SEK50135 Search Results


  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 97
    Cell Signaling Technology Inc anti erk1 2
    Effect of p38 MAPK silencing, using a specific siRNA (see “Materials and Methods”) and the effect of stearic acid (SA), on ( A ) the level of p38 MAPK, phospho-p38 MAPK, phospho-MAPKAPK-2 (substrate of p38 MAPK); ( B ) the level of phospho-c-Raf, phospho-MEK1/2, <t>phospho-ERK1/2</t> (the ERK signaling pathway); and ( C ) cell growth and viability of NES2Y cells. Cells incubated without siRNA represented control cells. After 18 h of incubation (see “Materials and Methods”) with or without stearic acid (SA) ( A , B ), the level of individual proteins was determined using Western blot analysis and the relevant antibodies (see “Materials and Methods”). A monoclonal antibody against human actin was used to confirm equal protein loading. The data shown were obtained in one representative experiment from three independent experiments. When assessing cell growth and viability ( C ), cells were seeded at a concentration of 2 × 10 4 cells/100 µL of culture medium per well of 96-well plate (see “Materials and Methods”). The number of living cells was determined after 48 h of incubation with or without SA. Non-specific siRNA was used as a negative control. Each column represents the mean of four separate cultures ± SEM. NS (non-significant) when comparing the number of cells incubated with p38 MAPK specific siRNA and with non-specific siRNA.
    Anti Erk1 2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti erk1 2/product/Cell Signaling Technology Inc
    Average 97 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti erk1 2 - by Bioz Stars, 2021-05
    97/100 stars
      Buy from Supplier

    97
    Cell Signaling Technology Inc rabbit anti erk1 2
    PKM2 interacted with Bcl-2 and resisted resveratrol-induced apoptosis in human melanoma cells. Notes: ( A ) Western blots showing the expression of <t>p-ERK1/2,</t> ERK1/2, PKM2, and Bcl-2 in MV3 cells after treating with 200 μM resveratrol for 48 hours. ( B ) RNA was extracted from MV3 cells after treating with 200 μM resveratrol for 48 hours and qPCR was performed using indicated primers for analysis of PKM2 . All data were shown as the means ± SD, * P
    Rabbit Anti Erk1 2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit anti erk1 2/product/Cell Signaling Technology Inc
    Average 97 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit anti erk1 2 - by Bioz Stars, 2021-05
    97/100 stars
      Buy from Supplier

    93
    Cell Signaling Technology Inc anti p p44 42 erk
    PKM2 interacted with Bcl-2 and resisted resveratrol-induced apoptosis in human melanoma cells. Notes: ( A ) Western blots showing the expression of <t>p-ERK1/2,</t> ERK1/2, PKM2, and Bcl-2 in MV3 cells after treating with 200 μM resveratrol for 48 hours. ( B ) RNA was extracted from MV3 cells after treating with 200 μM resveratrol for 48 hours and qPCR was performed using indicated primers for analysis of PKM2 . All data were shown as the means ± SD, * P
    Anti P P44 42 Erk, 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/result/anti p p44 42 erk/product/Cell Signaling Technology Inc
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti p p44 42 erk - by Bioz Stars, 2021-05
    93/100 stars
      Buy from Supplier

    Image Search Results


    Effect of p38 MAPK silencing, using a specific siRNA (see “Materials and Methods”) and the effect of stearic acid (SA), on ( A ) the level of p38 MAPK, phospho-p38 MAPK, phospho-MAPKAPK-2 (substrate of p38 MAPK); ( B ) the level of phospho-c-Raf, phospho-MEK1/2, phospho-ERK1/2 (the ERK signaling pathway); and ( C ) cell growth and viability of NES2Y cells. Cells incubated without siRNA represented control cells. After 18 h of incubation (see “Materials and Methods”) with or without stearic acid (SA) ( A , B ), the level of individual proteins was determined using Western blot analysis and the relevant antibodies (see “Materials and Methods”). A monoclonal antibody against human actin was used to confirm equal protein loading. The data shown were obtained in one representative experiment from three independent experiments. When assessing cell growth and viability ( C ), cells were seeded at a concentration of 2 × 10 4 cells/100 µL of culture medium per well of 96-well plate (see “Materials and Methods”). The number of living cells was determined after 48 h of incubation with or without SA. Non-specific siRNA was used as a negative control. Each column represents the mean of four separate cultures ± SEM. NS (non-significant) when comparing the number of cells incubated with p38 MAPK specific siRNA and with non-specific siRNA.

    Journal: International Journal of Molecular Sciences

    Article Title: p38 MAPK Is Activated but Does Not Play a Key Role during Apoptosis Induction by Saturated Fatty Acid in Human Pancreatic β-Cells

    doi: 10.3390/ijms17020159

    Figure Lengend Snippet: Effect of p38 MAPK silencing, using a specific siRNA (see “Materials and Methods”) and the effect of stearic acid (SA), on ( A ) the level of p38 MAPK, phospho-p38 MAPK, phospho-MAPKAPK-2 (substrate of p38 MAPK); ( B ) the level of phospho-c-Raf, phospho-MEK1/2, phospho-ERK1/2 (the ERK signaling pathway); and ( C ) cell growth and viability of NES2Y cells. Cells incubated without siRNA represented control cells. After 18 h of incubation (see “Materials and Methods”) with or without stearic acid (SA) ( A , B ), the level of individual proteins was determined using Western blot analysis and the relevant antibodies (see “Materials and Methods”). A monoclonal antibody against human actin was used to confirm equal protein loading. The data shown were obtained in one representative experiment from three independent experiments. When assessing cell growth and viability ( C ), cells were seeded at a concentration of 2 × 10 4 cells/100 µL of culture medium per well of 96-well plate (see “Materials and Methods”). The number of living cells was determined after 48 h of incubation with or without SA. Non-specific siRNA was used as a negative control. Each column represents the mean of four separate cultures ± SEM. NS (non-significant) when comparing the number of cells incubated with p38 MAPK specific siRNA and with non-specific siRNA.

    Article Snippet: For western blot analysis, the following primary and secondary antibodies were used: anti-phospho-MKK3/6 (#9236), anti-p38 MAPK (#8690), anti-phospho-p38 MAPK (#4511), anti-phospho-MAPKAPK-2 (#3007), anti-phospho-c-Raf (#9427), anti-phospho-MEK1/2 (#9154), anti-ERK1/2 (#5013), anti-phospho-ERK1/2 (#4370), anti-PARP (#9542), anti-cleaved caspase-7 (#9491), anti-cleaved caspase-8 (#9496), anti-cleaved caspase-9 (#9505) from Cell Signaling Technology (Danvers, MA, USA) and anti-actin (clone AC-40).

    Techniques: Incubation, Western Blot, Concentration Assay, Negative Control

    Effect of p38 MAPK overexpression, using transfection with a specific plasmid (Vector with p38 MAPK) (see “Materials and Methods”) and the effect of stearic acid (SA) on ( A ) the level of p38 MAPK, phospho-p38 MAPK and phospho-MAPKAPK-2 (substrate of p38 MAPK); ( B ) the level of phospho-c-Raf, phospho-MEK1/2, phospho-ERK1/2 (the ERK signaling pathway); and ( C ) cell growth and viability of NES2Y cells. Cells transfected with an empty vector (Empty vector) represented control cells. After 18 h of incubation (see “Materials and Methods”) with or without stearic acid (SA) ( A , B ), the level of individual proteins was determined using Western blot analysis and the relevant antibodies (see “Materials and Methods”). A monoclonal antibody against human actin was used to confirm equal protein loading. The data shown were obtained in one representative experiment from three independent experiments. The fact that the band of p38 MAPK in the control samples is not visible here resulted from a large difference in p38 MAPK content in control and transfected cells. When assessing cell growth and viability ( C ), cells were seeded at a concentration of 2 × 10 4 cells/100 µL of culture medium per well of 96-well plate (see “Materials and Methods”). The number of living cells was determined after 48 h of incubation with or without SA. Each column represents the mean of four separate cultures ± SEM. NS (non-significant) when comparing the number of cells incubated with plasmid DNA containing p38 MAPK (Vector with p38 MAPK) and cells incubated with empty plasmid DNA (empty vector).

    Journal: International Journal of Molecular Sciences

    Article Title: p38 MAPK Is Activated but Does Not Play a Key Role during Apoptosis Induction by Saturated Fatty Acid in Human Pancreatic β-Cells

    doi: 10.3390/ijms17020159

    Figure Lengend Snippet: Effect of p38 MAPK overexpression, using transfection with a specific plasmid (Vector with p38 MAPK) (see “Materials and Methods”) and the effect of stearic acid (SA) on ( A ) the level of p38 MAPK, phospho-p38 MAPK and phospho-MAPKAPK-2 (substrate of p38 MAPK); ( B ) the level of phospho-c-Raf, phospho-MEK1/2, phospho-ERK1/2 (the ERK signaling pathway); and ( C ) cell growth and viability of NES2Y cells. Cells transfected with an empty vector (Empty vector) represented control cells. After 18 h of incubation (see “Materials and Methods”) with or without stearic acid (SA) ( A , B ), the level of individual proteins was determined using Western blot analysis and the relevant antibodies (see “Materials and Methods”). A monoclonal antibody against human actin was used to confirm equal protein loading. The data shown were obtained in one representative experiment from three independent experiments. The fact that the band of p38 MAPK in the control samples is not visible here resulted from a large difference in p38 MAPK content in control and transfected cells. When assessing cell growth and viability ( C ), cells were seeded at a concentration of 2 × 10 4 cells/100 µL of culture medium per well of 96-well plate (see “Materials and Methods”). The number of living cells was determined after 48 h of incubation with or without SA. Each column represents the mean of four separate cultures ± SEM. NS (non-significant) when comparing the number of cells incubated with plasmid DNA containing p38 MAPK (Vector with p38 MAPK) and cells incubated with empty plasmid DNA (empty vector).

    Article Snippet: For western blot analysis, the following primary and secondary antibodies were used: anti-phospho-MKK3/6 (#9236), anti-p38 MAPK (#8690), anti-phospho-p38 MAPK (#4511), anti-phospho-MAPKAPK-2 (#3007), anti-phospho-c-Raf (#9427), anti-phospho-MEK1/2 (#9154), anti-ERK1/2 (#5013), anti-phospho-ERK1/2 (#4370), anti-PARP (#9542), anti-cleaved caspase-7 (#9491), anti-cleaved caspase-8 (#9496), anti-cleaved caspase-9 (#9505) from Cell Signaling Technology (Danvers, MA, USA) and anti-actin (clone AC-40).

    Techniques: Over Expression, Transfection, Plasmid Preparation, Incubation, Western Blot, Concentration Assay

    Effect of 1 mM stearic acid (SA) (see “Materials and Methods”) on ( A ) cell growth and viability; ( B ) the level of cleaved PARP, caspase-7 (C7), caspase-8 (C8) and caspase-9 (C9) (markers of apoptosis); ( C ) the level of phospho-MKK3/6, p38 MAPK, phospho-p38 MAPK, phospho-MAPKAPK-2 (p38 MAPK signaling pathway); and ( D ) the level of phospho-c-Raf, phospho-MEK1/2, ERK1/2, phospho-ERK1/2 (the ERK signaling pathway) in NES2Y cells. Cells incubated without SA represented control cells. After 18 h of incubation (see “Materials and Methods”) for markers of apoptosis ( B ) and 3, 6, 12 and 24 h of incubation for p38 MAPK and ERK pathways members ( C , D ), the levels of individual proteins were determined using Western blot analysis and the relevant antibodies (see “Materials and Methods”). Monoclonal antibody against human actin was used to confirm equal protein loading. The data shown were obtained in one representative experiment from at least three independent experiments. When assessing cell growth and viability ( A ), cells were seeded at a concentration of 2 × 10 4 cells/100 µL of culture medium per well of 96-well plate (see “Materials and Methods”). The number of living cells was determined after 48 h of incubation. Each column represents the mean of four separate cultures ± standard error of the mean (SEM). * p

    Journal: International Journal of Molecular Sciences

    Article Title: p38 MAPK Is Activated but Does Not Play a Key Role during Apoptosis Induction by Saturated Fatty Acid in Human Pancreatic β-Cells

    doi: 10.3390/ijms17020159

    Figure Lengend Snippet: Effect of 1 mM stearic acid (SA) (see “Materials and Methods”) on ( A ) cell growth and viability; ( B ) the level of cleaved PARP, caspase-7 (C7), caspase-8 (C8) and caspase-9 (C9) (markers of apoptosis); ( C ) the level of phospho-MKK3/6, p38 MAPK, phospho-p38 MAPK, phospho-MAPKAPK-2 (p38 MAPK signaling pathway); and ( D ) the level of phospho-c-Raf, phospho-MEK1/2, ERK1/2, phospho-ERK1/2 (the ERK signaling pathway) in NES2Y cells. Cells incubated without SA represented control cells. After 18 h of incubation (see “Materials and Methods”) for markers of apoptosis ( B ) and 3, 6, 12 and 24 h of incubation for p38 MAPK and ERK pathways members ( C , D ), the levels of individual proteins were determined using Western blot analysis and the relevant antibodies (see “Materials and Methods”). Monoclonal antibody against human actin was used to confirm equal protein loading. The data shown were obtained in one representative experiment from at least three independent experiments. When assessing cell growth and viability ( A ), cells were seeded at a concentration of 2 × 10 4 cells/100 µL of culture medium per well of 96-well plate (see “Materials and Methods”). The number of living cells was determined after 48 h of incubation. Each column represents the mean of four separate cultures ± standard error of the mean (SEM). * p

    Article Snippet: For western blot analysis, the following primary and secondary antibodies were used: anti-phospho-MKK3/6 (#9236), anti-p38 MAPK (#8690), anti-phospho-p38 MAPK (#4511), anti-phospho-MAPKAPK-2 (#3007), anti-phospho-c-Raf (#9427), anti-phospho-MEK1/2 (#9154), anti-ERK1/2 (#5013), anti-phospho-ERK1/2 (#4370), anti-PARP (#9542), anti-cleaved caspase-7 (#9491), anti-cleaved caspase-8 (#9496), anti-cleaved caspase-9 (#9505) from Cell Signaling Technology (Danvers, MA, USA) and anti-actin (clone AC-40).

    Techniques: Incubation, Western Blot, Concentration Assay

    Effect of the specific p38 MAPK activator, anisomycin, (see “Materials and Methods”) and the effect of stearic acid (SA) on ( A ) the level of p38 MAPK, phospho-p38 MAPK and phospho-MAPKAPK-2 (substrate of p38 MAPK); ( B ) the level of phospho-c-Raf, phospho-MEK1/2, phospho-ERK1/2 (the ERK signaling pathway); ( C ) cell growth and viability; and ( D ) cleavage of PARP, caspase-7 (C7), caspase-8 (C8) and caspase-9 (C9) (markers of apoptosis) in NES2Y cells. Cells incubated without the activator and SA represented control cells. After 12 h of incubation (see “Materials and Methods”) ( A , B , D ), the level of individual proteins was determined using western blot analysis and the relevant antibodies (see “Materials and Methods”). A monoclonal antibody against human actin was used to confirm equal protein loading. The data shown were obtained in one representative experiment from three independent experiments. When assessing cell growth and viability ( C ), cells were seeded at a concentration of 2 × 10 4 cells/100 µL of culture medium per well of 96-well plate (see “Materials and Methods”). The number of living cells was determined after 48 h of incubation. Each column represents the mean of four separate cultures ± SEM. * p

    Journal: International Journal of Molecular Sciences

    Article Title: p38 MAPK Is Activated but Does Not Play a Key Role during Apoptosis Induction by Saturated Fatty Acid in Human Pancreatic β-Cells

    doi: 10.3390/ijms17020159

    Figure Lengend Snippet: Effect of the specific p38 MAPK activator, anisomycin, (see “Materials and Methods”) and the effect of stearic acid (SA) on ( A ) the level of p38 MAPK, phospho-p38 MAPK and phospho-MAPKAPK-2 (substrate of p38 MAPK); ( B ) the level of phospho-c-Raf, phospho-MEK1/2, phospho-ERK1/2 (the ERK signaling pathway); ( C ) cell growth and viability; and ( D ) cleavage of PARP, caspase-7 (C7), caspase-8 (C8) and caspase-9 (C9) (markers of apoptosis) in NES2Y cells. Cells incubated without the activator and SA represented control cells. After 12 h of incubation (see “Materials and Methods”) ( A , B , D ), the level of individual proteins was determined using western blot analysis and the relevant antibodies (see “Materials and Methods”). A monoclonal antibody against human actin was used to confirm equal protein loading. The data shown were obtained in one representative experiment from three independent experiments. When assessing cell growth and viability ( C ), cells were seeded at a concentration of 2 × 10 4 cells/100 µL of culture medium per well of 96-well plate (see “Materials and Methods”). The number of living cells was determined after 48 h of incubation. Each column represents the mean of four separate cultures ± SEM. * p

    Article Snippet: For western blot analysis, the following primary and secondary antibodies were used: anti-phospho-MKK3/6 (#9236), anti-p38 MAPK (#8690), anti-phospho-p38 MAPK (#4511), anti-phospho-MAPKAPK-2 (#3007), anti-phospho-c-Raf (#9427), anti-phospho-MEK1/2 (#9154), anti-ERK1/2 (#5013), anti-phospho-ERK1/2 (#4370), anti-PARP (#9542), anti-cleaved caspase-7 (#9491), anti-cleaved caspase-8 (#9496), anti-cleaved caspase-9 (#9505) from Cell Signaling Technology (Danvers, MA, USA) and anti-actin (clone AC-40).

    Techniques: Incubation, Western Blot, Concentration Assay

    Effect of the specific p38 MAPK inhibitor, SB202190, (see “Materials and Methods”) and the effect of stearic acid (SA) on ( A ) the level of phospho-MAPKAPK-2 (substrate of p38 MAPK); ( B ) the level of phospho-c-Raf, phospho-MEK1/2, phospho-ERK1/2 (the ERK signaling pathway); and ( C ) cell growth and viability of NES2Y cells. Cells incubated without the inhibitor represented control cells. After 12 h of incubation (see “Materials and Methods”) ( A , B ), the level of individual proteins was determined using Western blot analysis and the relevant antibodies (see “Materials and Methods”). A monoclonal antibody against human actin was used to confirm equal protein loading. The data shown were obtained in one representative experiment from three independent experiments. When assessing cell growth and viability ( C ), cells were seeded at a concentration of 2 × 10 4 cells/100 µL of culture medium per well of 96-well plate (see “Materials and Methods”). The number of living cells was determined after 48 h of incubation. Each column represents the mean of four separate cultures ± SEM. NS (non-significant) when comparing the number of control cells and cells treated with SB202190 as well as when comparing the effect of SA alone and applied together with SB202190.

    Journal: International Journal of Molecular Sciences

    Article Title: p38 MAPK Is Activated but Does Not Play a Key Role during Apoptosis Induction by Saturated Fatty Acid in Human Pancreatic β-Cells

    doi: 10.3390/ijms17020159

    Figure Lengend Snippet: Effect of the specific p38 MAPK inhibitor, SB202190, (see “Materials and Methods”) and the effect of stearic acid (SA) on ( A ) the level of phospho-MAPKAPK-2 (substrate of p38 MAPK); ( B ) the level of phospho-c-Raf, phospho-MEK1/2, phospho-ERK1/2 (the ERK signaling pathway); and ( C ) cell growth and viability of NES2Y cells. Cells incubated without the inhibitor represented control cells. After 12 h of incubation (see “Materials and Methods”) ( A , B ), the level of individual proteins was determined using Western blot analysis and the relevant antibodies (see “Materials and Methods”). A monoclonal antibody against human actin was used to confirm equal protein loading. The data shown were obtained in one representative experiment from three independent experiments. When assessing cell growth and viability ( C ), cells were seeded at a concentration of 2 × 10 4 cells/100 µL of culture medium per well of 96-well plate (see “Materials and Methods”). The number of living cells was determined after 48 h of incubation. Each column represents the mean of four separate cultures ± SEM. NS (non-significant) when comparing the number of control cells and cells treated with SB202190 as well as when comparing the effect of SA alone and applied together with SB202190.

    Article Snippet: For western blot analysis, the following primary and secondary antibodies were used: anti-phospho-MKK3/6 (#9236), anti-p38 MAPK (#8690), anti-phospho-p38 MAPK (#4511), anti-phospho-MAPKAPK-2 (#3007), anti-phospho-c-Raf (#9427), anti-phospho-MEK1/2 (#9154), anti-ERK1/2 (#5013), anti-phospho-ERK1/2 (#4370), anti-PARP (#9542), anti-cleaved caspase-7 (#9491), anti-cleaved caspase-8 (#9496), anti-cleaved caspase-9 (#9505) from Cell Signaling Technology (Danvers, MA, USA) and anti-actin (clone AC-40).

    Techniques: Incubation, Western Blot, Concentration Assay

    PKM2 interacted with Bcl-2 and resisted resveratrol-induced apoptosis in human melanoma cells. Notes: ( A ) Western blots showing the expression of p-ERK1/2, ERK1/2, PKM2, and Bcl-2 in MV3 cells after treating with 200 μM resveratrol for 48 hours. ( B ) RNA was extracted from MV3 cells after treating with 200 μM resveratrol for 48 hours and qPCR was performed using indicated primers for analysis of PKM2 . All data were shown as the means ± SD, * P

    Journal: OncoTargets and therapy

    Article Title: Resveratrol induces apoptosis in human melanoma cell through negatively regulating Erk/PKM2/Bcl-2 axis

    doi: 10.2147/OTT.S186247

    Figure Lengend Snippet: PKM2 interacted with Bcl-2 and resisted resveratrol-induced apoptosis in human melanoma cells. Notes: ( A ) Western blots showing the expression of p-ERK1/2, ERK1/2, PKM2, and Bcl-2 in MV3 cells after treating with 200 μM resveratrol for 48 hours. ( B ) RNA was extracted from MV3 cells after treating with 200 μM resveratrol for 48 hours and qPCR was performed using indicated primers for analysis of PKM2 . All data were shown as the means ± SD, * P

    Article Snippet: Antibodies and reagents The following antibodies and reagents were used for this study: rabbit anti-p53 (1:500, ab1431; Abcam), rabbit anti-p53 (acetyl K382) (1:1,000, ab75754; Abcam), rabbit anti-p21 (1:500, ab109520; Abcam), rabbit anti-gamma H2AX (phospho S139) (1:1,000, ab2893; Abcam), rabbit anti-ERK1/2 (1:500, No 5013; Cell Signaling Technology Inc., Danvers, MA, USA), rabbit anti-phospho-ERK1/2 (Thr202/Tyr204) (1:2,000, No 4376; Cell Signaling Technology Inc.), rabbit anti-PKM2 (1:1,000, ab150377; Abcam), rabbit anti-β-actin (1:2,000, ab16039; Abcam), mouse anti-Tubulin (1:2,000, AT819; Beyotime Institute of Biotechnology), rabbit anti-active caspase3 (1:1,000, ab49822; Abcam), mouse anti-cleaved PARP1 (1:1,000, ab198490; Abcam), mouse anti-cytochrome C (1:2,000, ab13575; Abcam), rabbit anti-VDAC (1:1,000, ab15895; Abcam), mouse anti-Bcl-2 (1:1,000, ab201566; Abcam), rabbit anti-Bax (1:500, No 2774; Cell Signaling Technology Inc.), and mouse-anti-HA (1:500, H3663; Sigma-Aldrich Co.).

    Techniques: Western Blot, Expressing, Real-time Polymerase Chain Reaction