polyclonal anti–p-38 Search Results



90
Merck KGaA anti p38 mapk (rabbit polyclonal
Participation of <t>MAPK</t> pathways in oxLDL-dependent effects: a cell shortening of cardiomyocytes exposed to oxLDL (20 µg/ml) and SP600125 (10 µM). b Cell shortening of cardiomyocytes exposed to oxLDL (20 µg/ml) and PD98059 (10 µM). c Cell shortening of cardiomyocytes exposed to oxLDL (20 µg/ml) and SB202190 (10 µM). In a – c a represents p < 0.095 vs. control. d Representative immunoblot of samples from cardiomyocytes exposed to oxLDL (20 µg/ml) and quantified for <t>p38</t> <t>MAPK</t> expression and phosphorylation of <t>p38</t> <t>MAPK.</t> e Quantification of the blot shown in d . f Original western blot showing the oxidative modification of tropomyosin by oxLDL (20 mg/ml) in the left and the control blot under reducing conditions (right). g Quantification of oxidative modification of tropomyosin by oxLDL ( n = 3). Exact p values are given
Anti P38 Mapk (Rabbit Polyclonal, supplied by Merck KGaA, 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/polyclonal+anti%E2%80%93p-38/anti+p38+mapk++rabbit+polyclonal/pmc05599470-76-8-13
Average 90 stars, based on 1 article reviews
anti p38 mapk (rabbit polyclonal - by Bioz Stars, 2026-09
90/100 stars
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Rabbit anti p38 MAPK Phospho Thr180 Tyr182 Polyclonal Antibody
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The mitogen-activated protein kinases (MAPK), also known as extracellular signal-related kinase (ERKs), are praline-directed protein kinases that mediate the effects of numerous extracellular stimuli on a wide array of biological processes, such as cellular prolifeRation,
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Participation of MAPK pathways in oxLDL-dependent effects: a cell shortening of cardiomyocytes exposed to oxLDL (20 µg/ml) and SP600125 (10 µM). b Cell shortening of cardiomyocytes exposed to oxLDL (20 µg/ml) and PD98059 (10 µM). c Cell shortening of cardiomyocytes exposed to oxLDL (20 µg/ml) and SB202190 (10 µM). In a – c a represents p < 0.095 vs. control. d Representative immunoblot of samples from cardiomyocytes exposed to oxLDL (20 µg/ml) and quantified for p38 MAPK expression and phosphorylation of p38 MAPK. e Quantification of the blot shown in d . f Original western blot showing the oxidative modification of tropomyosin by oxLDL (20 mg/ml) in the left and the control blot under reducing conditions (right). g Quantification of oxidative modification of tropomyosin by oxLDL ( n = 3). Exact p values are given

Journal: Basic Research in Cardiology

Article Title: Oxidized low-density lipoprotein (oxLDL) affects load-free cell shortening of cardiomyocytes in a proprotein convertase subtilisin/kexin 9 (PCSK9)-dependent way

doi: 10.1007/s00395-017-0650-1

Figure Lengend Snippet: Participation of MAPK pathways in oxLDL-dependent effects: a cell shortening of cardiomyocytes exposed to oxLDL (20 µg/ml) and SP600125 (10 µM). b Cell shortening of cardiomyocytes exposed to oxLDL (20 µg/ml) and PD98059 (10 µM). c Cell shortening of cardiomyocytes exposed to oxLDL (20 µg/ml) and SB202190 (10 µM). In a – c a represents p < 0.095 vs. control. d Representative immunoblot of samples from cardiomyocytes exposed to oxLDL (20 µg/ml) and quantified for p38 MAPK expression and phosphorylation of p38 MAPK. e Quantification of the blot shown in d . f Original western blot showing the oxidative modification of tropomyosin by oxLDL (20 mg/ml) in the left and the control blot under reducing conditions (right). g Quantification of oxidative modification of tropomyosin by oxLDL ( n = 3). Exact p values are given

Article Snippet: Anti-PCSK9 (rabbit polyclonal, ab31762, Abcam, Cambridge, UK), anti p38 MAPK (rabbit polyclonal, #506123, Merck KGaA Darmstadt, Germany), and anti phosphorylated p38 MAPK (rabbit polyclonal, #M0800, Sigma, St. Louis, USA) antibodies were used to detect the expression of PCSK9 protein and phosphorylation of p38 MAPK.

Techniques: Western Blot, Expressing, Modification

Summary figure of our findings: oxidized LDL (oxLDL) activates the oxLDL receptor. Expression of the receptor by cardiomyocytes was shown in this study and silencing of the receptor by siRNA attenuated all subsequent steps. oxLDL induces oxidative stress as indicated by oxidative modifications of tropomyosin (Trp-ox). Oxidative stress activates p38 MAP kinase as indicated by western blot. Inhibition of p38 MAP kinase activation by SB20190 attenuates this effect. Subsequently, oxLDL causes increased expression of PCSK9 as indicated by western blots and inhibition of transcription by actinomycin D (ActD) or translation by cycloheximide (chx) block all subsequent steps. Silencing of PCSK9 upregulation attenuates future steps

Journal: Basic Research in Cardiology

Article Title: Oxidized low-density lipoprotein (oxLDL) affects load-free cell shortening of cardiomyocytes in a proprotein convertase subtilisin/kexin 9 (PCSK9)-dependent way

doi: 10.1007/s00395-017-0650-1

Figure Lengend Snippet: Summary figure of our findings: oxidized LDL (oxLDL) activates the oxLDL receptor. Expression of the receptor by cardiomyocytes was shown in this study and silencing of the receptor by siRNA attenuated all subsequent steps. oxLDL induces oxidative stress as indicated by oxidative modifications of tropomyosin (Trp-ox). Oxidative stress activates p38 MAP kinase as indicated by western blot. Inhibition of p38 MAP kinase activation by SB20190 attenuates this effect. Subsequently, oxLDL causes increased expression of PCSK9 as indicated by western blots and inhibition of transcription by actinomycin D (ActD) or translation by cycloheximide (chx) block all subsequent steps. Silencing of PCSK9 upregulation attenuates future steps

Article Snippet: Anti-PCSK9 (rabbit polyclonal, ab31762, Abcam, Cambridge, UK), anti p38 MAPK (rabbit polyclonal, #506123, Merck KGaA Darmstadt, Germany), and anti phosphorylated p38 MAPK (rabbit polyclonal, #M0800, Sigma, St. Louis, USA) antibodies were used to detect the expression of PCSK9 protein and phosphorylation of p38 MAPK.

Techniques: Expressing, Western Blot, Inhibition, Activation Assay, Blocking Assay