Santa Cruz Biotechnology anti pyk2

FIGURE 6. Inhibition of the LPS-induced activation of integrin signaling in lung tissue by PP1: phosphory- lations of integrin 3 (A), FAK (B), and <t>Pyk2</t> (C) at 4 and 24 h post-LPS. Where indicated, mice were i.p. ad- ministered PP1 once at 1 h before LPS, and sacriﬁced at 4 h post-LPS. Mice i.p. administered PP1 at 2, 8, and 14 h post-LPS, were sacriﬁced at 24 h post-LPS. West- ern blots with anti-speciﬁc (phospho) Ab were em- ployed in lung tissue homogenates. Relative values of phosphorylated integrin 3, FAK, or Pyk2 vs nonphos- phorylated integrin 3, FAK, or Pyk2, respectively, are indicated below the gel. Values represent means SEM of results from 5 mice per group. , Signiﬁcantly different vs saline, p 0.05, and , signiﬁcantly dif- ferent vs the LPS only treated animals, p 0.05.

Anti Pyk2, supplied by Santa Cruz Biotechnology, 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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Average 93 stars, based on 1 article reviews

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pt180y182 p38 (Cell Signaling Technology Inc)

Cell Signaling Technology Inc pt180y182 p38

Cells were seeded at confluence and incubated for 72 hours. Then, growth media was replaced by low serum media and cells were infected with adenovirus to express either LacZ (control) or DN-Csk. A , 16 h later, cells were treated with low dose TNF-α for 15 or 30 minutes and assayed for <t>p38</t> phosphorylation by Western blot. B , Cells were treated with low or high dose TNF-α and assayed for p38 and SFK activity 30 minutes post-treatment (as measured by pY-Src, pY-FAK and pS-HSP27) by Western blot. C , Cells were pretreated for 30 minutes with either DMSO (vehicle), SB203580 (p38 inhibitor) or Y-27632 (ROCK inhibitor), treated as in A, and assayed for pS82-HSP27 by Western blot. D , Cells were pretreated with either DMSO or SB203580 30 minutes prior to TNF-α addition and then TEER was measured on ECIS electrodes for an additional 20 hours. Data presented as mean±SEM. Notice that p38 inhibition reversed the loss of barrier function in LD-TNF/DN-Csk cells. Results are representative of at least three independent experiments (n = 2–4 per experiment). Bar graph and statistical analysis of TEER for the 20 h time point corresponding to C is shown in .

Pt180y182 P38, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/rabbit+polyclonal+anti+integrin+%CE%B23+(py773/Phospho-p38+MAPK+(Thr180%2FTyr182)+XP+Rabbit+mAb/pmc05014308-55-19-25
Average 98 stars, based on 1 article reviews

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FIGURE 6. Inhibition of the LPS-induced activation of integrin signaling in lung tissue by PP1: phosphory- lations of integrin 3 (A), FAK (B), and Pyk2 (C) at 4 and 24 h post-LPS. Where indicated, mice were i.p. ad- ministered PP1 once at 1 h before LPS, and sacriﬁced at 4 h post-LPS. Mice i.p. administered PP1 at 2, 8, and 14 h post-LPS, were sacriﬁced at 24 h post-LPS. West- ern blots with anti-speciﬁc (phospho) Ab were em- ployed in lung tissue homogenates. Relative values of phosphorylated integrin 3, FAK, or Pyk2 vs nonphos- phorylated integrin 3, FAK, or Pyk2, respectively, are indicated below the gel. Values represent means SEM of results from 5 mice per group. , Signiﬁcantly different vs saline, p 0.05, and , signiﬁcantly dif- ferent vs the LPS only treated animals, p 0.05.

Journal: Journal of immunology (Baltimore, Md. : 1950)

Article Title: Src tyrosine kinases mediate activations of NF-kappaB and integrin signal during lipopolysaccharide-induced acute lung injury.

doi: 10.4049/jimmunol.179.10.7001

Figure Lengend Snippet: FIGURE 6. Inhibition of the LPS-induced activation of integrin signaling in lung tissue by PP1: phosphory- lations of integrin 3 (A), FAK (B), and Pyk2 (C) at 4 and 24 h post-LPS. Where indicated, mice were i.p. ad- ministered PP1 once at 1 h before LPS, and sacriﬁced at 4 h post-LPS. Mice i.p. administered PP1 at 2, 8, and 14 h post-LPS, were sacriﬁced at 24 h post-LPS. West- ern blots with anti-speciﬁc (phospho) Ab were em- ployed in lung tissue homogenates. Relative values of phosphorylated integrin 3, FAK, or Pyk2 vs nonphos- phorylated integrin 3, FAK, or Pyk2, respectively, are indicated below the gel. Values represent means SEM of results from 5 mice per group. , Signiﬁcantly different vs saline, p 0.05, and , signiﬁcantly dif- ferent vs the LPS only treated animals, p 0.05.

Article Snippet: The Abs used in this study were: anti-I Brabbit polyclonal, antiphospho-I B- (Serine 32) (New England Biolabs), rabbit anti-phospho-c-Src (pY418), anti-c-Src, anti-phospho-integrin 3 (pY773) rabbit polyclonal (BioSource), anti-integrin v (RMV-7) mAb (24), anti-integrin 3 (HM ) mAb (BioLegend) (25), anti-phospho-FAK (pY397), anti-FAK, anti-phospho-Pyk2 (pY402), anti- Pyk2 (Santa Cruz Biotechnology).

Techniques: Inhibition, Activation Assay, Saline

FIGURE 8. Inhibition of LPS-in- duced NF-B activation and inte- grin (v3) signaling in lung tissue by anti-integrin v, 3, or RGDS at 4 h post-LPS. Where indicated, mice were i.p. administered anti-v, -3, IgG, RGDS, or RGES (5 mg/kg body weight) once at 1 h before LPS, and sacriﬁced at 4 h post-LPS. Nuclear extracts were then prepared from lung tissues. Densities of NF-B bands on EMSA are expressed as per- centages of saline controls (A and B). Western blots with anti-speciﬁc (phospho) Ab were employed in lung tissue homogenates. Relative values of phosphorylated c-Src, FAK, or Pyk2 vs nonphosphorylated c-Src, FAK or Pyk2, respectively, are indi- cated below the gel (C–E). Results are meansSEM of results from 5 mice per group. , Signiﬁcantly dif- ferent vs saline, p 0.05, and , sig- niﬁcantly different vs the LPS only treated animals, p 0.05.

Journal: Journal of immunology (Baltimore, Md. : 1950)

Article Title: Src tyrosine kinases mediate activations of NF-kappaB and integrin signal during lipopolysaccharide-induced acute lung injury.

doi: 10.4049/jimmunol.179.10.7001

Figure Lengend Snippet: FIGURE 8. Inhibition of LPS-in- duced NF-B activation and inte- grin (v3) signaling in lung tissue by anti-integrin v, 3, or RGDS at 4 h post-LPS. Where indicated, mice were i.p. administered anti-v, -3, IgG, RGDS, or RGES (5 mg/kg body weight) once at 1 h before LPS, and sacriﬁced at 4 h post-LPS. Nuclear extracts were then prepared from lung tissues. Densities of NF-B bands on EMSA are expressed as per- centages of saline controls (A and B). Western blots with anti-speciﬁc (phospho) Ab were employed in lung tissue homogenates. Relative values of phosphorylated c-Src, FAK, or Pyk2 vs nonphosphorylated c-Src, FAK or Pyk2, respectively, are indi- cated below the gel (C–E). Results are meansSEM of results from 5 mice per group. , Signiﬁcantly dif- ferent vs saline, p 0.05, and , sig- niﬁcantly different vs the LPS only treated animals, p 0.05.

Techniques: Inhibition, Activation Assay, Saline, Western Blot

Journal: PLoS ONE

Article Title: Src Family Kinases Modulate the Loss of Endothelial Barrier Function in Response to TNF-α: Crosstalk with p38 Signaling

doi: 10.1371/journal.pone.0161975

Figure Lengend Snippet: Cells were seeded at confluence and incubated for 72 hours. Then, growth media was replaced by low serum media and cells were infected with adenovirus to express either LacZ (control) or DN-Csk. A , 16 h later, cells were treated with low dose TNF-α for 15 or 30 minutes and assayed for p38 phosphorylation by Western blot. B , Cells were treated with low or high dose TNF-α and assayed for p38 and SFK activity 30 minutes post-treatment (as measured by pY-Src, pY-FAK and pS-HSP27) by Western blot. C , Cells were pretreated for 30 minutes with either DMSO (vehicle), SB203580 (p38 inhibitor) or Y-27632 (ROCK inhibitor), treated as in A, and assayed for pS82-HSP27 by Western blot. D , Cells were pretreated with either DMSO or SB203580 30 minutes prior to TNF-α addition and then TEER was measured on ECIS electrodes for an additional 20 hours. Data presented as mean±SEM. Notice that p38 inhibition reversed the loss of barrier function in LD-TNF/DN-Csk cells. Results are representative of at least three independent experiments (n = 2–4 per experiment). Bar graph and statistical analysis of TEER for the 20 h time point corresponding to C is shown in .

Article Snippet: The following antibodies were used for Western blot and/or immunofluorescence: pY419 Src (#2101), pS82 HSP27 (#2401), HSP27 (#2402) and pT180Y182 p38 (#4511) were obtained from Cell Signaling; pY118 paxillin (#ab75740) from Abcam; Src (GD11) and anti-pY (4G10) from Millipore; Csk (# sc-286), FAK (#sc-557), p38 (#sc-535) and VE-cadherin (#sc-6458) from Santa Cruz Biotechnology; paxillin (#612405) from BD Biosciences; claudin 5 (#34–1600), pY773 ITGB3 (#44-876G), pY397 FAK (#44-624G) and pY861 FAK (#44-626G) from Life Technologies; pS15 HSP27 (#2231–1) from Epitomics.

Techniques: Incubation, Infection, Control, Phospho-proteomics, Western Blot, Activity Assay, Inhibition

Pre-confluent monolayers of HDMEC were infected with lentivirus containing active FLAG-tagged MKK6 construct (iMKK6E) under the control of an inducible promoter. These cells were reseeded and allowed to become confluent for 3 days. Then, confluent iMKK6E-HDMEC monolayers were infected with adenovirus to express either LacZ or DN-Csk. After an additional incubation of 24 h, cells were treated with or without doxycycline to induce the expression of MKK6E in low serum media. A , Cells were then lysed 18 h later and assayed for SFK and p38 signaling by Western blot, demonstrating independent pathway activation. B , TEER was measured on ECIS electrodes in cells treated as in A. C , Cells expressing either LacZ or DN-Csk were treated with different concentrations of doxycycline and TEER was measured on ECIS electrodes for 24 h. D , FITC-Albumin permeability assay on Transwell chambers 18 h after doxycycline addition. Data presented as mean±SEM. Asterisk, p<0.05 (Two-way ANOVA and Tukey’s multiple comparison post-hoc test). Note the synergistic action to promote an increase in endothelial permeability. Results are representative of at least three independent experiments. E , Cells were fixed 18 h after doxycycline addition and stained for phosphorylated (pT180Y182) p38 and VE-cadherin. Nuclei were counterstained with DAPI. Note the nuclear localization of phospho-p38 in cells treated with doxycycline. Results are representative of at least three independent experiments performed in duplicate. F , Nuclear (pT180Y182) p38 fluorescence intensity was quantified from three fields from each treatment. Bar graphs and statistical analyses of TEER for the 20 h time point corresponding to B and C are shown in .

Journal: PLoS ONE

Article Title: Src Family Kinases Modulate the Loss of Endothelial Barrier Function in Response to TNF-α: Crosstalk with p38 Signaling

doi: 10.1371/journal.pone.0161975

Figure Lengend Snippet: Pre-confluent monolayers of HDMEC were infected with lentivirus containing active FLAG-tagged MKK6 construct (iMKK6E) under the control of an inducible promoter. These cells were reseeded and allowed to become confluent for 3 days. Then, confluent iMKK6E-HDMEC monolayers were infected with adenovirus to express either LacZ or DN-Csk. After an additional incubation of 24 h, cells were treated with or without doxycycline to induce the expression of MKK6E in low serum media. A , Cells were then lysed 18 h later and assayed for SFK and p38 signaling by Western blot, demonstrating independent pathway activation. B , TEER was measured on ECIS electrodes in cells treated as in A. C , Cells expressing either LacZ or DN-Csk were treated with different concentrations of doxycycline and TEER was measured on ECIS electrodes for 24 h. D , FITC-Albumin permeability assay on Transwell chambers 18 h after doxycycline addition. Data presented as mean±SEM. Asterisk, p<0.05 (Two-way ANOVA and Tukey’s multiple comparison post-hoc test). Note the synergistic action to promote an increase in endothelial permeability. Results are representative of at least three independent experiments. E , Cells were fixed 18 h after doxycycline addition and stained for phosphorylated (pT180Y182) p38 and VE-cadherin. Nuclei were counterstained with DAPI. Note the nuclear localization of phospho-p38 in cells treated with doxycycline. Results are representative of at least three independent experiments performed in duplicate. F , Nuclear (pT180Y182) p38 fluorescence intensity was quantified from three fields from each treatment. Bar graphs and statistical analyses of TEER for the 20 h time point corresponding to B and C are shown in .

Techniques: Infection, Construct, Control, Incubation, Expressing, Western Blot, Activation Assay, Permeability, Comparison, Staining, Fluorescence

rabbit polyclonal anti integrin β3 (py773 Search Results

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