mouse igd Search Results


mouse igd  (R&D Systems)
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R&D Systems mouse igd
Mouse Igd, supplied by R&D Systems, 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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anti igd  (SouthernBiotech)
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SouthernBiotech anti igd
Anti Igd, supplied by SouthernBiotech, 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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nbp2 69334 rrid ab 3354390  (Novus Biologicals)
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Novus Biologicals nbp2 69334 rrid ab 3354390
Nbp2 69334 Rrid Ab 3354390, supplied by Novus Biologicals, 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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igd  (Bio-Rad)
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Bio-Rad igd
Igd, supplied by Bio-Rad, 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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mouse monoclonal antibodies  (Novus Biologicals)
93
Novus Biologicals mouse monoclonal antibodies
FIG. 5. CsA activates Pro-564 hydroxylase. A kidney light mito- chondrial fraction was used as a source of enzyme. Activity was defined as the Pro-564 peptide-dependent degradation of 2-OG. The peptide- independent activity was determined in each experiment and was sub- strated from the data. Means S.E. from triplicate measurements are shown. A, 2-OG dependence. Experiments were performed in the pres- ence of 100 M Pro-564 peptide. B, dependence on Pro-564 peptide. Experiments were performed in the absence (G) or the presence (Œ) of 10 M CsA. C, dose-response curve for the stimulating action of CsA. Experiments were performed in the presence of 50 M Pro-564 peptide. D, vHL binding. GSTODD (170 g) was incubated for 30 min at 37 °C in the presence of the kidney extract and cofactors. Glutathione-Sepha- rose beads and 50,000 cpm of [35S]vHL were then added. The bound vHL was recovered after 2 h at 4 °C, subjected to 15% SDS-PAGE, and visualized by phosphorimaging. The left lane shows a band from di- rectly loaded [35S]vHL. E, in vivo hydroxylation of ODDGFP. ODDGFP-expressing cells were incubated under normoxia or hypoxia in the presence or absence of 10 M CsA. ODDGFP was immunopre- cipitated by using an anti-GFP <t>monoclonal</t> antibody, resolved by SDS- PAGE, and probed with an anti-vHL (upper panel) or an anti-GFP (lower panel) monoclonal antibodies. Note than in this experiment, the expression of ODDGFP was stabilized under hypoxia and reversed by addition of CsA. Results shown are representative of two other inde- pendent experiments.
Mouse Monoclonal Antibodies, supplied by Novus Biologicals, 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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igd  (SouthernBiotech)
93
SouthernBiotech igd
FIG. 5. CsA activates Pro-564 hydroxylase. A kidney light mito- chondrial fraction was used as a source of enzyme. Activity was defined as the Pro-564 peptide-dependent degradation of 2-OG. The peptide- independent activity was determined in each experiment and was sub- strated from the data. Means S.E. from triplicate measurements are shown. A, 2-OG dependence. Experiments were performed in the pres- ence of 100 M Pro-564 peptide. B, dependence on Pro-564 peptide. Experiments were performed in the absence (G) or the presence (Œ) of 10 M CsA. C, dose-response curve for the stimulating action of CsA. Experiments were performed in the presence of 50 M Pro-564 peptide. D, vHL binding. GSTODD (170 g) was incubated for 30 min at 37 °C in the presence of the kidney extract and cofactors. Glutathione-Sepha- rose beads and 50,000 cpm of [35S]vHL were then added. The bound vHL was recovered after 2 h at 4 °C, subjected to 15% SDS-PAGE, and visualized by phosphorimaging. The left lane shows a band from di- rectly loaded [35S]vHL. E, in vivo hydroxylation of ODDGFP. ODDGFP-expressing cells were incubated under normoxia or hypoxia in the presence or absence of 10 M CsA. ODDGFP was immunopre- cipitated by using an anti-GFP <t>monoclonal</t> antibody, resolved by SDS- PAGE, and probed with an anti-vHL (upper panel) or an anti-GFP (lower panel) monoclonal antibodies. Note than in this experiment, the expression of ODDGFP was stabilized under hypoxia and reversed by addition of CsA. Results shown are representative of two other inde- pendent experiments.
Igd, supplied by SouthernBiotech, 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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igd pe  (SouthernBiotech)
93
SouthernBiotech igd pe
FIG. 5. CsA activates Pro-564 hydroxylase. A kidney light mito- chondrial fraction was used as a source of enzyme. Activity was defined as the Pro-564 peptide-dependent degradation of 2-OG. The peptide- independent activity was determined in each experiment and was sub- strated from the data. Means S.E. from triplicate measurements are shown. A, 2-OG dependence. Experiments were performed in the pres- ence of 100 M Pro-564 peptide. B, dependence on Pro-564 peptide. Experiments were performed in the absence (G) or the presence (Œ) of 10 M CsA. C, dose-response curve for the stimulating action of CsA. Experiments were performed in the presence of 50 M Pro-564 peptide. D, vHL binding. GSTODD (170 g) was incubated for 30 min at 37 °C in the presence of the kidney extract and cofactors. Glutathione-Sepha- rose beads and 50,000 cpm of [35S]vHL were then added. The bound vHL was recovered after 2 h at 4 °C, subjected to 15% SDS-PAGE, and visualized by phosphorimaging. The left lane shows a band from di- rectly loaded [35S]vHL. E, in vivo hydroxylation of ODDGFP. ODDGFP-expressing cells were incubated under normoxia or hypoxia in the presence or absence of 10 M CsA. ODDGFP was immunopre- cipitated by using an anti-GFP <t>monoclonal</t> antibody, resolved by SDS- PAGE, and probed with an anti-vHL (upper panel) or an anti-GFP (lower panel) monoclonal antibodies. Note than in this experiment, the expression of ODDGFP was stabilized under hypoxia and reversed by addition of CsA. Results shown are representative of two other inde- pendent experiments.
Igd Pe, supplied by SouthernBiotech, 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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pe anti mouse igd antibody e ab f1189d  (Elabscience Biotechnology)
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Elabscience Biotechnology pe anti mouse igd antibody e ab f1189d
FIG. 5. CsA activates Pro-564 hydroxylase. A kidney light mito- chondrial fraction was used as a source of enzyme. Activity was defined as the Pro-564 peptide-dependent degradation of 2-OG. The peptide- independent activity was determined in each experiment and was sub- strated from the data. Means S.E. from triplicate measurements are shown. A, 2-OG dependence. Experiments were performed in the pres- ence of 100 M Pro-564 peptide. B, dependence on Pro-564 peptide. Experiments were performed in the absence (G) or the presence (Œ) of 10 M CsA. C, dose-response curve for the stimulating action of CsA. Experiments were performed in the presence of 50 M Pro-564 peptide. D, vHL binding. GSTODD (170 g) was incubated for 30 min at 37 °C in the presence of the kidney extract and cofactors. Glutathione-Sepha- rose beads and 50,000 cpm of [35S]vHL were then added. The bound vHL was recovered after 2 h at 4 °C, subjected to 15% SDS-PAGE, and visualized by phosphorimaging. The left lane shows a band from di- rectly loaded [35S]vHL. E, in vivo hydroxylation of ODDGFP. ODDGFP-expressing cells were incubated under normoxia or hypoxia in the presence or absence of 10 M CsA. ODDGFP was immunopre- cipitated by using an anti-GFP <t>monoclonal</t> antibody, resolved by SDS- PAGE, and probed with an anti-vHL (upper panel) or an anti-GFP (lower panel) monoclonal antibodies. Note than in this experiment, the expression of ODDGFP was stabilized under hypoxia and reversed by addition of CsA. Results shown are representative of two other inde- pendent experiments.
Pe Anti Mouse Igd Antibody E Ab F1189d, supplied by Elabscience 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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igd immunoglobulin  (R&D Systems)
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R&D Systems igd immunoglobulin
FIG. 5. CsA activates Pro-564 hydroxylase. A kidney light mito- chondrial fraction was used as a source of enzyme. Activity was defined as the Pro-564 peptide-dependent degradation of 2-OG. The peptide- independent activity was determined in each experiment and was sub- strated from the data. Means S.E. from triplicate measurements are shown. A, 2-OG dependence. Experiments were performed in the pres- ence of 100 M Pro-564 peptide. B, dependence on Pro-564 peptide. Experiments were performed in the absence (G) or the presence (Œ) of 10 M CsA. C, dose-response curve for the stimulating action of CsA. Experiments were performed in the presence of 50 M Pro-564 peptide. D, vHL binding. GSTODD (170 g) was incubated for 30 min at 37 °C in the presence of the kidney extract and cofactors. Glutathione-Sepha- rose beads and 50,000 cpm of [35S]vHL were then added. The bound vHL was recovered after 2 h at 4 °C, subjected to 15% SDS-PAGE, and visualized by phosphorimaging. The left lane shows a band from di- rectly loaded [35S]vHL. E, in vivo hydroxylation of ODDGFP. ODDGFP-expressing cells were incubated under normoxia or hypoxia in the presence or absence of 10 M CsA. ODDGFP was immunopre- cipitated by using an anti-GFP <t>monoclonal</t> antibody, resolved by SDS- PAGE, and probed with an anti-vHL (upper panel) or an anti-GFP (lower panel) monoclonal antibodies. Note than in this experiment, the expression of ODDGFP was stabilized under hypoxia and reversed by addition of CsA. Results shown are representative of two other inde- pendent experiments.
Igd Immunoglobulin, supplied by R&D Systems, 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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igd  (Novus Biologicals)
94
Novus Biologicals igd
FIG. 5. CsA activates Pro-564 hydroxylase. A kidney light mito- chondrial fraction was used as a source of enzyme. Activity was defined as the Pro-564 peptide-dependent degradation of 2-OG. The peptide- independent activity was determined in each experiment and was sub- strated from the data. Means S.E. from triplicate measurements are shown. A, 2-OG dependence. Experiments were performed in the pres- ence of 100 M Pro-564 peptide. B, dependence on Pro-564 peptide. Experiments were performed in the absence (G) or the presence (Œ) of 10 M CsA. C, dose-response curve for the stimulating action of CsA. Experiments were performed in the presence of 50 M Pro-564 peptide. D, vHL binding. GSTODD (170 g) was incubated for 30 min at 37 °C in the presence of the kidney extract and cofactors. Glutathione-Sepha- rose beads and 50,000 cpm of [35S]vHL were then added. The bound vHL was recovered after 2 h at 4 °C, subjected to 15% SDS-PAGE, and visualized by phosphorimaging. The left lane shows a band from di- rectly loaded [35S]vHL. E, in vivo hydroxylation of ODDGFP. ODDGFP-expressing cells were incubated under normoxia or hypoxia in the presence or absence of 10 M CsA. ODDGFP was immunopre- cipitated by using an anti-GFP <t>monoclonal</t> antibody, resolved by SDS- PAGE, and probed with an anti-vHL (upper panel) or an anti-GFP (lower panel) monoclonal antibodies. Note than in this experiment, the expression of ODDGFP was stabilized under hypoxia and reversed by addition of CsA. Results shown are representative of two other inde- pendent experiments.
Igd, supplied by Novus Biologicals, 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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rat anti mouse igd  (SouthernBiotech)
85
SouthernBiotech rat anti mouse igd
FIG. 5. CsA activates Pro-564 hydroxylase. A kidney light mito- chondrial fraction was used as a source of enzyme. Activity was defined as the Pro-564 peptide-dependent degradation of 2-OG. The peptide- independent activity was determined in each experiment and was sub- strated from the data. Means S.E. from triplicate measurements are shown. A, 2-OG dependence. Experiments were performed in the pres- ence of 100 M Pro-564 peptide. B, dependence on Pro-564 peptide. Experiments were performed in the absence (G) or the presence (Œ) of 10 M CsA. C, dose-response curve for the stimulating action of CsA. Experiments were performed in the presence of 50 M Pro-564 peptide. D, vHL binding. GSTODD (170 g) was incubated for 30 min at 37 °C in the presence of the kidney extract and cofactors. Glutathione-Sepha- rose beads and 50,000 cpm of [35S]vHL were then added. The bound vHL was recovered after 2 h at 4 °C, subjected to 15% SDS-PAGE, and visualized by phosphorimaging. The left lane shows a band from di- rectly loaded [35S]vHL. E, in vivo hydroxylation of ODDGFP. ODDGFP-expressing cells were incubated under normoxia or hypoxia in the presence or absence of 10 M CsA. ODDGFP was immunopre- cipitated by using an anti-GFP <t>monoclonal</t> antibody, resolved by SDS- PAGE, and probed with an anti-vHL (upper panel) or an anti-GFP (lower panel) monoclonal antibodies. Note than in this experiment, the expression of ODDGFP was stabilized under hypoxia and reversed by addition of CsA. Results shown are representative of two other inde- pendent experiments.
Rat Anti Mouse Igd, supplied by SouthernBiotech, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


FIG. 5. CsA activates Pro-564 hydroxylase. A kidney light mito- chondrial fraction was used as a source of enzyme. Activity was defined as the Pro-564 peptide-dependent degradation of 2-OG. The peptide- independent activity was determined in each experiment and was sub- strated from the data. Means S.E. from triplicate measurements are shown. A, 2-OG dependence. Experiments were performed in the pres- ence of 100 M Pro-564 peptide. B, dependence on Pro-564 peptide. Experiments were performed in the absence (G) or the presence (Œ) of 10 M CsA. C, dose-response curve for the stimulating action of CsA. Experiments were performed in the presence of 50 M Pro-564 peptide. D, vHL binding. GSTODD (170 g) was incubated for 30 min at 37 °C in the presence of the kidney extract and cofactors. Glutathione-Sepha- rose beads and 50,000 cpm of [35S]vHL were then added. The bound vHL was recovered after 2 h at 4 °C, subjected to 15% SDS-PAGE, and visualized by phosphorimaging. The left lane shows a band from di- rectly loaded [35S]vHL. E, in vivo hydroxylation of ODDGFP. ODDGFP-expressing cells were incubated under normoxia or hypoxia in the presence or absence of 10 M CsA. ODDGFP was immunopre- cipitated by using an anti-GFP monoclonal antibody, resolved by SDS- PAGE, and probed with an anti-vHL (upper panel) or an anti-GFP (lower panel) monoclonal antibodies. Note than in this experiment, the expression of ODDGFP was stabilized under hypoxia and reversed by addition of CsA. Results shown are representative of two other inde- pendent experiments.

Journal: Journal of Biological Chemistry

Article Title: Cyclosporin A Prevents the Hypoxic Adaptation by Activating Hypoxia-inducible Factor-1α Pro-564 Hydroxylation

doi: 10.1074/jbc.m211293200

Figure Lengend Snippet: FIG. 5. CsA activates Pro-564 hydroxylase. A kidney light mito- chondrial fraction was used as a source of enzyme. Activity was defined as the Pro-564 peptide-dependent degradation of 2-OG. The peptide- independent activity was determined in each experiment and was sub- strated from the data. Means S.E. from triplicate measurements are shown. A, 2-OG dependence. Experiments were performed in the pres- ence of 100 M Pro-564 peptide. B, dependence on Pro-564 peptide. Experiments were performed in the absence (G) or the presence (Œ) of 10 M CsA. C, dose-response curve for the stimulating action of CsA. Experiments were performed in the presence of 50 M Pro-564 peptide. D, vHL binding. GSTODD (170 g) was incubated for 30 min at 37 °C in the presence of the kidney extract and cofactors. Glutathione-Sepha- rose beads and 50,000 cpm of [35S]vHL were then added. The bound vHL was recovered after 2 h at 4 °C, subjected to 15% SDS-PAGE, and visualized by phosphorimaging. The left lane shows a band from di- rectly loaded [35S]vHL. E, in vivo hydroxylation of ODDGFP. ODDGFP-expressing cells were incubated under normoxia or hypoxia in the presence or absence of 10 M CsA. ODDGFP was immunopre- cipitated by using an anti-GFP monoclonal antibody, resolved by SDS- PAGE, and probed with an anti-vHL (upper panel) or an anti-GFP (lower panel) monoclonal antibodies. Note than in this experiment, the expression of ODDGFP was stabilized under hypoxia and reversed by addition of CsA. Results shown are representative of two other inde- pendent experiments.

Article Snippet: Mouse monoclonal antibodies were obtained from the following sources: HIF-1 (Novus Biologicals), GFP (Roche Molecular Biochemicals), -tubulin (Sigma), vHL (Pharmingen).

Techniques: Activity Assay, Binding Assay, Incubation, SDS Page, In Vivo, Expressing, Bioprocessing