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Cell Signaling Technology Inc k atpase
Identification of galactose as a hypoglycemic compound using the hyperglycemic silkworm model. (A) Preparation protocol for the jiou extract. (B) Silkworms were fed a 10% (w/w) glucose diet for 60 min. 50 µl of Jiou extract (1 mg/ml) or human insulin (3.5 mg/ml) was injected into the hemolymph of the hyperglycemic silkworms. The silkworms were fasted for 6 h and the sugar level in the hemolymph was determined. n = 6–7 per group. Data are shown as means ± SD. (C, D) The jiou extract was treated with TFA, and analyzed by TLC. Sugars were localized with 10% sulfuric acid solution. (E) Silkworms were fed a 10% (w/w) glucose diet for 60 min. 50 µl of D-Galactose (Gal), D-glucose (Glu), D-talose (Tal), D-mannose (Man), (1 mg/ml) or human insulin (3.5 mg/ml) was injected into the hemolymph of hyperglycemic silkworms. Silkworms were fasted for 6 h and sugar level in the hemolymph was determined. n = 6 per group. (F) Structure of sugar is shown by Fischer projection in the panel. Numbers shown on the left indicate the carbon positions of the sugar. Red hydroxyl group indicates the positions that differ from D-galactose. Activity represents the hypoglycemic effect. Data are shown as means ± SD. NS; not significant. (G) Galactose (10 mg/ml, 0.5 ml i.p.) was injected to streptozotocin induced-diabetic mice, and blood glucose level was determined after 4 h of fasting. Blood glucose levels in streptozotocin-induced hyperglycemic mice were measured (blood glucose 250–400 mg/dl) and then the mice were treated with either PBS or galactose solution. Four hours after administration and the removal of diet, the blood glucose levels were measured again. The data represent the blood glucose value after treatment divided by the blood glucose value before treatment of individual animals. In all panels, the statistical significance of the difference was evaluated using Student's t test. (H) Blood glucose levels in streptozotocin-induced hyperglycemic mice were measured (blood glucose 250–400 mg/dl) and then the mice were treated with either PBS, galactose (200 mg/kg mouse, i.p.), or glucose (200 mg/kg mouse, i.p.) solution. Two hours after administration and removal of the diet, the mice were killed and the membrane fraction in mouse liver was isolated. <t>GLUT2</t> and Na, <t>K-ATPase</t> were detected by Western blot analysis with anti-GLUT2 antibody or anti-Na, K-ATPase antibody. Immunoblots of GLUT2 and Na, K-ATPase (Top) and calculations of relative GLUT2 (Bottom). n = 3–4 per group. Data at the bottom of the figure are shown as means ± SD. In all panels, the statistical significance of the difference was evaluated using Student's t test.
K Atpase, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 92/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1) Product Images from "An Invertebrate Hyperglycemic Model for the Identification of Anti-Diabetic Drugs"

Article Title: An Invertebrate Hyperglycemic Model for the Identification of Anti-Diabetic Drugs

Journal: PLoS ONE

doi: 10.1371/journal.pone.0018292

Identification of galactose as a hypoglycemic compound using the hyperglycemic silkworm model. (A) Preparation protocol for the jiou extract. (B) Silkworms were fed a 10% (w/w) glucose diet for 60 min. 50 µl of Jiou extract (1 mg/ml) or human insulin (3.5 mg/ml) was injected into the hemolymph of the hyperglycemic silkworms. The silkworms were fasted for 6 h and the sugar level in the hemolymph was determined. n = 6–7 per group. Data are shown as means ± SD. (C, D) The jiou extract was treated with TFA, and analyzed by TLC. Sugars were localized with 10% sulfuric acid solution. (E) Silkworms were fed a 10% (w/w) glucose diet for 60 min. 50 µl of D-Galactose (Gal), D-glucose (Glu), D-talose (Tal), D-mannose (Man), (1 mg/ml) or human insulin (3.5 mg/ml) was injected into the hemolymph of hyperglycemic silkworms. Silkworms were fasted for 6 h and sugar level in the hemolymph was determined. n = 6 per group. (F) Structure of sugar is shown by Fischer projection in the panel. Numbers shown on the left indicate the carbon positions of the sugar. Red hydroxyl group indicates the positions that differ from D-galactose. Activity represents the hypoglycemic effect. Data are shown as means ± SD. NS; not significant. (G) Galactose (10 mg/ml, 0.5 ml i.p.) was injected to streptozotocin induced-diabetic mice, and blood glucose level was determined after 4 h of fasting. Blood glucose levels in streptozotocin-induced hyperglycemic mice were measured (blood glucose 250–400 mg/dl) and then the mice were treated with either PBS or galactose solution. Four hours after administration and the removal of diet, the blood glucose levels were measured again. The data represent the blood glucose value after treatment divided by the blood glucose value before treatment of individual animals. In all panels, the statistical significance of the difference was evaluated using Student's t test. (H) Blood glucose levels in streptozotocin-induced hyperglycemic mice were measured (blood glucose 250–400 mg/dl) and then the mice were treated with either PBS, galactose (200 mg/kg mouse, i.p.), or glucose (200 mg/kg mouse, i.p.) solution. Two hours after administration and removal of the diet, the mice were killed and the membrane fraction in mouse liver was isolated. GLUT2 and Na, K-ATPase were detected by Western blot analysis with anti-GLUT2 antibody or anti-Na, K-ATPase antibody. Immunoblots of GLUT2 and Na, K-ATPase (Top) and calculations of relative GLUT2 (Bottom). n = 3–4 per group. Data at the bottom of the figure are shown as means ± SD. In all panels, the statistical significance of the difference was evaluated using Student's t test.
Figure Legend Snippet: Identification of galactose as a hypoglycemic compound using the hyperglycemic silkworm model. (A) Preparation protocol for the jiou extract. (B) Silkworms were fed a 10% (w/w) glucose diet for 60 min. 50 µl of Jiou extract (1 mg/ml) or human insulin (3.5 mg/ml) was injected into the hemolymph of the hyperglycemic silkworms. The silkworms were fasted for 6 h and the sugar level in the hemolymph was determined. n = 6–7 per group. Data are shown as means ± SD. (C, D) The jiou extract was treated with TFA, and analyzed by TLC. Sugars were localized with 10% sulfuric acid solution. (E) Silkworms were fed a 10% (w/w) glucose diet for 60 min. 50 µl of D-Galactose (Gal), D-glucose (Glu), D-talose (Tal), D-mannose (Man), (1 mg/ml) or human insulin (3.5 mg/ml) was injected into the hemolymph of hyperglycemic silkworms. Silkworms were fasted for 6 h and sugar level in the hemolymph was determined. n = 6 per group. (F) Structure of sugar is shown by Fischer projection in the panel. Numbers shown on the left indicate the carbon positions of the sugar. Red hydroxyl group indicates the positions that differ from D-galactose. Activity represents the hypoglycemic effect. Data are shown as means ± SD. NS; not significant. (G) Galactose (10 mg/ml, 0.5 ml i.p.) was injected to streptozotocin induced-diabetic mice, and blood glucose level was determined after 4 h of fasting. Blood glucose levels in streptozotocin-induced hyperglycemic mice were measured (blood glucose 250–400 mg/dl) and then the mice were treated with either PBS or galactose solution. Four hours after administration and the removal of diet, the blood glucose levels were measured again. The data represent the blood glucose value after treatment divided by the blood glucose value before treatment of individual animals. In all panels, the statistical significance of the difference was evaluated using Student's t test. (H) Blood glucose levels in streptozotocin-induced hyperglycemic mice were measured (blood glucose 250–400 mg/dl) and then the mice were treated with either PBS, galactose (200 mg/kg mouse, i.p.), or glucose (200 mg/kg mouse, i.p.) solution. Two hours after administration and removal of the diet, the mice were killed and the membrane fraction in mouse liver was isolated. GLUT2 and Na, K-ATPase were detected by Western blot analysis with anti-GLUT2 antibody or anti-Na, K-ATPase antibody. Immunoblots of GLUT2 and Na, K-ATPase (Top) and calculations of relative GLUT2 (Bottom). n = 3–4 per group. Data at the bottom of the figure are shown as means ± SD. In all panels, the statistical significance of the difference was evaluated using Student's t test.

Techniques Used: Injection, Thin Layer Chromatography, Activity Assay, Mouse Assay, Isolation, Western Blot

2) Product Images from "An Invertebrate Hyperglycemic Model for the Identification of Anti-Diabetic Drugs"

Article Title: An Invertebrate Hyperglycemic Model for the Identification of Anti-Diabetic Drugs

Journal: PLoS ONE

doi: 10.1371/journal.pone.0018292

Identification of galactose as a hypoglycemic compound using the hyperglycemic silkworm model. (A) Preparation protocol for the jiou extract. (B) Silkworms were fed a 10% (w/w) glucose diet for 60 min. 50 µl of Jiou extract (1 mg/ml) or human insulin (3.5 mg/ml) was injected into the hemolymph of the hyperglycemic silkworms. The silkworms were fasted for 6 h and the sugar level in the hemolymph was determined. n = 6–7 per group. Data are shown as means ± SD. (C, D) The jiou extract was treated with TFA, and analyzed by TLC. Sugars were localized with 10% sulfuric acid solution. (E) Silkworms were fed a 10% (w/w) glucose diet for 60 min. 50 µl of D-Galactose (Gal), D-glucose (Glu), D-talose (Tal), D-mannose (Man), (1 mg/ml) or human insulin (3.5 mg/ml) was injected into the hemolymph of hyperglycemic silkworms. Silkworms were fasted for 6 h and sugar level in the hemolymph was determined. n = 6 per group. (F) Structure of sugar is shown by Fischer projection in the panel. Numbers shown on the left indicate the carbon positions of the sugar. Red hydroxyl group indicates the positions that differ from D-galactose. Activity represents the hypoglycemic effect. Data are shown as means ± SD. NS; not significant. (G) Galactose (10 mg/ml, 0.5 ml i.p.) was injected to streptozotocin induced-diabetic mice, and blood glucose level was determined after 4 h of fasting. Blood glucose levels in streptozotocin-induced hyperglycemic mice were measured (blood glucose 250–400 mg/dl) and then the mice were treated with either PBS or galactose solution. Four hours after administration and the removal of diet, the blood glucose levels were measured again. The data represent the blood glucose value after treatment divided by the blood glucose value before treatment of individual animals. In all panels, the statistical significance of the difference was evaluated using Student's t test. (H) Blood glucose levels in streptozotocin-induced hyperglycemic mice were measured (blood glucose 250–400 mg/dl) and then the mice were treated with either PBS, galactose (200 mg/kg mouse, i.p.), or glucose (200 mg/kg mouse, i.p.) solution. Two hours after administration and removal of the diet, the mice were killed and the membrane fraction in mouse liver was isolated. GLUT2 and Na, K-ATPase were detected by Western blot analysis with anti-GLUT2 antibody or anti-Na, K-ATPase antibody. Immunoblots of GLUT2 and Na, K-ATPase (Top) and calculations of relative GLUT2 (Bottom). n = 3–4 per group. Data at the bottom of the figure are shown as means ± SD. In all panels, the statistical significance of the difference was evaluated using Student's t test.
Figure Legend Snippet: Identification of galactose as a hypoglycemic compound using the hyperglycemic silkworm model. (A) Preparation protocol for the jiou extract. (B) Silkworms were fed a 10% (w/w) glucose diet for 60 min. 50 µl of Jiou extract (1 mg/ml) or human insulin (3.5 mg/ml) was injected into the hemolymph of the hyperglycemic silkworms. The silkworms were fasted for 6 h and the sugar level in the hemolymph was determined. n = 6–7 per group. Data are shown as means ± SD. (C, D) The jiou extract was treated with TFA, and analyzed by TLC. Sugars were localized with 10% sulfuric acid solution. (E) Silkworms were fed a 10% (w/w) glucose diet for 60 min. 50 µl of D-Galactose (Gal), D-glucose (Glu), D-talose (Tal), D-mannose (Man), (1 mg/ml) or human insulin (3.5 mg/ml) was injected into the hemolymph of hyperglycemic silkworms. Silkworms were fasted for 6 h and sugar level in the hemolymph was determined. n = 6 per group. (F) Structure of sugar is shown by Fischer projection in the panel. Numbers shown on the left indicate the carbon positions of the sugar. Red hydroxyl group indicates the positions that differ from D-galactose. Activity represents the hypoglycemic effect. Data are shown as means ± SD. NS; not significant. (G) Galactose (10 mg/ml, 0.5 ml i.p.) was injected to streptozotocin induced-diabetic mice, and blood glucose level was determined after 4 h of fasting. Blood glucose levels in streptozotocin-induced hyperglycemic mice were measured (blood glucose 250–400 mg/dl) and then the mice were treated with either PBS or galactose solution. Four hours after administration and the removal of diet, the blood glucose levels were measured again. The data represent the blood glucose value after treatment divided by the blood glucose value before treatment of individual animals. In all panels, the statistical significance of the difference was evaluated using Student's t test. (H) Blood glucose levels in streptozotocin-induced hyperglycemic mice were measured (blood glucose 250–400 mg/dl) and then the mice were treated with either PBS, galactose (200 mg/kg mouse, i.p.), or glucose (200 mg/kg mouse, i.p.) solution. Two hours after administration and removal of the diet, the mice were killed and the membrane fraction in mouse liver was isolated. GLUT2 and Na, K-ATPase were detected by Western blot analysis with anti-GLUT2 antibody or anti-Na, K-ATPase antibody. Immunoblots of GLUT2 and Na, K-ATPase (Top) and calculations of relative GLUT2 (Bottom). n = 3–4 per group. Data at the bottom of the figure are shown as means ± SD. In all panels, the statistical significance of the difference was evaluated using Student's t test.

Techniques Used: Injection, Thin Layer Chromatography, Activity Assay, Mouse Assay, Isolation, Western Blot

3) Product Images from "Intrinsic reaction-cycle time scale of Na+,K+-ATPase manifests itself in the lipid-protein interactions of nonequilibrium membranes"

Article Title: Intrinsic reaction-cycle time scale of Na+,K+-ATPase manifests itself in the lipid-protein interactions of nonequilibrium membranes

Journal: Proceedings of the National Academy of Sciences of the United States of America

doi: 10.1073/pnas.1209909109

Normalized temporal correlation function for mode n = 5 for proteoGUVs of DOPC/DOPS/Chol/ATPase of similar reduced membrane tension. ( A ) Nonactive membranes in the absence of ATP conforming to a monoexponential form of the short-time decay (solid line).
Figure Legend Snippet: Normalized temporal correlation function for mode n = 5 for proteoGUVs of DOPC/DOPS/Chol/ATPase of similar reduced membrane tension. ( A ) Nonactive membranes in the absence of ATP conforming to a monoexponential form of the short-time decay (solid line).

Techniques Used:

For a proteoGUV of DOPC/DOPS/Chol/ATPase, a radius of 12.97 μm in the presence of 1 mM of ATP is shown: ( A ) Experimental distribution of the Fourier amplitudes of the contour fluctuations; α 5 or β 5 . ( B ) Plot of the normalized temporal
Figure Legend Snippet: For a proteoGUV of DOPC/DOPS/Chol/ATPase, a radius of 12.97 μm in the presence of 1 mM of ATP is shown: ( A ) Experimental distribution of the Fourier amplitudes of the contour fluctuations; α 5 or β 5 . ( B ) Plot of the normalized temporal

Techniques Used:

Relaxation time as a function of mode number, n , for active membranes consisting of a proteoGUV of DOPC/DOPS/Chol/ATPase in the presence of ATP, (compare with ). ( A ) The initial relaxation time scales as τ 1 ∼ n –3.1 for modes
Figure Legend Snippet: Relaxation time as a function of mode number, n , for active membranes consisting of a proteoGUV of DOPC/DOPS/Chol/ATPase in the presence of ATP, (compare with ). ( A ) The initial relaxation time scales as τ 1 ∼ n –3.1 for modes

Techniques Used:

4) Product Images from "Intrinsic reaction-cycle time scale of Na+,K+-ATPase manifests itself in the lipid-protein interactions of nonequilibrium membranes"

Article Title: Intrinsic reaction-cycle time scale of Na+,K+-ATPase manifests itself in the lipid-protein interactions of nonequilibrium membranes

Journal: Proceedings of the National Academy of Sciences of the United States of America

doi: 10.1073/pnas.1209909109

For a proteoGUV of DOPC/DOPS/Chol/ATPase, a radius of 12.97 μm in the presence of 1 mM of ATP is shown: ( A ) Experimental distribution of the Fourier amplitudes of the contour fluctuations; α 5 or β 5 . ( B ) Plot of the normalized temporal
Figure Legend Snippet: For a proteoGUV of DOPC/DOPS/Chol/ATPase, a radius of 12.97 μm in the presence of 1 mM of ATP is shown: ( A ) Experimental distribution of the Fourier amplitudes of the contour fluctuations; α 5 or β 5 . ( B ) Plot of the normalized temporal

Techniques Used:

5) Product Images from "Effects of N-Acetylcysteine on Nicotinamide Dinucleotide Phosphate Oxidase Activation and Antioxidant Status in Heart, Lung, Liver and Kidney in Streptozotocin-Induced Diabetic Rats"

Article Title: Effects of N-Acetylcysteine on Nicotinamide Dinucleotide Phosphate Oxidase Activation and Antioxidant Status in Heart, Lung, Liver and Kidney in Streptozotocin-Induced Diabetic Rats

Journal: Yonsei Medical Journal

doi: 10.3349/ymj.2012.53.2.294

Western blots analysis of NADPH oxidase subunits p22phox and p67phox protein expression in various tissues. Control (C) or STZ-induced diabetic rats were either untreated (D) or treated with the antioxidant N-acetylcysteine (1.5 g/kg/day, D+NAC) by oral gavage for four weeks. (A) (top) Representative Western blot showing p22phox expression with GAPDH as a loading control in total tissue extracts; (bottom, graph) p22phox densitometric values were normalized to their corresponding GAPDH densitometric values and expressed as percent change relative to the measurement in control rats. (B) (top) Representative Western blot showing p67phox expression with GAPDH as a loading control in cytosol fractions; (bottom, graph) p67phox densitometric values were normalized to their corresponding GAPDH densitometric values and expressed as percent change relative to the measurement in control rats. (C)(top) Representative Western blot showing p67phox expression with Na, K-ATPase as a loading control in membrane fractions; (bottom, graph) p67phox densitometric values were normalized to their corresponding Na, K-ATPase densitometric values and expressed as percent change relative to the measurement in control rats. All the results are expressed as means±S.E.M., n=7, * p
Figure Legend Snippet: Western blots analysis of NADPH oxidase subunits p22phox and p67phox protein expression in various tissues. Control (C) or STZ-induced diabetic rats were either untreated (D) or treated with the antioxidant N-acetylcysteine (1.5 g/kg/day, D+NAC) by oral gavage for four weeks. (A) (top) Representative Western blot showing p22phox expression with GAPDH as a loading control in total tissue extracts; (bottom, graph) p22phox densitometric values were normalized to their corresponding GAPDH densitometric values and expressed as percent change relative to the measurement in control rats. (B) (top) Representative Western blot showing p67phox expression with GAPDH as a loading control in cytosol fractions; (bottom, graph) p67phox densitometric values were normalized to their corresponding GAPDH densitometric values and expressed as percent change relative to the measurement in control rats. (C)(top) Representative Western blot showing p67phox expression with Na, K-ATPase as a loading control in membrane fractions; (bottom, graph) p67phox densitometric values were normalized to their corresponding Na, K-ATPase densitometric values and expressed as percent change relative to the measurement in control rats. All the results are expressed as means±S.E.M., n=7, * p

Techniques Used: Western Blot, Expressing

6) Product Images from "Expression and Function of the Lipocalin-2 (24p3/NGAL) Receptor in Rodent and Human Intestinal Epithelia"

Article Title: Expression and Function of the Lipocalin-2 (24p3/NGAL) Receptor in Rodent and Human Intestinal Epithelia

Journal: PLoS ONE

doi: 10.1371/journal.pone.0071586

Expression of hNGAL-R in Caco-2 BBE cells. RT-PCR for hNGAL-R and GAPDH in colon-like Caco-2 BBE cells ( A ). A PCR product of 296 bp is amplified from colon-like Caco-2 BBE cell cDNA using specific primers for human NGAL-R and reverse transcriptase (+RT), but not in the control reaction without reverse transcriptase (-RT). The housekeeping gene human GAPDH is used as a control. A 326 bp PCR product is only amplified in the presence of reverse transcriptase (+RT). Immunoblotting of colon-like Caco-2 BBE cell homogenate (Ho) and plasma membranes (PM) ( B ). Specific signals are detected in PM of colon-like Caco-2 BBE cells with antibodies against hNGAL-R (α-CT-24p3-R; 1:500) and the α1-subunit of Na + ,K + -ATPase (1:500). Live immunofluorescence staining of non-permeabilized colon- and duodenum-like Caco-2 BBE cells ( C and D ). Immunofluorescence staining with α-NT-24p3-R (1:100) reveals hNGAL-R expression (red fluorescence) at apical (asterisks) and lateral plasma membranes (arrows) of colon-like Caco-2 BBE cells ( C ). No staining for hNGAL-R is detected in duodenum-like Caco-2 BBE cells ( D ).
Figure Legend Snippet: Expression of hNGAL-R in Caco-2 BBE cells. RT-PCR for hNGAL-R and GAPDH in colon-like Caco-2 BBE cells ( A ). A PCR product of 296 bp is amplified from colon-like Caco-2 BBE cell cDNA using specific primers for human NGAL-R and reverse transcriptase (+RT), but not in the control reaction without reverse transcriptase (-RT). The housekeeping gene human GAPDH is used as a control. A 326 bp PCR product is only amplified in the presence of reverse transcriptase (+RT). Immunoblotting of colon-like Caco-2 BBE cell homogenate (Ho) and plasma membranes (PM) ( B ). Specific signals are detected in PM of colon-like Caco-2 BBE cells with antibodies against hNGAL-R (α-CT-24p3-R; 1:500) and the α1-subunit of Na + ,K + -ATPase (1:500). Live immunofluorescence staining of non-permeabilized colon- and duodenum-like Caco-2 BBE cells ( C and D ). Immunofluorescence staining with α-NT-24p3-R (1:100) reveals hNGAL-R expression (red fluorescence) at apical (asterisks) and lateral plasma membranes (arrows) of colon-like Caco-2 BBE cells ( C ). No staining for hNGAL-R is detected in duodenum-like Caco-2 BBE cells ( D ).

Techniques Used: Expressing, Reverse Transcription Polymerase Chain Reaction, Polymerase Chain Reaction, Amplification, Immunofluorescence, Staining, Fluorescence

Related Articles

Modification:

Article Title: Intrinsic reaction-cycle time scale of Na+,K+-ATPase manifests itself in the lipid-protein interactions of nonequilibrium membranes
Article Snippet: .. This included the determination of ( i ) the pump density through protein determination of reconstituted ATPase performed according to Peterson modification ( ) of the Lowry method; ( ii ) the symmetry of protein insertion—i.e., rightside-out (r/o), inside-out (i/o), or nonoriented (n-o), where the fraction of enzyme reconstituted as i/o was determined using functional tests as described in detail in ( , ); and ( iii ) the maximum hydrolytic activity of reconstituted i/o-oriented Na+ ,K+ -ATPase measured using [32 P]-ATP as described in ( ). .. The protein orientation after reconstitution was determined taking advantage of the sidedness of the Na,K-ATPase including a high cytoplasmic Na+ -affinity, a high extracellular K+ -affinity, and an extracellular ouabain binding site.

Functional Assay:

Article Title: Intrinsic reaction-cycle time scale of Na+,K+-ATPase manifests itself in the lipid-protein interactions of nonequilibrium membranes
Article Snippet: .. This included the determination of ( i ) the pump density through protein determination of reconstituted ATPase performed according to Peterson modification ( ) of the Lowry method; ( ii ) the symmetry of protein insertion—i.e., rightside-out (r/o), inside-out (i/o), or nonoriented (n-o), where the fraction of enzyme reconstituted as i/o was determined using functional tests as described in detail in ( , ); and ( iii ) the maximum hydrolytic activity of reconstituted i/o-oriented Na+ ,K+ -ATPase measured using [32 P]-ATP as described in ( ). .. The protein orientation after reconstitution was determined taking advantage of the sidedness of the Na,K-ATPase including a high cytoplasmic Na+ -affinity, a high extracellular K+ -affinity, and an extracellular ouabain binding site.

other:

Article Title: An Invertebrate Hyperglycemic Model for the Identification of Anti-Diabetic Drugs
Article Snippet: The relative amount of phosphorylated Akt or phosphorylated AMPK or GLUT2 on total Akt or total AMPK or Na, K-ATPase was determined.

Article Title: Intrinsic reaction-cycle time scale of Na+,K+-ATPase manifests itself in the lipid-protein interactions of nonequilibrium membranes
Article Snippet: Cornelius F. Phosphorylation/dephosphorylation of reconstituted shark Na+ ,K(+ )-ATPase: One phosphorylation site per α β protomer.

Article Title: An Invertebrate Hyperglycemic Model for the Identification of Anti-Diabetic Drugs
Article Snippet: GLUT2 and Na, K-ATPase in the membrane fraction of mouse liver were detected by immunoblot analysis using anti-GLUT2 and anti-Na, K-ATPase antibody.

Article Title: Intrinsic reaction-cycle time scale of Na+,K+-ATPase manifests itself in the lipid-protein interactions of nonequilibrium membranes
Article Snippet: The detergent was subsequently removed by addition of hydrophobic Bio-Beads, and liposomes containing reconstituted Na+ ,K+ -ATPase spontaneously formed.

Activity Assay:

Article Title: Intrinsic reaction-cycle time scale of Na+,K+-ATPase manifests itself in the lipid-protein interactions of nonequilibrium membranes
Article Snippet: .. This included the determination of ( i ) the pump density through protein determination of reconstituted ATPase performed according to Peterson modification ( ) of the Lowry method; ( ii ) the symmetry of protein insertion—i.e., rightside-out (r/o), inside-out (i/o), or nonoriented (n-o), where the fraction of enzyme reconstituted as i/o was determined using functional tests as described in detail in ( , ); and ( iii ) the maximum hydrolytic activity of reconstituted i/o-oriented Na+ ,K+ -ATPase measured using [32 P]-ATP as described in ( ). .. The protein orientation after reconstitution was determined taking advantage of the sidedness of the Na,K-ATPase including a high cytoplasmic Na+ -affinity, a high extracellular K+ -affinity, and an extracellular ouabain binding site.

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    Cell Signaling Technology Inc k atpase
    Identification of galactose as a hypoglycemic compound using the hyperglycemic silkworm model. (A) Preparation protocol for the jiou extract. (B) Silkworms were fed a 10% (w/w) glucose diet for 60 min. 50 µl of Jiou extract (1 mg/ml) or human insulin (3.5 mg/ml) was injected into the hemolymph of the hyperglycemic silkworms. The silkworms were fasted for 6 h and the sugar level in the hemolymph was determined. n = 6–7 per group. Data are shown as means ± SD. (C, D) The jiou extract was treated with TFA, and analyzed by TLC. Sugars were localized with 10% sulfuric acid solution. (E) Silkworms were fed a 10% (w/w) glucose diet for 60 min. 50 µl of D-Galactose (Gal), D-glucose (Glu), D-talose (Tal), D-mannose (Man), (1 mg/ml) or human insulin (3.5 mg/ml) was injected into the hemolymph of hyperglycemic silkworms. Silkworms were fasted for 6 h and sugar level in the hemolymph was determined. n = 6 per group. (F) Structure of sugar is shown by Fischer projection in the panel. Numbers shown on the left indicate the carbon positions of the sugar. Red hydroxyl group indicates the positions that differ from D-galactose. Activity represents the hypoglycemic effect. Data are shown as means ± SD. NS; not significant. (G) Galactose (10 mg/ml, 0.5 ml i.p.) was injected to streptozotocin induced-diabetic mice, and blood glucose level was determined after 4 h of fasting. Blood glucose levels in streptozotocin-induced hyperglycemic mice were measured (blood glucose 250–400 mg/dl) and then the mice were treated with either PBS or galactose solution. Four hours after administration and the removal of diet, the blood glucose levels were measured again. The data represent the blood glucose value after treatment divided by the blood glucose value before treatment of individual animals. In all panels, the statistical significance of the difference was evaluated using Student's t test. (H) Blood glucose levels in streptozotocin-induced hyperglycemic mice were measured (blood glucose 250–400 mg/dl) and then the mice were treated with either PBS, galactose (200 mg/kg mouse, i.p.), or glucose (200 mg/kg mouse, i.p.) solution. Two hours after administration and removal of the diet, the mice were killed and the membrane fraction in mouse liver was isolated. <t>GLUT2</t> and Na, <t>K-ATPase</t> were detected by Western blot analysis with anti-GLUT2 antibody or anti-Na, K-ATPase antibody. Immunoblots of GLUT2 and Na, K-ATPase (Top) and calculations of relative GLUT2 (Bottom). n = 3–4 per group. Data at the bottom of the figure are shown as means ± SD. In all panels, the statistical significance of the difference was evaluated using Student's t test.
    K Atpase, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 92/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/k atpase/product/Cell Signaling Technology Inc
    Average 92 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    k atpase - by Bioz Stars, 2020-05
    92/100 stars
      Buy from Supplier

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    Cell Signaling Technology Inc na k atpase
    Effect of garlic and its metabolites on Na + /K + <t>-ATPase</t> expression. (A,B) Western blot and bar graph of Na + /K + -ATPase from H9C2 cells. (C,D) Western blot and bar graph of Na + /K + -ATPase from rat heart. (Gels and blots were cropped and run under same experimental conditions). ( N = 3). Data were shown as mean ± SEM, ∗ p
    Na K Atpase, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 36 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/na k atpase/product/Cell Signaling Technology Inc
    Average 93 stars, based on 36 article reviews
    Price from $9.99 to $1999.99
    na k atpase - by Bioz Stars, 2020-05
    93/100 stars
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    Identification of galactose as a hypoglycemic compound using the hyperglycemic silkworm model. (A) Preparation protocol for the jiou extract. (B) Silkworms were fed a 10% (w/w) glucose diet for 60 min. 50 µl of Jiou extract (1 mg/ml) or human insulin (3.5 mg/ml) was injected into the hemolymph of the hyperglycemic silkworms. The silkworms were fasted for 6 h and the sugar level in the hemolymph was determined. n = 6–7 per group. Data are shown as means ± SD. (C, D) The jiou extract was treated with TFA, and analyzed by TLC. Sugars were localized with 10% sulfuric acid solution. (E) Silkworms were fed a 10% (w/w) glucose diet for 60 min. 50 µl of D-Galactose (Gal), D-glucose (Glu), D-talose (Tal), D-mannose (Man), (1 mg/ml) or human insulin (3.5 mg/ml) was injected into the hemolymph of hyperglycemic silkworms. Silkworms were fasted for 6 h and sugar level in the hemolymph was determined. n = 6 per group. (F) Structure of sugar is shown by Fischer projection in the panel. Numbers shown on the left indicate the carbon positions of the sugar. Red hydroxyl group indicates the positions that differ from D-galactose. Activity represents the hypoglycemic effect. Data are shown as means ± SD. NS; not significant. (G) Galactose (10 mg/ml, 0.5 ml i.p.) was injected to streptozotocin induced-diabetic mice, and blood glucose level was determined after 4 h of fasting. Blood glucose levels in streptozotocin-induced hyperglycemic mice were measured (blood glucose 250–400 mg/dl) and then the mice were treated with either PBS or galactose solution. Four hours after administration and the removal of diet, the blood glucose levels were measured again. The data represent the blood glucose value after treatment divided by the blood glucose value before treatment of individual animals. In all panels, the statistical significance of the difference was evaluated using Student's t test. (H) Blood glucose levels in streptozotocin-induced hyperglycemic mice were measured (blood glucose 250–400 mg/dl) and then the mice were treated with either PBS, galactose (200 mg/kg mouse, i.p.), or glucose (200 mg/kg mouse, i.p.) solution. Two hours after administration and removal of the diet, the mice were killed and the membrane fraction in mouse liver was isolated. GLUT2 and Na, K-ATPase were detected by Western blot analysis with anti-GLUT2 antibody or anti-Na, K-ATPase antibody. Immunoblots of GLUT2 and Na, K-ATPase (Top) and calculations of relative GLUT2 (Bottom). n = 3–4 per group. Data at the bottom of the figure are shown as means ± SD. In all panels, the statistical significance of the difference was evaluated using Student's t test.

    Journal: PLoS ONE

    Article Title: An Invertebrate Hyperglycemic Model for the Identification of Anti-Diabetic Drugs

    doi: 10.1371/journal.pone.0018292

    Figure Lengend Snippet: Identification of galactose as a hypoglycemic compound using the hyperglycemic silkworm model. (A) Preparation protocol for the jiou extract. (B) Silkworms were fed a 10% (w/w) glucose diet for 60 min. 50 µl of Jiou extract (1 mg/ml) or human insulin (3.5 mg/ml) was injected into the hemolymph of the hyperglycemic silkworms. The silkworms were fasted for 6 h and the sugar level in the hemolymph was determined. n = 6–7 per group. Data are shown as means ± SD. (C, D) The jiou extract was treated with TFA, and analyzed by TLC. Sugars were localized with 10% sulfuric acid solution. (E) Silkworms were fed a 10% (w/w) glucose diet for 60 min. 50 µl of D-Galactose (Gal), D-glucose (Glu), D-talose (Tal), D-mannose (Man), (1 mg/ml) or human insulin (3.5 mg/ml) was injected into the hemolymph of hyperglycemic silkworms. Silkworms were fasted for 6 h and sugar level in the hemolymph was determined. n = 6 per group. (F) Structure of sugar is shown by Fischer projection in the panel. Numbers shown on the left indicate the carbon positions of the sugar. Red hydroxyl group indicates the positions that differ from D-galactose. Activity represents the hypoglycemic effect. Data are shown as means ± SD. NS; not significant. (G) Galactose (10 mg/ml, 0.5 ml i.p.) was injected to streptozotocin induced-diabetic mice, and blood glucose level was determined after 4 h of fasting. Blood glucose levels in streptozotocin-induced hyperglycemic mice were measured (blood glucose 250–400 mg/dl) and then the mice were treated with either PBS or galactose solution. Four hours after administration and the removal of diet, the blood glucose levels were measured again. The data represent the blood glucose value after treatment divided by the blood glucose value before treatment of individual animals. In all panels, the statistical significance of the difference was evaluated using Student's t test. (H) Blood glucose levels in streptozotocin-induced hyperglycemic mice were measured (blood glucose 250–400 mg/dl) and then the mice were treated with either PBS, galactose (200 mg/kg mouse, i.p.), or glucose (200 mg/kg mouse, i.p.) solution. Two hours after administration and removal of the diet, the mice were killed and the membrane fraction in mouse liver was isolated. GLUT2 and Na, K-ATPase were detected by Western blot analysis with anti-GLUT2 antibody or anti-Na, K-ATPase antibody. Immunoblots of GLUT2 and Na, K-ATPase (Top) and calculations of relative GLUT2 (Bottom). n = 3–4 per group. Data at the bottom of the figure are shown as means ± SD. In all panels, the statistical significance of the difference was evaluated using Student's t test.

    Article Snippet: The relative amount of phosphorylated Akt or phosphorylated AMPK or GLUT2 on total Akt or total AMPK or Na, K-ATPase was determined.

    Techniques: Injection, Thin Layer Chromatography, Activity Assay, Mouse Assay, Isolation, Western Blot

    Effect of garlic and its metabolites on Na + /K + -ATPase expression. (A,B) Western blot and bar graph of Na + /K + -ATPase from H9C2 cells. (C,D) Western blot and bar graph of Na + /K + -ATPase from rat heart. (Gels and blots were cropped and run under same experimental conditions). ( N = 3). Data were shown as mean ± SEM, ∗ p

    Journal: Frontiers in Pharmacology

    Article Title: Novel Sulfur Metabolites of Garlic Attenuate Cardiac Hypertrophy and Remodeling through Induction of Na+/K+-ATPase Expression

    doi: 10.3389/fphar.2017.00018

    Figure Lengend Snippet: Effect of garlic and its metabolites on Na + /K + -ATPase expression. (A,B) Western blot and bar graph of Na + /K + -ATPase from H9C2 cells. (C,D) Western blot and bar graph of Na + /K + -ATPase from rat heart. (Gels and blots were cropped and run under same experimental conditions). ( N = 3). Data were shown as mean ± SEM, ∗ p

    Article Snippet: Garlic and Its Metabolites Failed to Show Any Anti-Hypertrophic Effect in H9C2 Cells in Presence of Na+ /K+ -ATPase Inhibitor To confirm whether garlic and its metabolites showed their anti-hypertrophic effect through Na+ /K+ -ATPase, we treated H9C2 cells with Iso in presence and absence of digoxin, a Na+ /K+ -ATPase inhibitor.

    Techniques: Expressing, Western Blot

    Stable expression of wild-type and mutant forms of rat α -1 subunit of Na+ /K+ -ATPase in OK cells

    Journal: The Biochemical journal

    Article Title: Angiotensin II-dependent phosphorylation at Ser11/Ser18 and Ser938 shifts the E2 conformations of rat kidney Na+/K+-ATPase

    doi: 10.1042/BJ20111398

    Figure Lengend Snippet: Stable expression of wild-type and mutant forms of rat α -1 subunit of Na+ /K+ -ATPase in OK cells

    Article Snippet: This is the first demonstration that Ang II-dependent phosphorylation of any form of Na+/ K+ -ATPase can regulate any of the basic biochemical properties of the Na+/ K+ -ATPase.

    Techniques: Expressing, Mutagenesis

    Relative effect of Ang II on the elution of plasma membrane protein containing Populations #1, #2 and #3 of Na + /K + -ATPase from rat α -1.wild-type (A), α -1.S11A/S18A (B) and α -1.S938A (C) cells

    Journal: The Biochemical journal

    Article Title: Angiotensin II-dependent phosphorylation at Ser11/Ser18 and Ser938 shifts the E2 conformations of rat kidney Na+/K+-ATPase

    doi: 10.1042/BJ20111398

    Figure Lengend Snippet: Relative effect of Ang II on the elution of plasma membrane protein containing Populations #1, #2 and #3 of Na + /K + -ATPase from rat α -1.wild-type (A), α -1.S11A/S18A (B) and α -1.S938A (C) cells

    Article Snippet: This is the first demonstration that Ang II-dependent phosphorylation of any form of Na+/ K+ -ATPase can regulate any of the basic biochemical properties of the Na+/ K+ -ATPase.

    Techniques:

    Three populations of Na+ /K+ -ATPase in plasma membranes of α -1.S11A/S18A and α -1.S938A cells

    Journal: The Biochemical journal

    Article Title: Angiotensin II-dependent phosphorylation at Ser11/Ser18 and Ser938 shifts the E2 conformations of rat kidney Na+/K+-ATPase

    doi: 10.1042/BJ20111398

    Figure Lengend Snippet: Three populations of Na+ /K+ -ATPase in plasma membranes of α -1.S11A/S18A and α -1.S938A cells

    Article Snippet: This is the first demonstration that Ang II-dependent phosphorylation of any form of Na+/ K+ -ATPase can regulate any of the basic biochemical properties of the Na+/ K+ -ATPase.

    Techniques:

    Phosphorylation of rat kidney Na + /K + -ATPase at Ser 18

    Journal: The Biochemical journal

    Article Title: Angiotensin II-dependent phosphorylation at Ser11/Ser18 and Ser938 shifts the E2 conformations of rat kidney Na+/K+-ATPase

    doi: 10.1042/BJ20111398

    Figure Lengend Snippet: Phosphorylation of rat kidney Na + /K + -ATPase at Ser 18

    Article Snippet: This is the first demonstration that Ang II-dependent phosphorylation of any form of Na+/ K+ -ATPase can regulate any of the basic biochemical properties of the Na+/ K+ -ATPase.

    Techniques:

    Phosphorylation of rat kidney Na + /K + -ATPase at Ser 11

    Journal: The Biochemical journal

    Article Title: Angiotensin II-dependent phosphorylation at Ser11/Ser18 and Ser938 shifts the E2 conformations of rat kidney Na+/K+-ATPase

    doi: 10.1042/BJ20111398

    Figure Lengend Snippet: Phosphorylation of rat kidney Na + /K + -ATPase at Ser 11

    Article Snippet: This is the first demonstration that Ang II-dependent phosphorylation of any form of Na+/ K+ -ATPase can regulate any of the basic biochemical properties of the Na+/ K+ -ATPase.

    Techniques:

    Phosphorylation of rat kidney Na + /K + -ATPase at Ser 938

    Journal: The Biochemical journal

    Article Title: Angiotensin II-dependent phosphorylation at Ser11/Ser18 and Ser938 shifts the E2 conformations of rat kidney Na+/K+-ATPase

    doi: 10.1042/BJ20111398

    Figure Lengend Snippet: Phosphorylation of rat kidney Na + /K + -ATPase at Ser 938

    Article Snippet: This is the first demonstration that Ang II-dependent phosphorylation of any form of Na+/ K+ -ATPase can regulate any of the basic biochemical properties of the Na+/ K+ -ATPase.

    Techniques:

    Elution from digoxin-affinity columns of plasma membrane protein containing Na + /K + -ATPase Populations #1 (fractions 1–9), #2 (fractions 10–18) and #3 (fractions 19–22) from control and Ang II-treated α -1.S11A/S18A cells

    Journal: The Biochemical journal

    Article Title: Angiotensin II-dependent phosphorylation at Ser11/Ser18 and Ser938 shifts the E2 conformations of rat kidney Na+/K+-ATPase

    doi: 10.1042/BJ20111398

    Figure Lengend Snippet: Elution from digoxin-affinity columns of plasma membrane protein containing Na + /K + -ATPase Populations #1 (fractions 1–9), #2 (fractions 10–18) and #3 (fractions 19–22) from control and Ang II-treated α -1.S11A/S18A cells

    Article Snippet: This is the first demonstration that Ang II-dependent phosphorylation of any form of Na+/ K+ -ATPase can regulate any of the basic biochemical properties of the Na+/ K+ -ATPase.

    Techniques:

    Cell surface biotinylation of HT29-MTX cells. A, specificity of antibodies used for UGT1A and control protein detection with the ProteinSimple SIMON system. B, relative peak area of protein levels detected in surface biotinylation samples after streptavidin pulldown (UGT1A, Na + /K + -ATPase) and in whole cell lysate (GAPDH).

    Journal: The Journal of Biological Chemistry

    Article Title: Cellular Asymmetric Catalysis by UDP-glucuronosyltransferase 1A8 Shows Functional Localization to the Basolateral Plasma Membrane *

    doi: 10.1074/jbc.M114.634428

    Figure Lengend Snippet: Cell surface biotinylation of HT29-MTX cells. A, specificity of antibodies used for UGT1A and control protein detection with the ProteinSimple SIMON system. B, relative peak area of protein levels detected in surface biotinylation samples after streptavidin pulldown (UGT1A, Na + /K + -ATPase) and in whole cell lysate (GAPDH).

    Article Snippet: UGT1A was obtained from Santa Cruz Biotechnology (Dallas, TX); GAPDH, Na+ /K+ -ATPase, and α-actinin were from Cell Signaling Technologies (New England Biolabs, Herts, UK).

    Techniques: