sem photographs and elemental mapping results at 5 kv Search Results


arcview gis software  (Esri inc)
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goat anti sapk4  (Santa Cruz Biotechnology)
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Santa Cruz Biotechnology goat anti sapk4
FIG. 4. Regulation of p38 MAPK isoforms in keratinocytes. A, to measure the enzymatic activity of individual p38 isoforms in response to caMEK6, keratinocytes were co-infected with empty vector (Control (EV)), or caMEK6 and FLAG-p38a, b, g, or d. After 48 h, the p38 isoforms were immunoprecipitated using mouse monoclonal anti-FLAG antibody M2 (Sigma number F3165, diluted to 5 mg/ml) and 30 ml of protein G/A-agarose (Oncogene IP05). p38 activity was monitored based on ability of the precipitated kinase to phosphorylate ATF-2. Phospho- rylated ATF-2 was detected by immunoblot as in Fig. 3B. Immunoblot showing that p38a, b, g, and d are expressed in comparable levels when delivered by adenovirus vector. Cells were lysed 48 h after infection, and each p38 isoform was detected by immunoblot using peroxidase- conjugated mouse monoclonal anti-FLAG (Sigma A8592, diluted 1:10,000). C, endogenous p38a activity was measured by mock infecting keratinocytes, infecting with empty (EV) adenovirus, or infecting with adenovirus encoding caMEK6. After 48 h, the cells were harvested and endogenous p38a, b, and d were immunoprecipitated, respectively, us- ing rabbit anti-p38a (Sigma number M0800), mouse anti-p38-b2 (Am- ersham Pharmacia Biotech number 33–8700), and goat <t>anti-p38d</t> (San- ta Cruz sc-7585), each at 5 mg/precipitation. p38 kinase activity was monitored based on the ability to phosphorylate ATF-2. Phosphorylated ATF-2 was detected by immunoblot as in Fig. 3. This result was con- firmed in three separate experiments.
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mapk erk kinase inhibitor u0126  (Cell Signaling Technology Inc)
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Cell Signaling Technology Inc mapk erk kinase inhibitor u0126
FIG. 4. Regulation of p38 MAPK isoforms in keratinocytes. A, to measure the enzymatic activity of individual p38 isoforms in response to caMEK6, keratinocytes were co-infected with empty vector (Control (EV)), or caMEK6 and FLAG-p38a, b, g, or d. After 48 h, the p38 isoforms were immunoprecipitated using mouse monoclonal anti-FLAG antibody M2 (Sigma number F3165, diluted to 5 mg/ml) and 30 ml of protein G/A-agarose (Oncogene IP05). p38 activity was monitored based on ability of the precipitated kinase to phosphorylate ATF-2. Phospho- rylated ATF-2 was detected by immunoblot as in Fig. 3B. Immunoblot showing that p38a, b, g, and d are expressed in comparable levels when delivered by adenovirus vector. Cells were lysed 48 h after infection, and each p38 isoform was detected by immunoblot using peroxidase- conjugated mouse monoclonal anti-FLAG (Sigma A8592, diluted 1:10,000). C, endogenous p38a activity was measured by mock infecting keratinocytes, infecting with empty (EV) adenovirus, or infecting with adenovirus encoding caMEK6. After 48 h, the cells were harvested and endogenous p38a, b, and d were immunoprecipitated, respectively, us- ing rabbit anti-p38a (Sigma number M0800), mouse anti-p38-b2 (Am- ersham Pharmacia Biotech number 33–8700), and goat <t>anti-p38d</t> (San- ta Cruz sc-7585), each at 5 mg/precipitation. p38 kinase activity was monitored based on the ability to phosphorylate ATF-2. Phosphorylated ATF-2 was detected by immunoblot as in Fig. 3. This result was con- firmed in three separate experiments.
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FIG. 4. Regulation of p38 MAPK isoforms in keratinocytes. A, to measure the enzymatic activity of individual p38 isoforms in response to caMEK6, keratinocytes were co-infected with empty vector (Control (EV)), or caMEK6 and FLAG-p38a, b, g, or d. After 48 h, the p38 isoforms were immunoprecipitated using mouse monoclonal anti-FLAG antibody M2 (Sigma number F3165, diluted to 5 mg/ml) and 30 ml of protein G/A-agarose (Oncogene IP05). p38 activity was monitored based on ability of the precipitated kinase to phosphorylate ATF-2. Phospho- rylated ATF-2 was detected by immunoblot as in Fig. 3B. Immunoblot showing that p38a, b, g, and d are expressed in comparable levels when delivered by adenovirus vector. Cells were lysed 48 h after infection, and each p38 isoform was detected by immunoblot using peroxidase- conjugated mouse monoclonal anti-FLAG (Sigma A8592, diluted 1:10,000). C, endogenous p38a activity was measured by mock infecting keratinocytes, infecting with empty (EV) adenovirus, or infecting with adenovirus encoding caMEK6. After 48 h, the cells were harvested and endogenous p38a, b, and d were immunoprecipitated, respectively, us- ing rabbit anti-p38a (Sigma number M0800), mouse anti-p38-b2 (Am- ersham Pharmacia Biotech number 33–8700), and goat <t>anti-p38d</t> (San- ta Cruz sc-7585), each at 5 mg/precipitation. p38 kinase activity was monitored based on the ability to phosphorylate ATF-2. Phosphorylated ATF-2 was detected by immunoblot as in Fig. 3. This result was con- firmed in three separate experiments.
Waist Worn Actigraph Gt3x, supplied by ActiGraph llc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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energy dispersive x ray spectroscopy edx mapping scanning electron microscopy  (JEOL)
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JEOL energy dispersive x ray spectroscopy edx mapping scanning electron microscopy
FIG. 4. Regulation of p38 MAPK isoforms in keratinocytes. A, to measure the enzymatic activity of individual p38 isoforms in response to caMEK6, keratinocytes were co-infected with empty vector (Control (EV)), or caMEK6 and FLAG-p38a, b, g, or d. After 48 h, the p38 isoforms were immunoprecipitated using mouse monoclonal anti-FLAG antibody M2 (Sigma number F3165, diluted to 5 mg/ml) and 30 ml of protein G/A-agarose (Oncogene IP05). p38 activity was monitored based on ability of the precipitated kinase to phosphorylate ATF-2. Phospho- rylated ATF-2 was detected by immunoblot as in Fig. 3B. Immunoblot showing that p38a, b, g, and d are expressed in comparable levels when delivered by adenovirus vector. Cells were lysed 48 h after infection, and each p38 isoform was detected by immunoblot using peroxidase- conjugated mouse monoclonal anti-FLAG (Sigma A8592, diluted 1:10,000). C, endogenous p38a activity was measured by mock infecting keratinocytes, infecting with empty (EV) adenovirus, or infecting with adenovirus encoding caMEK6. After 48 h, the cells were harvested and endogenous p38a, b, and d were immunoprecipitated, respectively, us- ing rabbit anti-p38a (Sigma number M0800), mouse anti-p38-b2 (Am- ersham Pharmacia Biotech number 33–8700), and goat <t>anti-p38d</t> (San- ta Cruz sc-7585), each at 5 mg/precipitation. p38 kinase activity was monitored based on the ability to phosphorylate ATF-2. Phosphorylated ATF-2 was detected by immunoblot as in Fig. 3. This result was con- firmed in three separate experiments.
Energy Dispersive X Ray Spectroscopy Edx Mapping Scanning Electron Microscopy, supplied by JEOL, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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fractional area of habitat maps at 5-km resolution esri 54017  (Esri inc)
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Esri inc fractional area of habitat maps at 5-km resolution esri 54017
FIG. 4. Regulation of p38 MAPK isoforms in keratinocytes. A, to measure the enzymatic activity of individual p38 isoforms in response to caMEK6, keratinocytes were co-infected with empty vector (Control (EV)), or caMEK6 and FLAG-p38a, b, g, or d. After 48 h, the p38 isoforms were immunoprecipitated using mouse monoclonal anti-FLAG antibody M2 (Sigma number F3165, diluted to 5 mg/ml) and 30 ml of protein G/A-agarose (Oncogene IP05). p38 activity was monitored based on ability of the precipitated kinase to phosphorylate ATF-2. Phospho- rylated ATF-2 was detected by immunoblot as in Fig. 3B. Immunoblot showing that p38a, b, g, and d are expressed in comparable levels when delivered by adenovirus vector. Cells were lysed 48 h after infection, and each p38 isoform was detected by immunoblot using peroxidase- conjugated mouse monoclonal anti-FLAG (Sigma A8592, diluted 1:10,000). C, endogenous p38a activity was measured by mock infecting keratinocytes, infecting with empty (EV) adenovirus, or infecting with adenovirus encoding caMEK6. After 48 h, the cells were harvested and endogenous p38a, b, and d were immunoprecipitated, respectively, us- ing rabbit anti-p38a (Sigma number M0800), mouse anti-p38-b2 (Am- ersham Pharmacia Biotech number 33–8700), and goat <t>anti-p38d</t> (San- ta Cruz sc-7585), each at 5 mg/precipitation. p38 kinase activity was monitored based on the ability to phosphorylate ATF-2. Phosphorylated ATF-2 was detected by immunoblot as in Fig. 3. This result was con- firmed in three separate experiments.
Fractional Area Of Habitat Maps At 5 Km Resolution Esri 54017, supplied by Esri inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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xmax 150 sdd detector  (Oxford Instruments)
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FIG. 4. Regulation of p38 MAPK isoforms in keratinocytes. A, to measure the enzymatic activity of individual p38 isoforms in response to caMEK6, keratinocytes were co-infected with empty vector (Control (EV)), or caMEK6 and FLAG-p38a, b, g, or d. After 48 h, the p38 isoforms were immunoprecipitated using mouse monoclonal anti-FLAG antibody M2 (Sigma number F3165, diluted to 5 mg/ml) and 30 ml of protein G/A-agarose (Oncogene IP05). p38 activity was monitored based on ability of the precipitated kinase to phosphorylate ATF-2. Phospho- rylated ATF-2 was detected by immunoblot as in Fig. 3B. Immunoblot showing that p38a, b, g, and d are expressed in comparable levels when delivered by adenovirus vector. Cells were lysed 48 h after infection, and each p38 isoform was detected by immunoblot using peroxidase- conjugated mouse monoclonal anti-FLAG (Sigma A8592, diluted 1:10,000). C, endogenous p38a activity was measured by mock infecting keratinocytes, infecting with empty (EV) adenovirus, or infecting with adenovirus encoding caMEK6. After 48 h, the cells were harvested and endogenous p38a, b, and d were immunoprecipitated, respectively, us- ing rabbit anti-p38a (Sigma number M0800), mouse anti-p38-b2 (Am- ersham Pharmacia Biotech number 33–8700), and goat <t>anti-p38d</t> (San- ta Cruz sc-7585), each at 5 mg/precipitation. p38 kinase activity was monitored based on the ability to phosphorylate ATF-2. Phosphorylated ATF-2 was detected by immunoblot as in Fig. 3. This result was con- firmed in three separate experiments.
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origin 2017  (OriginLab corp)
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FIG. 4. Regulation of p38 MAPK isoforms in keratinocytes. A, to measure the enzymatic activity of individual p38 isoforms in response to caMEK6, keratinocytes were co-infected with empty vector (Control (EV)), or caMEK6 and FLAG-p38a, b, g, or d. After 48 h, the p38 isoforms were immunoprecipitated using mouse monoclonal anti-FLAG antibody M2 (Sigma number F3165, diluted to 5 mg/ml) and 30 ml of protein G/A-agarose (Oncogene IP05). p38 activity was monitored based on ability of the precipitated kinase to phosphorylate ATF-2. Phospho- rylated ATF-2 was detected by immunoblot as in Fig. 3B. Immunoblot showing that p38a, b, g, and d are expressed in comparable levels when delivered by adenovirus vector. Cells were lysed 48 h after infection, and each p38 isoform was detected by immunoblot using peroxidase- conjugated mouse monoclonal anti-FLAG (Sigma A8592, diluted 1:10,000). C, endogenous p38a activity was measured by mock infecting keratinocytes, infecting with empty (EV) adenovirus, or infecting with adenovirus encoding caMEK6. After 48 h, the cells were harvested and endogenous p38a, b, and d were immunoprecipitated, respectively, us- ing rabbit anti-p38a (Sigma number M0800), mouse anti-p38-b2 (Am- ersham Pharmacia Biotech number 33–8700), and goat <t>anti-p38d</t> (San- ta Cruz sc-7585), each at 5 mg/precipitation. p38 kinase activity was monitored based on the ability to phosphorylate ATF-2. Phosphorylated ATF-2 was detected by immunoblot as in Fig. 3. This result was con- firmed in three separate experiments.
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map kinases  (Cell Signaling Technology Inc)
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Cell Signaling Technology Inc map kinases
FIG. 4. Regulation of p38 MAPK isoforms in keratinocytes. A, to measure the enzymatic activity of individual p38 isoforms in response to caMEK6, keratinocytes were co-infected with empty vector (Control (EV)), or caMEK6 and FLAG-p38a, b, g, or d. After 48 h, the p38 isoforms were immunoprecipitated using mouse monoclonal anti-FLAG antibody M2 (Sigma number F3165, diluted to 5 mg/ml) and 30 ml of protein G/A-agarose (Oncogene IP05). p38 activity was monitored based on ability of the precipitated kinase to phosphorylate ATF-2. Phospho- rylated ATF-2 was detected by immunoblot as in Fig. 3B. Immunoblot showing that p38a, b, g, and d are expressed in comparable levels when delivered by adenovirus vector. Cells were lysed 48 h after infection, and each p38 isoform was detected by immunoblot using peroxidase- conjugated mouse monoclonal anti-FLAG (Sigma A8592, diluted 1:10,000). C, endogenous p38a activity was measured by mock infecting keratinocytes, infecting with empty (EV) adenovirus, or infecting with adenovirus encoding caMEK6. After 48 h, the cells were harvested and endogenous p38a, b, and d were immunoprecipitated, respectively, us- ing rabbit anti-p38a (Sigma number M0800), mouse anti-p38-b2 (Am- ersham Pharmacia Biotech number 33–8700), and goat <t>anti-p38d</t> (San- ta Cruz sc-7585), each at 5 mg/precipitation. p38 kinase activity was monitored based on the ability to phosphorylate ATF-2. Phosphorylated ATF-2 was detected by immunoblot as in Fig. 3. This result was con- firmed in three separate experiments.
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5′-trfs  (First BASE Laboratories)
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FIG. 4. Regulation of p38 MAPK isoforms in keratinocytes. A, to measure the enzymatic activity of individual p38 isoforms in response to caMEK6, keratinocytes were co-infected with empty vector (Control (EV)), or caMEK6 and FLAG-p38a, b, g, or d. After 48 h, the p38 isoforms were immunoprecipitated using mouse monoclonal anti-FLAG antibody M2 (Sigma number F3165, diluted to 5 mg/ml) and 30 ml of protein G/A-agarose (Oncogene IP05). p38 activity was monitored based on ability of the precipitated kinase to phosphorylate ATF-2. Phospho- rylated ATF-2 was detected by immunoblot as in Fig. 3B. Immunoblot showing that p38a, b, g, and d are expressed in comparable levels when delivered by adenovirus vector. Cells were lysed 48 h after infection, and each p38 isoform was detected by immunoblot using peroxidase- conjugated mouse monoclonal anti-FLAG (Sigma A8592, diluted 1:10,000). C, endogenous p38a activity was measured by mock infecting keratinocytes, infecting with empty (EV) adenovirus, or infecting with adenovirus encoding caMEK6. After 48 h, the cells were harvested and endogenous p38a, b, and d were immunoprecipitated, respectively, us- ing rabbit anti-p38a (Sigma number M0800), mouse anti-p38-b2 (Am- ersham Pharmacia Biotech number 33–8700), and goat <t>anti-p38d</t> (San- ta Cruz sc-7585), each at 5 mg/precipitation. p38 kinase activity was monitored based on the ability to phosphorylate ATF-2. Phosphorylated ATF-2 was detected by immunoblot as in Fig. 3. This result was con- firmed in three separate experiments.
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recombinant human active map3k8 tpl2 cot protein cf  (R&D Systems)
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Image Search Results


FIG. 4. Regulation of p38 MAPK isoforms in keratinocytes. A, to measure the enzymatic activity of individual p38 isoforms in response to caMEK6, keratinocytes were co-infected with empty vector (Control (EV)), or caMEK6 and FLAG-p38a, b, g, or d. After 48 h, the p38 isoforms were immunoprecipitated using mouse monoclonal anti-FLAG antibody M2 (Sigma number F3165, diluted to 5 mg/ml) and 30 ml of protein G/A-agarose (Oncogene IP05). p38 activity was monitored based on ability of the precipitated kinase to phosphorylate ATF-2. Phospho- rylated ATF-2 was detected by immunoblot as in Fig. 3B. Immunoblot showing that p38a, b, g, and d are expressed in comparable levels when delivered by adenovirus vector. Cells were lysed 48 h after infection, and each p38 isoform was detected by immunoblot using peroxidase- conjugated mouse monoclonal anti-FLAG (Sigma A8592, diluted 1:10,000). C, endogenous p38a activity was measured by mock infecting keratinocytes, infecting with empty (EV) adenovirus, or infecting with adenovirus encoding caMEK6. After 48 h, the cells were harvested and endogenous p38a, b, and d were immunoprecipitated, respectively, us- ing rabbit anti-p38a (Sigma number M0800), mouse anti-p38-b2 (Am- ersham Pharmacia Biotech number 33–8700), and goat anti-p38d (San- ta Cruz sc-7585), each at 5 mg/precipitation. p38 kinase activity was monitored based on the ability to phosphorylate ATF-2. Phosphorylated ATF-2 was detected by immunoblot as in Fig. 3. This result was con- firmed in three separate experiments.

Journal: Journal of Biological Chemistry

Article Title: MEK6 Regulates Human Involucrin Gene Expression via a p38α- and p38δ-dependent Mechanism

doi: 10.1074/jbc.m100465200

Figure Lengend Snippet: FIG. 4. Regulation of p38 MAPK isoforms in keratinocytes. A, to measure the enzymatic activity of individual p38 isoforms in response to caMEK6, keratinocytes were co-infected with empty vector (Control (EV)), or caMEK6 and FLAG-p38a, b, g, or d. After 48 h, the p38 isoforms were immunoprecipitated using mouse monoclonal anti-FLAG antibody M2 (Sigma number F3165, diluted to 5 mg/ml) and 30 ml of protein G/A-agarose (Oncogene IP05). p38 activity was monitored based on ability of the precipitated kinase to phosphorylate ATF-2. Phospho- rylated ATF-2 was detected by immunoblot as in Fig. 3B. Immunoblot showing that p38a, b, g, and d are expressed in comparable levels when delivered by adenovirus vector. Cells were lysed 48 h after infection, and each p38 isoform was detected by immunoblot using peroxidase- conjugated mouse monoclonal anti-FLAG (Sigma A8592, diluted 1:10,000). C, endogenous p38a activity was measured by mock infecting keratinocytes, infecting with empty (EV) adenovirus, or infecting with adenovirus encoding caMEK6. After 48 h, the cells were harvested and endogenous p38a, b, and d were immunoprecipitated, respectively, us- ing rabbit anti-p38a (Sigma number M0800), mouse anti-p38-b2 (Am- ersham Pharmacia Biotech number 33–8700), and goat anti-p38d (San- ta Cruz sc-7585), each at 5 mg/precipitation. p38 kinase activity was monitored based on the ability to phosphorylate ATF-2. Phosphorylated ATF-2 was detected by immunoblot as in Fig. 3. This result was con- firmed in three separate experiments.

Article Snippet: Goat anti-MEK6 (sc-6073, diluted 1:1000), goat anti-SAPK4 (p38d, sc-7585 used at 5 mg/immunoprecipitation), and peroxidase-conjugated donkey anti-goat IgG (sc-2020, diluted 1:10,000) were purchased from Santa Cruz.

Techniques: Activity Assay, Infection, Plasmid Preparation, Control, Immunoprecipitation, Western Blot

FIG. 6. p38d inhibits hINV promoter activity. Keratinocytes were transfected with 2 mg/dish of the pINV-2473 hINV promoter construct. After 24 h, the cells were infected with either p38d-encoding or empty (control) adenovirus at 10 pfu/cell. After an additional 24 h, the cells were harvested and assayed for hINV promoter activity. The experi- ment was repeated three times with essentially identical results.

Journal: Journal of Biological Chemistry

Article Title: MEK6 Regulates Human Involucrin Gene Expression via a p38α- and p38δ-dependent Mechanism

doi: 10.1074/jbc.m100465200

Figure Lengend Snippet: FIG. 6. p38d inhibits hINV promoter activity. Keratinocytes were transfected with 2 mg/dish of the pINV-2473 hINV promoter construct. After 24 h, the cells were infected with either p38d-encoding or empty (control) adenovirus at 10 pfu/cell. After an additional 24 h, the cells were harvested and assayed for hINV promoter activity. The experi- ment was repeated three times with essentially identical results.

Article Snippet: Goat anti-MEK6 (sc-6073, diluted 1:1000), goat anti-SAPK4 (p38d, sc-7585 used at 5 mg/immunoprecipitation), and peroxidase-conjugated donkey anti-goat IgG (sc-2020, diluted 1:10,000) were purchased from Santa Cruz.

Techniques: Activity Assay, Transfection, Construct, Infection, Control

FIG. 7. p38a and d differentially reg- ulate endogenous hINV gene expres- sion. A, keratinocytes were infected with 12.5 pfu/cell of empty adenovirus (EV), p38a-encoding, or caMEK6-encoding ade- novirus. After 48 h, the cells were har- vested and hINV protein level was as- sayed by immunoblot as in Fig. 2. Involucrin sometimes runs as a doublet on gel electrophoresis. B, keratinocytes were infected adenoviruses encoding p38d and/or caMEK6 at 5 pfu/cell. Total viral load was maintained at 15 pfu/cell by ad- dition of empty adenovirus (EV). After 48 h, the cells were treated with 50 ng/ml TPA for 24 h. The cells were then har- vested and extracts were prepared for de- tection of hINV by immunoblot.

Journal: Journal of Biological Chemistry

Article Title: MEK6 Regulates Human Involucrin Gene Expression via a p38α- and p38δ-dependent Mechanism

doi: 10.1074/jbc.m100465200

Figure Lengend Snippet: FIG. 7. p38a and d differentially reg- ulate endogenous hINV gene expres- sion. A, keratinocytes were infected with 12.5 pfu/cell of empty adenovirus (EV), p38a-encoding, or caMEK6-encoding ade- novirus. After 48 h, the cells were har- vested and hINV protein level was as- sayed by immunoblot as in Fig. 2. Involucrin sometimes runs as a doublet on gel electrophoresis. B, keratinocytes were infected adenoviruses encoding p38d and/or caMEK6 at 5 pfu/cell. Total viral load was maintained at 15 pfu/cell by ad- dition of empty adenovirus (EV). After 48 h, the cells were treated with 50 ng/ml TPA for 24 h. The cells were then har- vested and extracts were prepared for de- tection of hINV by immunoblot.

Article Snippet: Goat anti-MEK6 (sc-6073, diluted 1:1000), goat anti-SAPK4 (p38d, sc-7585 used at 5 mg/immunoprecipitation), and peroxidase-conjugated donkey anti-goat IgG (sc-2020, diluted 1:10,000) were purchased from Santa Cruz.

Techniques: Infection, Western Blot, Nucleic Acid Electrophoresis