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Gp91phox antibody

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The Gp91phox antibody is a laboratory reagent used in research applications. It is a tool for the detection and analysis of the Gp91phox protein, which is a subunit of the NADPH oxidase complex. The antibody can be used in techniques such as Western blotting, immunohistochemistry, and flow cytometry to study the expression and localization of Gp91phox in biological samples.

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Lab products found in correlation

Phospho p47phox antibody, by Merck Group (4 mentions) P47phox antibody, by Merck Group (2 mentions) Ab152, by Merck Group (1 mentions) 4 hydroxynonenal 4 hne, by Abcam (1 mentions) Mab318, by Merck Group (1 mentions) Biotinylated secondary antibody, by Thermo Fisher Scientific (1 mentions) Agarose, by Merck Group (1 mentions) Dab reagent, by Vector Laboratories (1 mentions) Klenow dna polymerase, by New England Biolabs (1 mentions) Anti β tubulin monoclonal antibody, by Merck Group (1 mentions) Deoxynucleoside triphosphates dntps, by New England Biolabs (1 mentions) Precisionplus 2x qpcr mastermix with sybr green, by Primerdesign (1 mentions) Taq polymerase, by New England Biolabs (1 mentions) High capacity cdna reverse transcription kit, by Thermo Fisher Scientific (1 mentions) Phenyl methyl sulfonyl fluoride (pmsf), by Merck Group (1 mentions) Aprotinin, by Merck Group (1 mentions) Leupeptin, by Merck Group (1 mentions) Restriction enzyme, by New England Biolabs (1 mentions)

Spelling variants of this product

Gp91phox (18 citations) Mouse anti-mouse gp91phox monoclonal antibody (2 citations) Anti-gp91phox antibody (2 citations)

4 protocols using gp91phox antibody

1

Phosphorylation and Association of p47phox

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Immunoprecipitation and western blot analysis were performed as previously described (Sayeski et al., 1998 (link)). To determine phosphorylation of p47phox, protein sample was extracted from the homogenates of isolated DCs and immunoprecipitated using p47phox antibody (Millipore) followed by western blotting using phospho-p47phox antibody (Sigma). To investigate association of p47phox with gp91phox, protein lysates from DCs were immunoprecipitated using the gp91phox antibody (Becton Dickinson) followed by western blotting using phospho-p47phox antibody (Millipore).
Barbaro N.R., Foss J.D., Kryshtal D.O., Tsyba N., Kumaresan S., Xiao L., Mernaugh R.L., Itani H.A., Loperena R., Chen W., Dikalov S., Titze J.M., Knollmann B.C., Harrison D.G, & Kirabo A. (2017). Dendritic Cell Amiloride-Sensitive Channels Mediate Sodium-Induced Inflammation and Hypertension. Cell reports, 21(4), 1009-1020.
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2

Phosphorylation and Association of p47phox

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Immunoprecipitation and western blot analysis were performed as previously described (Sayeski et al., 1998 (link)). To determine phosphorylation of p47phox, protein sample was extracted from the homogenates of isolated DCs and immunoprecipitated using p47phox antibody (Millipore) followed by western blotting using phospho-p47phox antibody (Sigma). To investigate association of p47phox with gp91phox, protein lysates from DCs were immunoprecipitated using the gp91phox antibody (Becton Dickinson) followed by western blotting using phospho-p47phox antibody (Millipore).
Barbaro N.R., Foss J.D., Kryshtal D.O., Tsyba N., Kumaresan S., Xiao L., Mernaugh R.L., Itani H.A., Loperena R., Chen W., Dikalov S., Titze J.M., Knollmann B.C., Harrison D.G, & Kirabo A. (2017). Dendritic Cell Amiloride-Sensitive Channels Mediate Sodium-Induced Inflammation and Hypertension. Cell reports, 21(4), 1009-1020.
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3

Oxidative Stress Immunohistochemistry Protocol

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The free-floating sections were immune-blocked with 4% goat serum in 0.25% triton/PBS for 2 hours and then incubated with 3-Nitrotyrosine (3-NT, mouse, 1:200, Abcam, Cambridge, MA), 4-Hydroxynonenal (4-HNE, rabbit, 1:200, Abcam, Cambridge, MA) or gp91phox antibody (mouse, 1:500, BD Biosciences, 611414) antibodies overnight at 4 °C. On the second day, the sections were washed with 1% BSA in 0.25% triton/PBS before incubation with polyclonal rabbit anti-TH antibody (mouse: MAB318, 1:2000; rabbit: AB152, 1:2000; EMD Millipore, Temecula, CA) overnight at 4 °C. The double-label immunofluorescence pictures were taken under the confocal microscope using Alexa-488 (green) and Alexa-594 (red) conjugated secondary antibodies (1:1,000) to visualize the double TH and 3-NT, 4-HNE or gp91phox-positive neurons. Densitometry was performed using ImageJ.
Song S., Wang Q., Jiang L., Oyarzabal E., Riddick N.V., Wilson B., Moy S.S., Shih Y.Y, & Hong J.S. (2019). Noradrenergic dysfunction accelerates LPS-elicited inflammation-related ascending sequential neurodegeneration and deficits in non-motor/motor functions. Brain, behavior, and immunity, 81, 374-387.
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4

Western Blot and qRT-PCR Analysis

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PMSF, leupeptin, aprotinin, agarose, monoclonal anti-β-tubulin antibodies, horseradish-peroxidase-coupled, and anti-mouse IgG were purchased from Sigma, Deisenhofen, Germany. Restriction enzymes, Taq polymerase, Klenow DNA polymerase, and deoxynucleoside triphosphates (dNTPs) were purchased from New England Biolabs, Frankfurt, Germany. All oligonucleotides were from Sigma, Deisenhofen, Germany. The High-Capacity cDNA Reverse Transcription Kit was purchased from Applied Biosystems, Darmstadt, Germany. The PrecisionPLUS 2x qPCR MasterMix with SYBR green was obtained from Primer Design, Chandler’s Ford, United Kingdom. Primer-Probe-Mixes of murine NADPH oxidase (NOX-2 Mm00432775_m1) and murine TATA box binding protein (TBP, Mm_00446973_m1) were purchased from Applied Biosystems, Foster City, CA, USA. The mouse monoclonal gp91phox antibody was obtained from BD Biosciences, USA. The secondary antibody peroxidase-labeled goat-anti-mouse (GAM-POX), avidin-biotin complex (ABC) reagent, and DAB reagent (used for IHC) were from Vector Laboratories, CA, USA. The polyclonal NOX-2 antibody used for immunohistochemistry was obtained from LSBio, Seattle, WA, USA. The biotinylated secondary antibody was from Thermo Fisher Scientific, Waltham, MA, USA. The Bradford reagent mix for determination of protein concentration was obtained from BioRad, Munich, Germany.
Göllner M., Ihrig-Biedert I., Petermann V., Saurin S., Oelze M., Kröller-Schön S., Vujacic-Mirski K., Kuntic M., Pautz A., Daiber A, & Kleinert H. (2020). NOX2ko Mice Show Largely Increased Expression of a Mutated NOX2 mRNA Encoding an Inactive NOX2 Protein. Antioxidants, 9(11), 1043.
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