mouse anti human akt3 Search Results


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Antibodies used in the experiment.
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Figure 1. RNA transcript and protein expression of AKT isoforms in human skeletal muscle. Real-time PCR was performed on cDNA derived from human vastus lateralis using AKT isoform-specific primers/probes. Expression levels are normalized to expression of AKT1 which was set to 1.0. (means SEMs; n = 4; ***, P < 0.001 versus AKT1 and <t>AKT3).</t> (B) Western immunoblotting was performed on synthetic peptides of full- length human AKT1, AKT2, or AKT3 using the indicated antibodies. (C) Immunoprecipitations were performed using either rabbit or mouse pan AKT antibodies followed by western blotting with isoform-specific antibodies as indicated. Twenty-five micrograms of whole cell lysate (“WCL”) were also subjected to SDS-PAGE. Control immunoprecipitations were performed using the relevant species-specific IgG instead of antibody. Molecular mass in kDa is shown on the left of each blot. “HC;” heavy chain; LC, light chain.
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Figure 1. RNA transcript and protein expression of AKT isoforms in human skeletal muscle. Real-time PCR was performed on cDNA derived from human vastus lateralis using AKT isoform-specific primers/probes. Expression levels are normalized to expression of AKT1 which was set to 1.0. (means SEMs; n = 4; ***, P < 0.001 versus AKT1 and <t>AKT3).</t> (B) Western immunoblotting was performed on synthetic peptides of full- length human AKT1, AKT2, or AKT3 using the indicated antibodies. (C) Immunoprecipitations were performed using either rabbit or mouse pan AKT antibodies followed by western blotting with isoform-specific antibodies as indicated. Twenty-five micrograms of whole cell lysate (“WCL”) were also subjected to SDS-PAGE. Control immunoprecipitations were performed using the relevant species-specific IgG instead of antibody. Molecular mass in kDa is shown on the left of each blot. “HC;” heavy chain; LC, light chain.
Mouse Anti Human Akt3, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Figure 1. RNA transcript and protein expression of AKT isoforms in human skeletal muscle. Real-time PCR was performed on cDNA derived from human vastus lateralis using AKT isoform-specific primers/probes. Expression levels are normalized to expression of AKT1 which was set to 1.0. (means SEMs; n = 4; ***, P < 0.001 versus AKT1 and <t>AKT3).</t> (B) Western immunoblotting was performed on synthetic peptides of full- length human AKT1, AKT2, or AKT3 using the indicated antibodies. (C) Immunoprecipitations were performed using either rabbit or mouse pan AKT antibodies followed by western blotting with isoform-specific antibodies as indicated. Twenty-five micrograms of whole cell lysate (“WCL”) were also subjected to SDS-PAGE. Control immunoprecipitations were performed using the relevant species-specific IgG instead of antibody. Molecular mass in kDa is shown on the left of each blot. “HC;” heavy chain; LC, light chain.
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Figure 1. RNA transcript and protein expression of AKT isoforms in human skeletal muscle. Real-time PCR was performed on cDNA derived from human vastus lateralis using AKT isoform-specific primers/probes. Expression levels are normalized to expression of AKT1 which was set to 1.0. (means SEMs; n = 4; ***, P < 0.001 versus AKT1 and <t>AKT3).</t> (B) Western immunoblotting was performed on synthetic peptides of full- length human AKT1, AKT2, or AKT3 using the indicated antibodies. (C) Immunoprecipitations were performed using either rabbit or mouse pan AKT antibodies followed by western blotting with isoform-specific antibodies as indicated. Twenty-five micrograms of whole cell lysate (“WCL”) were also subjected to SDS-PAGE. Control immunoprecipitations were performed using the relevant species-specific IgG instead of antibody. Molecular mass in kDa is shown on the left of each blot. “HC;” heavy chain; LC, light chain.
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Figure 1. RNA transcript and protein expression of AKT isoforms in human skeletal muscle. Real-time PCR was performed on cDNA derived from human vastus lateralis using AKT isoform-specific primers/probes. Expression levels are normalized to expression of AKT1 which was set to 1.0. (means SEMs; n = 4; ***, P < 0.001 versus AKT1 and <t>AKT3).</t> (B) Western immunoblotting was performed on synthetic peptides of full- length human AKT1, AKT2, or AKT3 using the indicated antibodies. (C) Immunoprecipitations were performed using either rabbit or mouse pan AKT antibodies followed by western blotting with isoform-specific antibodies as indicated. Twenty-five micrograms of whole cell lysate (“WCL”) were also subjected to SDS-PAGE. Control immunoprecipitations were performed using the relevant species-specific IgG instead of antibody. Molecular mass in kDa is shown on the left of each blot. “HC;” heavy chain; LC, light chain.
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Cell Signaling Technology Inc total protein kinase b akt
Figure 1. RNA transcript and protein expression of AKT isoforms in human skeletal muscle. Real-time PCR was performed on cDNA derived from human vastus lateralis using AKT isoform-specific primers/probes. Expression levels are normalized to expression of AKT1 which was set to 1.0. (means SEMs; n = 4; ***, P < 0.001 versus AKT1 and <t>AKT3).</t> (B) Western immunoblotting was performed on synthetic peptides of full- length human AKT1, AKT2, or AKT3 using the indicated antibodies. (C) Immunoprecipitations were performed using either rabbit or mouse pan AKT antibodies followed by western blotting with isoform-specific antibodies as indicated. Twenty-five micrograms of whole cell lysate (“WCL”) were also subjected to SDS-PAGE. Control immunoprecipitations were performed using the relevant species-specific IgG instead of antibody. Molecular mass in kDa is shown on the left of each blot. “HC;” heavy chain; LC, light chain.
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Effects of wood creosote on diabetic obese mice treated with metformin. Wood creosote does not affect efficacy of metformin. Weight change (A) and blood glucose levels (fed condition) (B) were examined during the experiment in . Data are shown as means±SEM. No significant differences between the metformin group and the metformin with wood creosote (M+C) group were observed. Mice were fasted for 3 hours after the final administration of drugs. (C) One g/kg glucose was administrated via oral gavage. One to 2 µL blood was collected via tail vein at indicated time points, and blood glucose was measured by using GlucoSensor. (D) At day 4 of , mice were fasted for 2 hours and then injected intraperitoneally with 36 µg/kg insulin. Blood glucose levels are shown as % initial. At day 5 in , blood was collected and measured serum bile acid levels (E) and alanine aminotransferase (F) were measured. (G) Western blots were carried out using liver protein (50 µg) to detect levels of phospho-AMPK and <t>phoshopho-AKT.</t> AKT, Protein Kinase B; AMPK, AMP-activated kinase.
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Effects of wood creosote on diabetic obese mice treated with metformin. Wood creosote does not affect efficacy of metformin. Weight change (A) and blood glucose levels (fed condition) (B) were examined during the experiment in . Data are shown as means±SEM. No significant differences between the metformin group and the metformin with wood creosote (M+C) group were observed. Mice were fasted for 3 hours after the final administration of drugs. (C) One g/kg glucose was administrated via oral gavage. One to 2 µL blood was collected via tail vein at indicated time points, and blood glucose was measured by using GlucoSensor. (D) At day 4 of , mice were fasted for 2 hours and then injected intraperitoneally with 36 µg/kg insulin. Blood glucose levels are shown as % initial. At day 5 in , blood was collected and measured serum bile acid levels (E) and alanine aminotransferase (F) were measured. (G) Western blots were carried out using liver protein (50 µg) to detect levels of phospho-AMPK and <t>phoshopho-AKT.</t> AKT, Protein Kinase B; AMPK, AMP-activated kinase.
P Akt, supplied by Proteintech, 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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Effects of wood creosote on diabetic obese mice treated with metformin. Wood creosote does not affect efficacy of metformin. Weight change (A) and blood glucose levels (fed condition) (B) were examined during the experiment in . Data are shown as means±SEM. No significant differences between the metformin group and the metformin with wood creosote (M+C) group were observed. Mice were fasted for 3 hours after the final administration of drugs. (C) One g/kg glucose was administrated via oral gavage. One to 2 µL blood was collected via tail vein at indicated time points, and blood glucose was measured by using GlucoSensor. (D) At day 4 of , mice were fasted for 2 hours and then injected intraperitoneally with 36 µg/kg insulin. Blood glucose levels are shown as % initial. At day 5 in , blood was collected and measured serum bile acid levels (E) and alanine aminotransferase (F) were measured. (G) Western blots were carried out using liver protein (50 µg) to detect levels of phospho-AMPK and <t>phoshopho-AKT.</t> AKT, Protein Kinase B; AMPK, AMP-activated kinase.
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Effects of wood creosote on diabetic obese mice treated with metformin. Wood creosote does not affect efficacy of metformin. Weight change (A) and blood glucose levels (fed condition) (B) were examined during the experiment in . Data are shown as means±SEM. No significant differences between the metformin group and the metformin with wood creosote (M+C) group were observed. Mice were fasted for 3 hours after the final administration of drugs. (C) One g/kg glucose was administrated via oral gavage. One to 2 µL blood was collected via tail vein at indicated time points, and blood glucose was measured by using GlucoSensor. (D) At day 4 of , mice were fasted for 2 hours and then injected intraperitoneally with 36 µg/kg insulin. Blood glucose levels are shown as % initial. At day 5 in , blood was collected and measured serum bile acid levels (E) and alanine aminotransferase (F) were measured. (G) Western blots were carried out using liver protein (50 µg) to detect levels of phospho-AMPK and <t>phoshopho-AKT.</t> AKT, Protein Kinase B; AMPK, AMP-activated kinase.
Total 4691p Akt, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Effects of wood creosote on diabetic obese mice treated with metformin. Wood creosote does not affect efficacy of metformin. Weight change (A) and blood glucose levels (fed condition) (B) were examined during the experiment in . Data are shown as means±SEM. No significant differences between the metformin group and the metformin with wood creosote (M+C) group were observed. Mice were fasted for 3 hours after the final administration of drugs. (C) One g/kg glucose was administrated via oral gavage. One to 2 µL blood was collected via tail vein at indicated time points, and blood glucose was measured by using GlucoSensor. (D) At day 4 of , mice were fasted for 2 hours and then injected intraperitoneally with 36 µg/kg insulin. Blood glucose levels are shown as % initial. At day 5 in , blood was collected and measured serum bile acid levels (E) and alanine aminotransferase (F) were measured. (G) Western blots were carried out using liver protein (50 µg) to detect levels of phospho-AMPK and <t>phoshopho-AKT.</t> AKT, Protein Kinase B; AMPK, AMP-activated kinase.
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Image Search Results


Antibodies used in the experiment.

Journal: BioMed Research International

Article Title: Shenmai Injection Supresses Glycolysis and Enhances Cisplatin Cytotoxicity in Cisplatin-Resistant A549/DDP Cells via the AKT-mTOR-c-Myc Signaling Pathway

doi: 10.1155/2020/9243681

Figure Lengend Snippet: Antibodies used in the experiment.

Article Snippet: p-Akt (Ser473) , 33281 M , Bioss , Mouse , 1 : 500.

Techniques:

Figure 1. RNA transcript and protein expression of AKT isoforms in human skeletal muscle. Real-time PCR was performed on cDNA derived from human vastus lateralis using AKT isoform-specific primers/probes. Expression levels are normalized to expression of AKT1 which was set to 1.0. (means SEMs; n = 4; ***, P < 0.001 versus AKT1 and AKT3). (B) Western immunoblotting was performed on synthetic peptides of full- length human AKT1, AKT2, or AKT3 using the indicated antibodies. (C) Immunoprecipitations were performed using either rabbit or mouse pan AKT antibodies followed by western blotting with isoform-specific antibodies as indicated. Twenty-five micrograms of whole cell lysate (“WCL”) were also subjected to SDS-PAGE. Control immunoprecipitations were performed using the relevant species-specific IgG instead of antibody. Molecular mass in kDa is shown on the left of each blot. “HC;” heavy chain; LC, light chain.

Journal: Physiological reports

Article Title: AKT2 is the predominant AKT isoform expressed in human skeletal muscle.

doi: 10.14814/phy2.13652

Figure Lengend Snippet: Figure 1. RNA transcript and protein expression of AKT isoforms in human skeletal muscle. Real-time PCR was performed on cDNA derived from human vastus lateralis using AKT isoform-specific primers/probes. Expression levels are normalized to expression of AKT1 which was set to 1.0. (means SEMs; n = 4; ***, P < 0.001 versus AKT1 and AKT3). (B) Western immunoblotting was performed on synthetic peptides of full- length human AKT1, AKT2, or AKT3 using the indicated antibodies. (C) Immunoprecipitations were performed using either rabbit or mouse pan AKT antibodies followed by western blotting with isoform-specific antibodies as indicated. Twenty-five micrograms of whole cell lysate (“WCL”) were also subjected to SDS-PAGE. Control immunoprecipitations were performed using the relevant species-specific IgG instead of antibody. Molecular mass in kDa is shown on the left of each blot. “HC;” heavy chain; LC, light chain.

Article Snippet: Antibodies for AKT1 (C73H10; #2938), AKT2 (D6G4; #3063), AKT3 (E2B6R; #14293), AKT (Pan) (C67E7) (rabbit monoclonal; #4691), AKT (Pan) (40D4) (mouse monoclonal; #2920), and Protein A HRP (#12291S), were purchased from Cell Signaling Technologies (Danvers, MA).

Techniques: Expressing, Real-time Polymerase Chain Reaction, Derivative Assay, Western Blot, SDS Page, Control

Effects of wood creosote on diabetic obese mice treated with metformin. Wood creosote does not affect efficacy of metformin. Weight change (A) and blood glucose levels (fed condition) (B) were examined during the experiment in . Data are shown as means±SEM. No significant differences between the metformin group and the metformin with wood creosote (M+C) group were observed. Mice were fasted for 3 hours after the final administration of drugs. (C) One g/kg glucose was administrated via oral gavage. One to 2 µL blood was collected via tail vein at indicated time points, and blood glucose was measured by using GlucoSensor. (D) At day 4 of , mice were fasted for 2 hours and then injected intraperitoneally with 36 µg/kg insulin. Blood glucose levels are shown as % initial. At day 5 in , blood was collected and measured serum bile acid levels (E) and alanine aminotransferase (F) were measured. (G) Western blots were carried out using liver protein (50 µg) to detect levels of phospho-AMPK and phoshopho-AKT. AKT, Protein Kinase B; AMPK, AMP-activated kinase.

Journal: BMJ Open Diabetes Research & Care

Article Title: Mouse model of metformin-induced diarrhea

doi: 10.1136/bmjdrc-2019-000898

Figure Lengend Snippet: Effects of wood creosote on diabetic obese mice treated with metformin. Wood creosote does not affect efficacy of metformin. Weight change (A) and blood glucose levels (fed condition) (B) were examined during the experiment in . Data are shown as means±SEM. No significant differences between the metformin group and the metformin with wood creosote (M+C) group were observed. Mice were fasted for 3 hours after the final administration of drugs. (C) One g/kg glucose was administrated via oral gavage. One to 2 µL blood was collected via tail vein at indicated time points, and blood glucose was measured by using GlucoSensor. (D) At day 4 of , mice were fasted for 2 hours and then injected intraperitoneally with 36 µg/kg insulin. Blood glucose levels are shown as % initial. At day 5 in , blood was collected and measured serum bile acid levels (E) and alanine aminotransferase (F) were measured. (G) Western blots were carried out using liver protein (50 µg) to detect levels of phospho-AMPK and phoshopho-AKT. AKT, Protein Kinase B; AMPK, AMP-activated kinase.

Article Snippet: Antibodies are as follows: Anti-glyceraldehyde 3-phosphate dehydrogenase (GAPDH) (1E6D9, Proteintech, Rosemont, Illinois, USA), anti-AMPK (ABV10739, ABGENT, San Diego, California, USA), anti-phospho AMPK (pT172) (40H9, Cell Signaling Technology, Danvers, Massachusetts, USA), anti-total Protein Kinase B (AKT) (200–401 N98, Rockland, Limerick, Pennsylvania, USA), and anti-phosho AKT (pS473) (D9E, Cell Signaling Technology).

Techniques: Injection, Western Blot