP-9, XIAP, MCL-1 and their quantification bar chart are presented. (D, E) The tumor ex vivo Western blotting from each mice of cleaved caspase-3, -8, -9 and PARP-1 is presented. ( ** p < 0.01 vs . vehicle; scale bar =100 μm).
Rabbit Anti Pkcε Pser Substrate, 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
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Average 96 stars, based on 1 article reviews
rabbit anti pkcε pser substrate - by Bioz Stars, 2026-09
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pser660 pkcβ  (Cell Signaling Technology Inc)
96
Cell Signaling Technology Inc pser660 pkcβ
The inhibition of EGFR/PKC-δ/NF-κB proteins phosphorylation and induction of apoptosis-related proteins by imipramine in CL1-5-F4/ NF-κB-luc2 bearing tumor. (A–C) The protein expression from IHC of EGFR (Try 1068), PKC-δ (Thr507), NF-κB (Ser536), cleaved caspase-3, -8, -9, MMP-9, XIAP, MCL-1 and their quantification bar chart are presented. (D, E) The tumor ex vivo Western blotting from each mice of cleaved caspase-3, -8, -9 and PARP-1 is presented. ( ** p < 0.01 vs . vehicle; scale bar =100 μm).
Pser660 Pkcβ, 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/phospho+pkc/Phospho-PKC+(pan)+(betaII+Ser660)+Antibody/pmc11310474-305-72-74
Average 96 stars, based on 1 article reviews
pser660 pkcβ - by Bioz Stars, 2026-09
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phospho pkc kit 9921  (Cell Signaling Technology Inc)
93
Cell Signaling Technology Inc phospho pkc kit 9921
The inhibition of EGFR/PKC-δ/NF-κB proteins phosphorylation and induction of apoptosis-related proteins by imipramine in CL1-5-F4/ NF-κB-luc2 bearing tumor. (A–C) The protein expression from IHC of EGFR (Try 1068), PKC-δ (Thr507), NF-κB (Ser536), cleaved caspase-3, -8, -9, MMP-9, XIAP, MCL-1 and their quantification bar chart are presented. (D, E) The tumor ex vivo Western blotting from each mice of cleaved caspase-3, -8, -9 and PARP-1 is presented. ( ** p < 0.01 vs . vehicle; scale bar =100 μm).
Phospho Pkc Kit 9921, supplied by Cell Signaling Technology Inc, 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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phospho pkc pan  (Cell Signaling Technology Inc)
93
Cell Signaling Technology Inc phospho pkc pan
( A ) IP3R blocking inhibits PLCE1-induced signal transduction in the axis of <t>PKC/GSK-3β/β-Catenin.</t> ECA-109 cells were transfected with the plasmid expressing Plce1 for 6 hr and then treated with 2-APB (10 µM) for additional 18 hr. ( B ) [Ca 2+ ] blocking represses signal transduction in the axis of PKC/GSK-3β/β-Catenin induced by PLCE1. ECA-109 cells were transfected with the plasmid expressing Plce1 for 6 hr and then treated with BAPTA-AM (10 µM) for additional 18 hr. ( C ) PKC inhibition blocks PLCE1 stimulated signal transduction in the axis of PKC/GSK-3β/β-Catenin. ECA-109 cells were transfected with the plasmid expressing Plce1 . 6 hr post-transfection, cells were treated with 100 nM of Midostaurin for additional 18 hr. ( D ) PKC inhibition represses PLCE1-induced nuclear translocation of β-Catenin in ECA-109 cells. Cells were transfected with the plasmid expressing PLCE1. 6 hr post-transfection, 2-APB (10 µM), BAPTA-AM (10 µM), or Midostaurin (100 nM) was added in culture medium, and cells were cultured for additional 18 hr. Scale bar = 10 µm. Immunofluorescence was used to examine subcellular distribution of β-Catenin. ( E <t>)</t> <t>TAK1</t> counteracts PLCE1-induced signal transduction in the axis of PKC/GSK-3β/β-Catenin. ECA-109 cells were transfected with the plasmids expressing Plce1 or Map3k7 as indicated for 24 hr. ( F ) TAK1 reduces PLCE1-induced nuclear distribution of β-Catenin in ECA-109 cells. Cells were transfected with the plasmids expressing Plce1 or Map3k7 as indicated. Scale bar = 10 µm. ( G ) Dominant negative TAK1 (K63W) fails to block signal transduction in the axis of PKC/GSK-3β/β-Catenin/MMP2 induced by PLCE1. ECA-109 cells were transfected with the plasmids expressing Plce1 or mutated Map3k7 (TAK1 K63W) for 24 hr. ( H ) TAK1 has no effect on PLCE1 S1060A-induced signal transduction in the axis of PKC/GSK-3β/β-Catenin. ECA-109 cells were transfected with the plasmids expressing PLCE1 S1060A or TAK1 for 24 hr. Protein levels were analyzed by western blot, and Actin was used as a loading control. Representative blots were shown. Figure 5—source data 1. PDF file containing original western blots for , indicating the relevant bands. Figure 5—source data 2. Original files for western blot analysis displayed in .
Phospho Pkc Pan, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/phospho+pkc/Phospho-PKC+(pan)+(gamma+Thr514)+Rabbit+mAb/pmc12017773-278-11-71
Average 93 stars, based on 1 article reviews
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rabbit anti phospho pkcsubstrate motif antibody  (Cell Signaling Technology Inc)
95
Cell Signaling Technology Inc rabbit anti phospho pkcsubstrate motif antibody
( A ) IP3R blocking inhibits PLCE1-induced signal transduction in the axis of <t>PKC/GSK-3β/β-Catenin.</t> ECA-109 cells were transfected with the plasmid expressing Plce1 for 6 hr and then treated with 2-APB (10 µM) for additional 18 hr. ( B ) [Ca 2+ ] blocking represses signal transduction in the axis of PKC/GSK-3β/β-Catenin induced by PLCE1. ECA-109 cells were transfected with the plasmid expressing Plce1 for 6 hr and then treated with BAPTA-AM (10 µM) for additional 18 hr. ( C ) PKC inhibition blocks PLCE1 stimulated signal transduction in the axis of PKC/GSK-3β/β-Catenin. ECA-109 cells were transfected with the plasmid expressing Plce1 . 6 hr post-transfection, cells were treated with 100 nM of Midostaurin for additional 18 hr. ( D ) PKC inhibition represses PLCE1-induced nuclear translocation of β-Catenin in ECA-109 cells. Cells were transfected with the plasmid expressing PLCE1. 6 hr post-transfection, 2-APB (10 µM), BAPTA-AM (10 µM), or Midostaurin (100 nM) was added in culture medium, and cells were cultured for additional 18 hr. Scale bar = 10 µm. Immunofluorescence was used to examine subcellular distribution of β-Catenin. ( E <t>)</t> <t>TAK1</t> counteracts PLCE1-induced signal transduction in the axis of PKC/GSK-3β/β-Catenin. ECA-109 cells were transfected with the plasmids expressing Plce1 or Map3k7 as indicated for 24 hr. ( F ) TAK1 reduces PLCE1-induced nuclear distribution of β-Catenin in ECA-109 cells. Cells were transfected with the plasmids expressing Plce1 or Map3k7 as indicated. Scale bar = 10 µm. ( G ) Dominant negative TAK1 (K63W) fails to block signal transduction in the axis of PKC/GSK-3β/β-Catenin/MMP2 induced by PLCE1. ECA-109 cells were transfected with the plasmids expressing Plce1 or mutated Map3k7 (TAK1 K63W) for 24 hr. ( H ) TAK1 has no effect on PLCE1 S1060A-induced signal transduction in the axis of PKC/GSK-3β/β-Catenin. ECA-109 cells were transfected with the plasmids expressing PLCE1 S1060A or TAK1 for 24 hr. Protein levels were analyzed by western blot, and Actin was used as a loading control. Representative blots were shown. Figure 5—source data 1. PDF file containing original western blots for , indicating the relevant bands. Figure 5—source data 2. Original files for western blot analysis displayed in .
Rabbit Anti Phospho Pkcsubstrate Motif Antibody, 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/phospho+pkc/Phospho-PKC+Substrate+Motif+%5B(R%2FK)XpSX(R%2FK)%5D+MultiMab+Rabbit+mAb+mix/pm27599717-71-29-33
Average 95 stars, based on 1 article reviews
rabbit anti phospho pkcsubstrate motif antibody - by Bioz Stars, 2026-09
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rabbit phospho pkc pan thr410 antibody  (Cell Signaling Technology Inc)
93
Cell Signaling Technology Inc rabbit phospho pkc pan thr410 antibody
( A ) IP3R blocking inhibits PLCE1-induced signal transduction in the axis of <t>PKC/GSK-3β/β-Catenin.</t> ECA-109 cells were transfected with the plasmid expressing Plce1 for 6 hr and then treated with 2-APB (10 µM) for additional 18 hr. ( B ) [Ca 2+ ] blocking represses signal transduction in the axis of PKC/GSK-3β/β-Catenin induced by PLCE1. ECA-109 cells were transfected with the plasmid expressing Plce1 for 6 hr and then treated with BAPTA-AM (10 µM) for additional 18 hr. ( C ) PKC inhibition blocks PLCE1 stimulated signal transduction in the axis of PKC/GSK-3β/β-Catenin. ECA-109 cells were transfected with the plasmid expressing Plce1 . 6 hr post-transfection, cells were treated with 100 nM of Midostaurin for additional 18 hr. ( D ) PKC inhibition represses PLCE1-induced nuclear translocation of β-Catenin in ECA-109 cells. Cells were transfected with the plasmid expressing PLCE1. 6 hr post-transfection, 2-APB (10 µM), BAPTA-AM (10 µM), or Midostaurin (100 nM) was added in culture medium, and cells were cultured for additional 18 hr. Scale bar = 10 µm. Immunofluorescence was used to examine subcellular distribution of β-Catenin. ( E <t>)</t> <t>TAK1</t> counteracts PLCE1-induced signal transduction in the axis of PKC/GSK-3β/β-Catenin. ECA-109 cells were transfected with the plasmids expressing Plce1 or Map3k7 as indicated for 24 hr. ( F ) TAK1 reduces PLCE1-induced nuclear distribution of β-Catenin in ECA-109 cells. Cells were transfected with the plasmids expressing Plce1 or Map3k7 as indicated. Scale bar = 10 µm. ( G ) Dominant negative TAK1 (K63W) fails to block signal transduction in the axis of PKC/GSK-3β/β-Catenin/MMP2 induced by PLCE1. ECA-109 cells were transfected with the plasmids expressing Plce1 or mutated Map3k7 (TAK1 K63W) for 24 hr. ( H ) TAK1 has no effect on PLCE1 S1060A-induced signal transduction in the axis of PKC/GSK-3β/β-Catenin. ECA-109 cells were transfected with the plasmids expressing PLCE1 S1060A or TAK1 for 24 hr. Protein levels were analyzed by western blot, and Actin was used as a loading control. Representative blots were shown. Figure 5—source data 1. PDF file containing original western blots for , indicating the relevant bands. Figure 5—source data 2. Original files for western blot analysis displayed in .
Rabbit Phospho Pkc Pan Thr410 Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/phospho+pkc/Phospho-PKC+(pan)+(zeta+Thr410)+Rabbit+mAb/pmc09866800-116-29-43
Average 93 stars, based on 1 article reviews
rabbit phospho pkc pan thr410 antibody - by Bioz Stars, 2026-09
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gap43  (Boster Bio)
93
Boster Bio gap43
( A ) IP3R blocking inhibits PLCE1-induced signal transduction in the axis of <t>PKC/GSK-3β/β-Catenin.</t> ECA-109 cells were transfected with the plasmid expressing Plce1 for 6 hr and then treated with 2-APB (10 µM) for additional 18 hr. ( B ) [Ca 2+ ] blocking represses signal transduction in the axis of PKC/GSK-3β/β-Catenin induced by PLCE1. ECA-109 cells were transfected with the plasmid expressing Plce1 for 6 hr and then treated with BAPTA-AM (10 µM) for additional 18 hr. ( C ) PKC inhibition blocks PLCE1 stimulated signal transduction in the axis of PKC/GSK-3β/β-Catenin. ECA-109 cells were transfected with the plasmid expressing Plce1 . 6 hr post-transfection, cells were treated with 100 nM of Midostaurin for additional 18 hr. ( D ) PKC inhibition represses PLCE1-induced nuclear translocation of β-Catenin in ECA-109 cells. Cells were transfected with the plasmid expressing PLCE1. 6 hr post-transfection, 2-APB (10 µM), BAPTA-AM (10 µM), or Midostaurin (100 nM) was added in culture medium, and cells were cultured for additional 18 hr. Scale bar = 10 µm. Immunofluorescence was used to examine subcellular distribution of β-Catenin. ( E <t>)</t> <t>TAK1</t> counteracts PLCE1-induced signal transduction in the axis of PKC/GSK-3β/β-Catenin. ECA-109 cells were transfected with the plasmids expressing Plce1 or Map3k7 as indicated for 24 hr. ( F ) TAK1 reduces PLCE1-induced nuclear distribution of β-Catenin in ECA-109 cells. Cells were transfected with the plasmids expressing Plce1 or Map3k7 as indicated. Scale bar = 10 µm. ( G ) Dominant negative TAK1 (K63W) fails to block signal transduction in the axis of PKC/GSK-3β/β-Catenin/MMP2 induced by PLCE1. ECA-109 cells were transfected with the plasmids expressing Plce1 or mutated Map3k7 (TAK1 K63W) for 24 hr. ( H ) TAK1 has no effect on PLCE1 S1060A-induced signal transduction in the axis of PKC/GSK-3β/β-Catenin. ECA-109 cells were transfected with the plasmids expressing PLCE1 S1060A or TAK1 for 24 hr. Protein levels were analyzed by western blot, and Actin was used as a loading control. Representative blots were shown. Figure 5—source data 1. PDF file containing original western blots for , indicating the relevant bands. Figure 5—source data 2. Original files for western blot analysis displayed in .
Gap43, supplied by Boster Bio, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/phospho+pkc/Anti-Phospho-p62+(Ser28)+SQSTM1+Antibody/10__36721_slash_pjps__2026__39__6__154__1-41-14-11
Average 93 stars, based on 1 article reviews
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lance ultra europium anti phospho pkc ala25ser peptide antibody  (Revvity)
91
Revvity lance ultra europium anti phospho pkc ala25ser peptide antibody
( A ) IP3R blocking inhibits PLCE1-induced signal transduction in the axis of <t>PKC/GSK-3β/β-Catenin.</t> ECA-109 cells were transfected with the plasmid expressing Plce1 for 6 hr and then treated with 2-APB (10 µM) for additional 18 hr. ( B ) [Ca 2+ ] blocking represses signal transduction in the axis of PKC/GSK-3β/β-Catenin induced by PLCE1. ECA-109 cells were transfected with the plasmid expressing Plce1 for 6 hr and then treated with BAPTA-AM (10 µM) for additional 18 hr. ( C ) PKC inhibition blocks PLCE1 stimulated signal transduction in the axis of PKC/GSK-3β/β-Catenin. ECA-109 cells were transfected with the plasmid expressing Plce1 . 6 hr post-transfection, cells were treated with 100 nM of Midostaurin for additional 18 hr. ( D ) PKC inhibition represses PLCE1-induced nuclear translocation of β-Catenin in ECA-109 cells. Cells were transfected with the plasmid expressing PLCE1. 6 hr post-transfection, 2-APB (10 µM), BAPTA-AM (10 µM), or Midostaurin (100 nM) was added in culture medium, and cells were cultured for additional 18 hr. Scale bar = 10 µm. Immunofluorescence was used to examine subcellular distribution of β-Catenin. ( E <t>)</t> <t>TAK1</t> counteracts PLCE1-induced signal transduction in the axis of PKC/GSK-3β/β-Catenin. ECA-109 cells were transfected with the plasmids expressing Plce1 or Map3k7 as indicated for 24 hr. ( F ) TAK1 reduces PLCE1-induced nuclear distribution of β-Catenin in ECA-109 cells. Cells were transfected with the plasmids expressing Plce1 or Map3k7 as indicated. Scale bar = 10 µm. ( G ) Dominant negative TAK1 (K63W) fails to block signal transduction in the axis of PKC/GSK-3β/β-Catenin/MMP2 induced by PLCE1. ECA-109 cells were transfected with the plasmids expressing Plce1 or mutated Map3k7 (TAK1 K63W) for 24 hr. ( H ) TAK1 has no effect on PLCE1 S1060A-induced signal transduction in the axis of PKC/GSK-3β/β-Catenin. ECA-109 cells were transfected with the plasmids expressing PLCE1 S1060A or TAK1 for 24 hr. Protein levels were analyzed by western blot, and Actin was used as a loading control. Representative blots were shown. Figure 5—source data 1. PDF file containing original western blots for , indicating the relevant bands. Figure 5—source data 2. Original files for western blot analysis displayed in .
Lance Ultra Europium Anti Phospho Pkc Ala25ser Peptide Antibody, supplied by Revvity, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/phospho+pkc/LANCE+Ultra+Europium-anti-phospho-PKC+(Ala25Ser)+peptide+Antibody/bio_rxiv__2023__06__01__543325-194-29-35
Average 91 stars, based on 1 article reviews
lance ultra europium anti phospho pkc ala25ser peptide antibody - by Bioz Stars, 2026-09
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aging pkcε  (Biorbyt)
90
Biorbyt aging pkcε
( A ) IP3R blocking inhibits PLCE1-induced signal transduction in the axis of <t>PKC/GSK-3β/β-Catenin.</t> ECA-109 cells were transfected with the plasmid expressing Plce1 for 6 hr and then treated with 2-APB (10 µM) for additional 18 hr. ( B ) [Ca 2+ ] blocking represses signal transduction in the axis of PKC/GSK-3β/β-Catenin induced by PLCE1. ECA-109 cells were transfected with the plasmid expressing Plce1 for 6 hr and then treated with BAPTA-AM (10 µM) for additional 18 hr. ( C ) PKC inhibition blocks PLCE1 stimulated signal transduction in the axis of PKC/GSK-3β/β-Catenin. ECA-109 cells were transfected with the plasmid expressing Plce1 . 6 hr post-transfection, cells were treated with 100 nM of Midostaurin for additional 18 hr. ( D ) PKC inhibition represses PLCE1-induced nuclear translocation of β-Catenin in ECA-109 cells. Cells were transfected with the plasmid expressing PLCE1. 6 hr post-transfection, 2-APB (10 µM), BAPTA-AM (10 µM), or Midostaurin (100 nM) was added in culture medium, and cells were cultured for additional 18 hr. Scale bar = 10 µm. Immunofluorescence was used to examine subcellular distribution of β-Catenin. ( E <t>)</t> <t>TAK1</t> counteracts PLCE1-induced signal transduction in the axis of PKC/GSK-3β/β-Catenin. ECA-109 cells were transfected with the plasmids expressing Plce1 or Map3k7 as indicated for 24 hr. ( F ) TAK1 reduces PLCE1-induced nuclear distribution of β-Catenin in ECA-109 cells. Cells were transfected with the plasmids expressing Plce1 or Map3k7 as indicated. Scale bar = 10 µm. ( G ) Dominant negative TAK1 (K63W) fails to block signal transduction in the axis of PKC/GSK-3β/β-Catenin/MMP2 induced by PLCE1. ECA-109 cells were transfected with the plasmids expressing Plce1 or mutated Map3k7 (TAK1 K63W) for 24 hr. ( H ) TAK1 has no effect on PLCE1 S1060A-induced signal transduction in the axis of PKC/GSK-3β/β-Catenin. ECA-109 cells were transfected with the plasmids expressing PLCE1 S1060A or TAK1 for 24 hr. Protein levels were analyzed by western blot, and Actin was used as a loading control. Representative blots were shown. Figure 5—source data 1. PDF file containing original western blots for , indicating the relevant bands. Figure 5—source data 2. Original files for western blot analysis displayed in .
Aging Pkcε, supplied by Biorbyt, 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/phospho+pkc/PKC+Epsilon+(Phospho+Ser729antibody/pm28846530-60-60-70
Average 90 stars, based on 1 article reviews
aging pkcε - by Bioz Stars, 2026-09
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anti phospho pkcɛ ser729  (Biorbyt)
93
Biorbyt anti phospho pkcɛ ser729
( A ) Representative confocal immunofluorescence staining of Rac1 in HUVECs treated with vehicle (Ctrl) or sortilin alone or pretreated with the S1P3 inhibitor TY52156. Arrows indicate membrane translocation of Rac1. Scale bar: 10 μm. Insets show higher magnification, zoom ×4.7. ( B ) Acetylcholine-evoked vasorelaxation in WT mesenteric arteries exposed to vehicle, sortilin alone, or sortilin in the presence of NSC23766 ( n = 3). ( C ) Acetylcholine-evoked vasorelaxation in WT mesenteric arteries treated with vehicle or sortilin alone or pretreated with either ML171 or GSK2795039 before sortilin stimulation ( n = 3). ( D ) NOX activity in HUVECs treated with vehicle or sortilin alone or preincubated with ML171 or GSK2795039 before sortilin ( n = 4–5 replicates from 3 independent experiments). ( E ) NOX activity in WT and gp91 phox–/– mesenteric arteries exposed to vehicle or sortilin ( n = 3 replicates from 3 independent experiments). Data are expressed as increase of chemiluminescence per minute in arbitrary units. ( F ) Acetylcholine-evoked vasorelaxation in mesenteric arteries from WT and gp91 phox–/– mice exposed to vehicle or sortilin ( n = 5). ( G ) Representative immunoblots and densitometric analyses of 3 independent experiments evaluating protein levels of phospho-Tyr579-PYK2, <t>phospho-Ser729-PKCɛ,</t> phospho-Thr497-PKCα, PKC, S1P3, and Rac1-GTP in HUVECs treated with vehicle or sortilin in the presence or absence of TY52156 or GSK2795039. Data are represented as mean ± SD. One-way ANOVA ( D , E , and G ) or 2-way ANOVA ( B , C , and F ) followed by Bonferroni’s post hoc test was used. ( C ) * P < 0.0001 versus vehicle or GSK2795039 plus sortilin at the same acetylcholine concentration (as indicated by color code).
Anti Phospho Pkcɛ Ser729, supplied by Biorbyt, 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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Image Search Results


The inhibition of EGFR/PKC-δ/NF-κB proteins phosphorylation and induction of apoptosis-related proteins by imipramine in CL1-5-F4/ NF-κB-luc2 bearing tumor. (A–C) The protein expression from IHC of EGFR (Try 1068), PKC-δ (Thr507), NF-κB (Ser536), cleaved caspase-3, -8, -9, MMP-9, XIAP, MCL-1 and their quantification bar chart are presented. (D, E) The tumor ex vivo Western blotting from each mice of cleaved caspase-3, -8, -9 and PARP-1 is presented. ( ** p < 0.01 vs . vehicle; scale bar =100 μm).

Journal: Frontiers in Oncology

Article Title: Suppression of EGFR/PKC-δ/NF-κB Signaling Associated With Imipramine-Inhibited Progression of Non-Small Cell Lung Cancer

doi: 10.3389/fonc.2021.735183

Figure Lengend Snippet: The inhibition of EGFR/PKC-δ/NF-κB proteins phosphorylation and induction of apoptosis-related proteins by imipramine in CL1-5-F4/ NF-κB-luc2 bearing tumor. (A–C) The protein expression from IHC of EGFR (Try 1068), PKC-δ (Thr507), NF-κB (Ser536), cleaved caspase-3, -8, -9, MMP-9, XIAP, MCL-1 and their quantification bar chart are presented. (D, E) The tumor ex vivo Western blotting from each mice of cleaved caspase-3, -8, -9 and PARP-1 is presented. ( ** p < 0.01 vs . vehicle; scale bar =100 μm).

Article Snippet: Primary antibodies against Matrix metalloproteinase-9 (MMP-9) (AB19016, Millipore), vascular endothelial growth factor (VEGF) (ab1316, Abcam, Cambridge, UK), EGFR (Try 1068) (#2234, Cell signaling, Danvers, MA, USA), EGFR (E-AB-63555, Elabscience, Houston, TX, USA), PKC-δ (Thr507) (E-AB-20968, Elabscience), PKC-δ (E-AB-14675, Elabscience), NF-κB p65 (Ser536) (E-AB-70335, Elabscience), NF-κB p65 (E-AB-22066, Elabscience), cell leukemia-1 (MCL-1) (BV-438, BioVision), cellular FLICE (FADD-like IL-1β-converting enzyme)-inhibitory protein (cFLIP) (D16A8, Cell signaling), X-linked inhibitor of apoptosis protein (XIAP) (PA5-29253, Thermo Fisher Scientific), Fas (E-AB-40063, Elabscience), Fas ligand (FasL) (E-AB-31410, Elabscience), cleaved caspase-3 (E-AB-30004, Elabscience), cleaved caspase-8 (E-AB-22107, Elabscience), cleaved caspase-9 (#9505, Cell Signaling Technology), PARP-1 (#9532, Cell Signaling Technology) and β-actin (sc-47778, Santa Cruz Biotechnology, Dallas, Texas, Waltam, MA, USA) for Western blotting were purchased from different companies as listed.

Techniques: Inhibition, Phospho-proteomics, Expressing, Ex Vivo, Western Blot

( A ) IP3R blocking inhibits PLCE1-induced signal transduction in the axis of PKC/GSK-3β/β-Catenin. ECA-109 cells were transfected with the plasmid expressing Plce1 for 6 hr and then treated with 2-APB (10 µM) for additional 18 hr. ( B ) [Ca 2+ ] blocking represses signal transduction in the axis of PKC/GSK-3β/β-Catenin induced by PLCE1. ECA-109 cells were transfected with the plasmid expressing Plce1 for 6 hr and then treated with BAPTA-AM (10 µM) for additional 18 hr. ( C ) PKC inhibition blocks PLCE1 stimulated signal transduction in the axis of PKC/GSK-3β/β-Catenin. ECA-109 cells were transfected with the plasmid expressing Plce1 . 6 hr post-transfection, cells were treated with 100 nM of Midostaurin for additional 18 hr. ( D ) PKC inhibition represses PLCE1-induced nuclear translocation of β-Catenin in ECA-109 cells. Cells were transfected with the plasmid expressing PLCE1. 6 hr post-transfection, 2-APB (10 µM), BAPTA-AM (10 µM), or Midostaurin (100 nM) was added in culture medium, and cells were cultured for additional 18 hr. Scale bar = 10 µm. Immunofluorescence was used to examine subcellular distribution of β-Catenin. ( E ) TAK1 counteracts PLCE1-induced signal transduction in the axis of PKC/GSK-3β/β-Catenin. ECA-109 cells were transfected with the plasmids expressing Plce1 or Map3k7 as indicated for 24 hr. ( F ) TAK1 reduces PLCE1-induced nuclear distribution of β-Catenin in ECA-109 cells. Cells were transfected with the plasmids expressing Plce1 or Map3k7 as indicated. Scale bar = 10 µm. ( G ) Dominant negative TAK1 (K63W) fails to block signal transduction in the axis of PKC/GSK-3β/β-Catenin/MMP2 induced by PLCE1. ECA-109 cells were transfected with the plasmids expressing Plce1 or mutated Map3k7 (TAK1 K63W) for 24 hr. ( H ) TAK1 has no effect on PLCE1 S1060A-induced signal transduction in the axis of PKC/GSK-3β/β-Catenin. ECA-109 cells were transfected with the plasmids expressing PLCE1 S1060A or TAK1 for 24 hr. Protein levels were analyzed by western blot, and Actin was used as a loading control. Representative blots were shown. Figure 5—source data 1. PDF file containing original western blots for , indicating the relevant bands. Figure 5—source data 2. Original files for western blot analysis displayed in .

Journal: eLife

Article Title: TAK1-mediated phosphorylation of PLCE1 represses PIP2 hydrolysis to impede esophageal squamous cancer metastasis

doi: 10.7554/eLife.97373

Figure Lengend Snippet: ( A ) IP3R blocking inhibits PLCE1-induced signal transduction in the axis of PKC/GSK-3β/β-Catenin. ECA-109 cells were transfected with the plasmid expressing Plce1 for 6 hr and then treated with 2-APB (10 µM) for additional 18 hr. ( B ) [Ca 2+ ] blocking represses signal transduction in the axis of PKC/GSK-3β/β-Catenin induced by PLCE1. ECA-109 cells were transfected with the plasmid expressing Plce1 for 6 hr and then treated with BAPTA-AM (10 µM) for additional 18 hr. ( C ) PKC inhibition blocks PLCE1 stimulated signal transduction in the axis of PKC/GSK-3β/β-Catenin. ECA-109 cells were transfected with the plasmid expressing Plce1 . 6 hr post-transfection, cells were treated with 100 nM of Midostaurin for additional 18 hr. ( D ) PKC inhibition represses PLCE1-induced nuclear translocation of β-Catenin in ECA-109 cells. Cells were transfected with the plasmid expressing PLCE1. 6 hr post-transfection, 2-APB (10 µM), BAPTA-AM (10 µM), or Midostaurin (100 nM) was added in culture medium, and cells were cultured for additional 18 hr. Scale bar = 10 µm. Immunofluorescence was used to examine subcellular distribution of β-Catenin. ( E ) TAK1 counteracts PLCE1-induced signal transduction in the axis of PKC/GSK-3β/β-Catenin. ECA-109 cells were transfected with the plasmids expressing Plce1 or Map3k7 as indicated for 24 hr. ( F ) TAK1 reduces PLCE1-induced nuclear distribution of β-Catenin in ECA-109 cells. Cells were transfected with the plasmids expressing Plce1 or Map3k7 as indicated. Scale bar = 10 µm. ( G ) Dominant negative TAK1 (K63W) fails to block signal transduction in the axis of PKC/GSK-3β/β-Catenin/MMP2 induced by PLCE1. ECA-109 cells were transfected with the plasmids expressing Plce1 or mutated Map3k7 (TAK1 K63W) for 24 hr. ( H ) TAK1 has no effect on PLCE1 S1060A-induced signal transduction in the axis of PKC/GSK-3β/β-Catenin. ECA-109 cells were transfected with the plasmids expressing PLCE1 S1060A or TAK1 for 24 hr. Protein levels were analyzed by western blot, and Actin was used as a loading control. Representative blots were shown. Figure 5—source data 1. PDF file containing original western blots for , indicating the relevant bands. Figure 5—source data 2. Original files for western blot analysis displayed in .

Article Snippet: Rabbit monoclonal antibodies against TAK1 (#5206), phospho-TAK1 (Ser412, #9339), PKCα (#2056), phospho-PKC (pan) (gamma Thr514) (#38938), GSK-3β (#9315), phospho-GSK-3β (Ser9) (#5558), β-Catenin (#8480), phospho-β-Catenin (Ser33/37/Thr41) (#9561), MMP-2 (#87809), mouse monoclonal antibodies against Actin (#3700), Myc-Tag (Sepharose Bead Conjugate) (#55464), Epithelial-Mesenchymal Transition (EMT) antibody sample kit (#9782), phosphor-IKK (#2078), IKK (#61294), phosphor-JNK (#4668), JNK (#9252), phospho-ERK (#4370), ERK (#9102), phospho-P38 MAPK (#9211), P38 MPAK (#9212), and normal rabbit IgG (#2729) were from Cell Signaling Technology (Beverley, MA, USA).

Techniques: Blocking Assay, Transduction, Transfection, Plasmid Preparation, Expressing, Inhibition, Translocation Assay, Cell Culture, Immunofluorescence, Dominant Negative Mutation, Western Blot, Control

( A–F ) Quantified data for the western blots as shown in . n=3 biologically independent replicates. Data are presented as mean ± SD. Statistical significance was tested by two-tailed one-way ANOVA test. *p<0.05, **p<0.01, and ***p<0.001. Figure 5—figure supplement 7—source data 1. TAK1 mitigates PLCE1-induced signal transduction in the axis of PKC/GSK-3β/β-Catenin.

Journal: eLife

Article Title: TAK1-mediated phosphorylation of PLCE1 represses PIP2 hydrolysis to impede esophageal squamous cancer metastasis

doi: 10.7554/eLife.97373

Figure Lengend Snippet: ( A–F ) Quantified data for the western blots as shown in . n=3 biologically independent replicates. Data are presented as mean ± SD. Statistical significance was tested by two-tailed one-way ANOVA test. *p<0.05, **p<0.01, and ***p<0.001. Figure 5—figure supplement 7—source data 1. TAK1 mitigates PLCE1-induced signal transduction in the axis of PKC/GSK-3β/β-Catenin.

Article Snippet: Rabbit monoclonal antibodies against TAK1 (#5206), phospho-TAK1 (Ser412, #9339), PKCα (#2056), phospho-PKC (pan) (gamma Thr514) (#38938), GSK-3β (#9315), phospho-GSK-3β (Ser9) (#5558), β-Catenin (#8480), phospho-β-Catenin (Ser33/37/Thr41) (#9561), MMP-2 (#87809), mouse monoclonal antibodies against Actin (#3700), Myc-Tag (Sepharose Bead Conjugate) (#55464), Epithelial-Mesenchymal Transition (EMT) antibody sample kit (#9782), phosphor-IKK (#2078), IKK (#61294), phosphor-JNK (#4668), JNK (#9252), phospho-ERK (#4370), ERK (#9102), phospho-P38 MAPK (#9211), P38 MPAK (#9212), and normal rabbit IgG (#2729) were from Cell Signaling Technology (Beverley, MA, USA).

Techniques: Western Blot, Two Tailed Test, Transduction

Each mouse was intravenously injected with 1×10 6 ECA-109 cells diluted in 100 µl PBS. Mice were treated with Takinib at the dosage of 50 mg/kg/day for 15 days, mice in control group were received vehicle (corn oil). Eight weeks later, mice were sacrificed, and the lungs and livers from each group were collected and photographed. ( A ) Typical images of specimens. ( B ) Hematoxylin and eosin staining of metastatic nodules in lungs. ( C ) The number of nodules in lungs. ( D ) Takinib treatment induces signal transduction in the axis of PKC/GSK-3β/β-Catenin. Protein levels were analyzed by western blot, and Actin was used as a loading control. n=3 biologically independent replicates. ( E ) Quantitative analysis of the western blot data shown in ( D ). Data are presented as mean ± SD. Statistical significance was tested by unpaired Student’s t-test. * p < 0.05 , ** p<0.01, and *** p<0.001 . Figure 6—source data 1. Inhibition of TAK1 by Takinib promotes esophageal squamous cell carcinoma (ESCC) metastasis in nude mice. Figure 6—source data 2. PDF file containing original western blots for , indicating the relevant bands. Figure 6—source data 3. Original files for western blot analysis displayed in .

Journal: eLife

Article Title: TAK1-mediated phosphorylation of PLCE1 represses PIP2 hydrolysis to impede esophageal squamous cancer metastasis

doi: 10.7554/eLife.97373

Figure Lengend Snippet: Each mouse was intravenously injected with 1×10 6 ECA-109 cells diluted in 100 µl PBS. Mice were treated with Takinib at the dosage of 50 mg/kg/day for 15 days, mice in control group were received vehicle (corn oil). Eight weeks later, mice were sacrificed, and the lungs and livers from each group were collected and photographed. ( A ) Typical images of specimens. ( B ) Hematoxylin and eosin staining of metastatic nodules in lungs. ( C ) The number of nodules in lungs. ( D ) Takinib treatment induces signal transduction in the axis of PKC/GSK-3β/β-Catenin. Protein levels were analyzed by western blot, and Actin was used as a loading control. n=3 biologically independent replicates. ( E ) Quantitative analysis of the western blot data shown in ( D ). Data are presented as mean ± SD. Statistical significance was tested by unpaired Student’s t-test. * p < 0.05 , ** p<0.01, and *** p<0.001 . Figure 6—source data 1. Inhibition of TAK1 by Takinib promotes esophageal squamous cell carcinoma (ESCC) metastasis in nude mice. Figure 6—source data 2. PDF file containing original western blots for , indicating the relevant bands. Figure 6—source data 3. Original files for western blot analysis displayed in .

Article Snippet: Rabbit monoclonal antibodies against TAK1 (#5206), phospho-TAK1 (Ser412, #9339), PKCα (#2056), phospho-PKC (pan) (gamma Thr514) (#38938), GSK-3β (#9315), phospho-GSK-3β (Ser9) (#5558), β-Catenin (#8480), phospho-β-Catenin (Ser33/37/Thr41) (#9561), MMP-2 (#87809), mouse monoclonal antibodies against Actin (#3700), Myc-Tag (Sepharose Bead Conjugate) (#55464), Epithelial-Mesenchymal Transition (EMT) antibody sample kit (#9782), phosphor-IKK (#2078), IKK (#61294), phosphor-JNK (#4668), JNK (#9252), phospho-ERK (#4370), ERK (#9102), phospho-P38 MAPK (#9211), P38 MPAK (#9212), and normal rabbit IgG (#2729) were from Cell Signaling Technology (Beverley, MA, USA).

Techniques: Injection, Control, Staining, Transduction, Western Blot, Inhibition

ECA-109 cells were transduced with lentivirus bearing PLCE1 shRNA (LV-shPLCE1) or NC shRNA (LV-shPLCE1 NC). Each mouse was intravenously injected with the LV transduced cells (1×10 6 cells/mouse). Eight weeks later, mice were sacrificed, and the lungs and livers from each group were collected and photographed. ( A ) Typical images of lung specimens. ( B ) Hematoxylin and eosin staining of metastatic nodules in lungs. ( C ) The number of nodules in lungs. ( D ) PLCE1 knockdown represses signal transduction in the axis of PKC/GSK-3β/β-Catenin. Protein levels were analyzed by western blot, and Actin was used as a loading control. n=3 biologically independent replicates. ( E ) Quantitative analysis of the western blot data shown in ( D ). Data are presented as mean ± SD. Statistical significance was tested by unpaired Student’s t-test. ** p<0.01 and *** p<0.001 . Figure 7—source data 1. PLCE1 knockdown inhibits esophageal squamous cell carcinoma (ESCC) metastasis in nude mice. Figure 7—source data 2. PDF file containing original western blots for , indicating the relevant bands. Figure 7—source data 3. Original files for western blot analysis displayed in .

Journal: eLife

Article Title: TAK1-mediated phosphorylation of PLCE1 represses PIP2 hydrolysis to impede esophageal squamous cancer metastasis

doi: 10.7554/eLife.97373

Figure Lengend Snippet: ECA-109 cells were transduced with lentivirus bearing PLCE1 shRNA (LV-shPLCE1) or NC shRNA (LV-shPLCE1 NC). Each mouse was intravenously injected with the LV transduced cells (1×10 6 cells/mouse). Eight weeks later, mice were sacrificed, and the lungs and livers from each group were collected and photographed. ( A ) Typical images of lung specimens. ( B ) Hematoxylin and eosin staining of metastatic nodules in lungs. ( C ) The number of nodules in lungs. ( D ) PLCE1 knockdown represses signal transduction in the axis of PKC/GSK-3β/β-Catenin. Protein levels were analyzed by western blot, and Actin was used as a loading control. n=3 biologically independent replicates. ( E ) Quantitative analysis of the western blot data shown in ( D ). Data are presented as mean ± SD. Statistical significance was tested by unpaired Student’s t-test. ** p<0.01 and *** p<0.001 . Figure 7—source data 1. PLCE1 knockdown inhibits esophageal squamous cell carcinoma (ESCC) metastasis in nude mice. Figure 7—source data 2. PDF file containing original western blots for , indicating the relevant bands. Figure 7—source data 3. Original files for western blot analysis displayed in .

Article Snippet: Rabbit monoclonal antibodies against TAK1 (#5206), phospho-TAK1 (Ser412, #9339), PKCα (#2056), phospho-PKC (pan) (gamma Thr514) (#38938), GSK-3β (#9315), phospho-GSK-3β (Ser9) (#5558), β-Catenin (#8480), phospho-β-Catenin (Ser33/37/Thr41) (#9561), MMP-2 (#87809), mouse monoclonal antibodies against Actin (#3700), Myc-Tag (Sepharose Bead Conjugate) (#55464), Epithelial-Mesenchymal Transition (EMT) antibody sample kit (#9782), phosphor-IKK (#2078), IKK (#61294), phosphor-JNK (#4668), JNK (#9252), phospho-ERK (#4370), ERK (#9102), phospho-P38 MAPK (#9211), P38 MPAK (#9212), and normal rabbit IgG (#2729) were from Cell Signaling Technology (Beverley, MA, USA).

Techniques: Transduction, shRNA, Injection, Staining, Knockdown, Western Blot, Control

Journal: eLife

Article Title: TAK1-mediated phosphorylation of PLCE1 represses PIP2 hydrolysis to impede esophageal squamous cancer metastasis

doi: 10.7554/eLife.97373

Figure Lengend Snippet:

Article Snippet: Rabbit monoclonal antibodies against TAK1 (#5206), phospho-TAK1 (Ser412, #9339), PKCα (#2056), phospho-PKC (pan) (gamma Thr514) (#38938), GSK-3β (#9315), phospho-GSK-3β (Ser9) (#5558), β-Catenin (#8480), phospho-β-Catenin (Ser33/37/Thr41) (#9561), MMP-2 (#87809), mouse monoclonal antibodies against Actin (#3700), Myc-Tag (Sepharose Bead Conjugate) (#55464), Epithelial-Mesenchymal Transition (EMT) antibody sample kit (#9782), phosphor-IKK (#2078), IKK (#61294), phosphor-JNK (#4668), JNK (#9252), phospho-ERK (#4370), ERK (#9102), phospho-P38 MAPK (#9211), P38 MPAK (#9212), and normal rabbit IgG (#2729) were from Cell Signaling Technology (Beverley, MA, USA).

Techniques: Transfection, Construct, shRNA, Recombinant, Plasmid Preparation, Sequencing, Activity Assay, Enzyme-linked Immunosorbent Assay, Software

( A ) Representative confocal immunofluorescence staining of Rac1 in HUVECs treated with vehicle (Ctrl) or sortilin alone or pretreated with the S1P3 inhibitor TY52156. Arrows indicate membrane translocation of Rac1. Scale bar: 10 μm. Insets show higher magnification, zoom ×4.7. ( B ) Acetylcholine-evoked vasorelaxation in WT mesenteric arteries exposed to vehicle, sortilin alone, or sortilin in the presence of NSC23766 ( n = 3). ( C ) Acetylcholine-evoked vasorelaxation in WT mesenteric arteries treated with vehicle or sortilin alone or pretreated with either ML171 or GSK2795039 before sortilin stimulation ( n = 3). ( D ) NOX activity in HUVECs treated with vehicle or sortilin alone or preincubated with ML171 or GSK2795039 before sortilin ( n = 4–5 replicates from 3 independent experiments). ( E ) NOX activity in WT and gp91 phox–/– mesenteric arteries exposed to vehicle or sortilin ( n = 3 replicates from 3 independent experiments). Data are expressed as increase of chemiluminescence per minute in arbitrary units. ( F ) Acetylcholine-evoked vasorelaxation in mesenteric arteries from WT and gp91 phox–/– mice exposed to vehicle or sortilin ( n = 5). ( G ) Representative immunoblots and densitometric analyses of 3 independent experiments evaluating protein levels of phospho-Tyr579-PYK2, phospho-Ser729-PKCɛ, phospho-Thr497-PKCα, PKC, S1P3, and Rac1-GTP in HUVECs treated with vehicle or sortilin in the presence or absence of TY52156 or GSK2795039. Data are represented as mean ± SD. One-way ANOVA ( D , E , and G ) or 2-way ANOVA ( B , C , and F ) followed by Bonferroni’s post hoc test was used. ( C ) * P < 0.0001 versus vehicle or GSK2795039 plus sortilin at the same acetylcholine concentration (as indicated by color code).

Journal: The Journal of Clinical Investigation

Article Title: Targeting the ASMase/S1P pathway protects from sortilin-evoked vascular damage in hypertension

doi: 10.1172/JCI146343

Figure Lengend Snippet: ( A ) Representative confocal immunofluorescence staining of Rac1 in HUVECs treated with vehicle (Ctrl) or sortilin alone or pretreated with the S1P3 inhibitor TY52156. Arrows indicate membrane translocation of Rac1. Scale bar: 10 μm. Insets show higher magnification, zoom ×4.7. ( B ) Acetylcholine-evoked vasorelaxation in WT mesenteric arteries exposed to vehicle, sortilin alone, or sortilin in the presence of NSC23766 ( n = 3). ( C ) Acetylcholine-evoked vasorelaxation in WT mesenteric arteries treated with vehicle or sortilin alone or pretreated with either ML171 or GSK2795039 before sortilin stimulation ( n = 3). ( D ) NOX activity in HUVECs treated with vehicle or sortilin alone or preincubated with ML171 or GSK2795039 before sortilin ( n = 4–5 replicates from 3 independent experiments). ( E ) NOX activity in WT and gp91 phox–/– mesenteric arteries exposed to vehicle or sortilin ( n = 3 replicates from 3 independent experiments). Data are expressed as increase of chemiluminescence per minute in arbitrary units. ( F ) Acetylcholine-evoked vasorelaxation in mesenteric arteries from WT and gp91 phox–/– mice exposed to vehicle or sortilin ( n = 5). ( G ) Representative immunoblots and densitometric analyses of 3 independent experiments evaluating protein levels of phospho-Tyr579-PYK2, phospho-Ser729-PKCɛ, phospho-Thr497-PKCα, PKC, S1P3, and Rac1-GTP in HUVECs treated with vehicle or sortilin in the presence or absence of TY52156 or GSK2795039. Data are represented as mean ± SD. One-way ANOVA ( D , E , and G ) or 2-way ANOVA ( B , C , and F ) followed by Bonferroni’s post hoc test was used. ( C ) * P < 0.0001 versus vehicle or GSK2795039 plus sortilin at the same acetylcholine concentration (as indicated by color code).

Article Snippet: Immunoblotting was performed as previously described , using the following antibodies: anti–phospho-eNOS serine 1177 (Enzo Life Sciences, catalog ALX-804-396-C100, clone 15E2); anti-phospho-eNOS-Thr494 (Cell Signaling Technology, catalog 9574); anti-eNOS (Cell Signaling Technology, catalog 9570); anti–β-actin (Abcam, mAb, catalog ab8226, clone mAbcam 8226); anti–phospho-protein-tyrosine kinase 2-β phospho-Tyr579 (PYK2B pY579) (Elabscience, catalog E-AB-21240); anti–phospho-PKCɛ Ser729 (Biorbyt, catalog orb315664); anti–PKCα (phospho T497) antibody (Abcam, catalog ab76016, clone EP2608Y); anti–PKC-PAN (Sigma-Aldrich, catalog SAB4502356); anti-ASMase (SMPD1; Biorbyt, catalog ORB214591); anti-S1P1 (Immunological Sciences, catalog AB-83739); anti-S1P3 (Elabscience, catalog E-AB-31267); anti-gp91phox (Santa Cruz Biotechnology Inc., catalog sc-130543, clone 54.1); anti-SphK1 (Santa Cruz Biotechnology Inc., catalog sc-365401, clone G-11); anti-SphK2 (MyBioSource, catalog MBS2518663); anti-aCDase (ASAH1; MyBioSource, catalog MBS1492517), and anti-active Rac1 (Rac1-GTP) (Neweast Bioscience, catalog 26903).

Techniques: Immunofluorescence, Staining, Membrane, Translocation Assay, Activity Assay, Western Blot, Concentration Assay