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Rabbit anti gfp antibody

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Rabbit anti-GFP antibody is a primary antibody that specifically binds to the Green Fluorescent Protein (GFP). It is designed for detection and quantification of GFP-tagged proteins in various applications such as Western blotting, immunoprecipitation, and immunocytochemistry.

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Lab products found in correlation

Rat anti ha antibody, by Roche (2 mentions) Anti rabbit secondary antibody, by Jackson ImmunoResearch (2 mentions) Alexa fluor 488 goat anti rabbit igg, by Thermo Fisher Scientific (2 mentions) Alexa fluor 647 goat anti rat igg, by Thermo Fisher Scientific (2 mentions) Rat anti elav antibody, by Developmental Studies Hybridoma Bank (2 mentions) Goat anti mouse igg alexa fluor plus 555, by Thermo Fisher Scientific (2 mentions) Lsm 780 multiphoton laser scanning confocal microscope, by Zeiss (2 mentions) Mouse anti ha antibody ha 11, by Fortrea (2 mentions) Dynabeads protein a, by Thermo Fisher Scientific (2 mentions) Sds page gel, by Bio-Rad (2 mentions) Imagequant las 4000 biomolecular imager, by GE Healthcare (2 mentions) Hq silver, by Nanoprobes (1 mentions) Goat anti rabbit igg, by Nanoprobes (1 mentions) Rabbit polyclonal antibodies, by Thermo Fisher Scientific (1 mentions) Axioplan 2 microscope, by Leica (1 mentions) Alkaline phosphatase kit, by Promega (1 mentions) Mouse anti myc antibody, by Santa Cruz Biotechnology (1 mentions) Goat anti rat hrp, by Merck Group (1 mentions) Triton x 100, by Thermo Fisher Scientific (1 mentions) Supersignal west dura kit, by Thermo Fisher Scientific (1 mentions)

Close spelling variants of this product

Anti-GFP (367 citations) Anti-GFP antibody (174 citations) Rabbit anti-GFP (173 citations) GFP antibody (48 citations) Rabbit anti-GFP polyclonal antibody (18 citations) Rabbit anti- (5 citations) Rabbit monoclonal anti-GFP antibody (4 citations) Rabbit anti-GFP primary antibody (3 citations) Rabbit anti-GFP antibody ab290 (2 citations) Rabbit anti-GFP polyclonal antibody-Chip Grade (ab290) (2 citations)

36 protocols using rabbit anti gfp antibody

1

Nuclear and Cytoplasmic Protein Extraction from N. benthamiana

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A plant nuclear and cytoplasmic protein extraction kit (BestBio) was used to extract nuclear and cytoplasmic fractions from N. benthamiana leaves expressing OsWRKY19‐GFP or OsRLR1‐GFP, following the protocol provided by the manufacturer. The rabbit anti‐GFP antibodies (Abcam) and anti‐Rabbit IgG light‐chain antibodies (Abcam) were used to detect the fusion proteins by Western blot.
Du D., Zhang C., Xing Y., Lu X., Cai L., Yun H., Zhang Q., Zhang Y., Chen X., Liu M., Sang X., Ling Y., Yang Z., Li Y., Lefebvre B, & He G. (2021). The CC‐NB‐LRR OsRLR1 mediates rice disease resistance through interaction with OsWRKY19. Plant Biotechnology Journal, 19(5), 1052-1064.
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2

Ultrastructural Analysis of Plant Root Tips

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For ultrastructural analysis, root tips were high-pressure frozen (Bal-Tec HPM010; Balzers) in hexadecene (Merck Sharp and Dohme, Haar, Germany), freeze-substituted in acetone containing 2.5% osmium tetroxide, washed at 0°C with acetone, and embedded in Epon. For immunogold labeling of ultrathin thawed cryosections, root tips were fixed with 8% formaldehyde (2 hr), embedded in gelatin, and infiltrated with 2.1 M sucrose in PBS as previously described (Dettmer et al., 2006 (link)). Thawed ultrathin sections were labeled with rabbit anti-GFP antibodies (1:300; Abcam) and silver-enhanced (HQ Silver, 8 min; Nanoprobes, Yaphank, NY, USA) goat anti-rabbit IgG coupled to Nanogold (no. 2004; Nanoprobes). Antibodies and markers were diluted in blocking buffer (PBS supplemented with 0.5% BSA and 1% milk powder).
Richter S., Kientz M., Brumm S., Nielsen M.E., Park M., Gavidia R., Krause C., Voss U., Beckmann H., Mayer U., Stierhof Y.D, & Jürgens G. (2014). Delivery of endocytosed proteins to the cell–division plane requires change of pathway from recycling to secretion. eLife, 3, e02131.
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3

Immunofluorescence and Immunoblot Analyses of Connexins

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Cx40 was detected using rabbit polyclonal antibodies (Invitrogen). For double-labeling experiments, cells were incubated simultaneously with both mouse anti-mCherry monoclonal and rabbit anti-GFP antibodies (Abcam). Immunoblots were performed as described earlier [10 (link)] using cell homogenates prepared 48 h after transfection with connexin DNA as described by Gong et al. [11 (link)]. For immunofluorescence microscopy, cultured cells were fixed in methanol/acetone (1:1), stained as previously described [8 (link)], and imaged using a Zeiss Axioplan 2 microscope or Leica TCS SP2 laser-scanning confocal microscope.
Patel D., Gemel J., Xu Q., Simon A.R., Lin X., Matiukas A., Beyer E.C, & Veenstra R.D. (2014). Atrial fibrillation-associated Connexin40 mutants make hemichannels and synergistically form gap junction channels with novel properties. FEBS letters, 588(8), 1458-1464.
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4

Western Blot Detection of Parasite Proteins

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To detect HA3-TgArk1 or DD-Myc-TgArk1WT or DD- Myc-TgArk1D/A or SAG1, GFP or TgINCENP1-GFP or TgIN-CENP1-HA3 or TgINCENP1i-HA3 or Myc-TgIN- CENP2 proteins, parasite lysates or eluted proteins were fractionated on 12 and 10% acrylamide gels, respectively, prior to detection. Separated proteins were transferred to nitrocellulose membranes and probed with appropriate antibodies in 5% non-fat milk powder in TNT buffer (50 mM Tris pH 8.0; 150 mM NaCl; 0.05% Tween20). The primary antibodies used for detection and their respective dilutions were: rat anti-HA antibodies (Roche) at 1/300, mouse anti-Myc antibodies (SANTA CRUZ BIOTECHNOLOGY) at 1/100, rabbit polyclonal anti-TgSAG1 at 1/1000 [36 (link)], rabbit anti-GFP antibodies (abcam) at 1/1000. Bound secondary conjugated antibodies were visualized using either the ECL system (Amersham Corp) or using alkaline phosphatase kit according to manufacturer’s instructions (Promega).
Berry L., Chen C.T., Francia M.E., Guerin A., Graindorge A., Saliou J.M., Grandmougin M., Wein S., Bechara C., Morlon-Guyot J., Bordat Y., Gubbels M.J., Lebrun M., Dubremetz J.F, & Daher W. (2018). Toxoplasma gondii chromosomal passenger complex is essential for the organization of a functional mitotic spindle: a prerequisite for productive endodyogeny. Cellular and molecular life sciences : CMLS, 75(23), 4417-4443.
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5

Western Blotting of Malaria Proteins

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Western Blotting was performed according to standard methods. Briefly, Rex2.GFP or FIKK10.1.HA-expressing parasites were released from erythrocytes by addition of 0.1% (w/v) saponin/PBS for 5 min at room temperature. 0.1% saponin lysates were centrifuged (>15000 × G) and the resulting parasite pellet was solubilized with 1X sample buffer with 5% beta-mercaptoethanol at a concentration of 2.5–5 × 108 parasites/ml. Parasite extracts were subjected to SDS PAGE and transferred onto nitrocellulose membranes. Rex2.GFP was visualized by probing the blots with rabbit anti-GFP antibodies (Abcam (1:500)) and goat anti-rabbit-HRP (Insight Biotechnology (1:4000)). FIKK10.1.HA was visualised using rat anti-HA hi affinity (Roche (1:500)) and goat anti-rat-HRP (1:4000 (Sigma)). For detection of MSP1, schizonts were Percoll-enriched according to standard methods then solubilized by addition of SDS sample buffer, subjected to SDS PAGE, and proteins transferred to nitrocellulose membranes. MSP1 was visualized by probing blots with anti-MSP1 mAb X509 or mAB 89.120 (link) (undiluted hybridoma culture supernatant) and a goat anti-human-HRP secondary antibody (Sigma). SERA5 was visualized using polyclonal rabbit anti-SERA5 serum.
Jones M.L., Das S., Belda H., Collins C.R., Blackman M.J, & Treeck M. (2016). A versatile strategy for rapid conditional genome engineering using loxP sites in a small synthetic intron in Plasmodium falciparum. Scientific Reports, 6, 21800.
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6

Hippocampal GFP Expression Visualization

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The injection sites were confirmed in all animals. One hr after behavioral testing, rats were given an overdose of pentobarbital and perfused transcardially with 0.9% saline, followed by cold 4% paraformaldehyde. The brains were extracted, postfixed overnight in 4% paraformaldehyde and stored in 20% glycerol solution. Coronal sections (45 μm) through the hippocampus were taken on a microtome and stored in 0.1 M sodium phosphate buffer with 0.05% sodium azide. Sections were processed to examine the targeting of GFP expression within the hippocampus as previously described (Warren et al., 2011 (link)). Hippocampal free-floating coronal sections were processed for immunohistochemistry using a rabbit anti-GFP antibody (1:1000; Abcam, Cambridge, Massachusetts). Adjacent sections were blocked in 3% normal donkey serum (NDS) and incubated overnight in the primary antibody mentioned above, along with 0.3% Triton X-100 (Fisher Scientific, Pittsburgh, Pennsylvania) and 1% NDS. Sections were incubated with anti-rabbit secondary antibody (1:1000; Jackson ImmunoResearch, West Grove, Pennsylvania) for 2 hr at room temperature. Stained sections were then slide mounted (Fisher Scientific), dehydrated in ethanol and Citrosolv, and coverslipped with clear DPX adhesive (Sigma, St. Louis, Missouri). Slides were visualized and photographed using a fluorescence microscope and a digital camera.
Iñiguez S.D., Parise L.F., Lobo M.K., Flores-Ramirez F.J., Garcia-Carachure I., Warren B.L, & Robison A.J. (2019). Upregulation of hippocampal extracellular signal-regulated kinase (ERK)-2 induces antidepressant-like behavior in the rat forced swim test. Behavioral neuroscience, 133(2), 225-231.
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7

Western Blot Analysis of GFP Protein

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Animals were lethally anesthetized and transcardially perfused with 0.1 M PBS. Tissues were immediately frozen in liquid nitrogen and stored at −80°C until use. For protein extraction, tissues were grinded in a lysis buffer (150 mM NaCl, 50 mM Tris–HCl, 0.5% sodium deoxycholate, 1% NP40, 1% SDS) supplied with protease inhibitors cocktail (Complete Mini, Roche Diagnostics). Lysates were quantified with the DC protein assay (BioRad,) and 50 μg were loaded on a 10% polyacrylamide gel (Criterion XT 10% bis-Tris, Biorad). Proteins were transferred onto a PVDF membrane (Imobilon P, Millipore). Successively, membranes were blocked with a Tris-buffered saline solution (10 mM Tris–HCl pH 7.4, 150 mM NaCl) and 0.05% Tween 20 (TBS-T) containing 5% fat-free dry milk. Membranes were incubated overnight at 4°C with a rabbit anti-GFP antibody (1:10,000; Abcam) or a mouse anti-α-tubulin antibody (1:10,000; Sigma-Aldrich) diluted in TBS-T, 5% fat-free dry milk. After washes in TBS-T buffer, membranes were incubated with horseradish peroxidase conjugated anti-mouse or anti-rabbit secondary antibodies (1:10,000, Amersham Pharmacia Biotech) for 1 h at room temperature. Western blots were developed using SuperSignal West Dura kit (Thermoscientific).
Tanguy Y., Biferi M.G., Besse A., Astord S., Cohen-Tannoudji M., Marais T, & Barkats M. (2015). Systemic AAVrh10 provides higher transgene expression than AAV9 in the brain and the spinal cord of neonatal mice. Frontiers in Molecular Neuroscience, 8, 36.
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8

Quantitative Protein Analysis by Western Blot

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Western blot was done to study protein levels in whole-cell protein samples or nuclear fractions. Protein samples were loaded onto a SDS polyacrylamide gel. Polyvinylidene difluoride membrane was used for the Western blot as described earlier (Laskar et al., 2011 (link)). The primary antibodies used were mouse anti-Act1 antibody (Abcam), rabbit anti-Rad51 (Abcam), mouse anti-Hsp82 antibody (Calbiochem), rabbit anti-Aha1 antibody (Invitrogen), mouse Anti-DDDDK tag antibody (Abcam), and rabbit anti-GFP antibody (Abcam) at 1:5000 dilutions. For subcellular fractionation, we used mouse anti-Nsp1 antibody (Abcam) as loading control at 1:5000 dilution. For secondary antibodies, horseradish peroxide–conjugated anti-rabbit antibody (Promega) and anti-mouse antibody (Promega) were used at 1:10,000 dilution. The Western blots were developed using chemiluminescent detection system (Thermo Fisher Scientific). Every experiment was repeated at least three times and band intensities were quantified by using ImageJ software. Mean relative densities were plotted using GraphPad Prism.
Fangaria N., Rani K., Singh P., Dey S., Kumar K.A, & Bhattacharyya S. (2022). DNA damage-induced nuclear import of HSP90α is promoted by Aha1. Molecular Biology of the Cell, 33(14), ar140.
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9

GFP Immunohistochemical Detection

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Following ISH, sections were further processed to reveal GFP immunoreactivity as described previously (Huang et al., 2008 (link)). The sections were incubated at RT overnight with rabbit anti-GFP antibody (1:1,000; Abcam) and further incubated in PBS-XCD at RT for 3 h with biotinylated anti-rabbit antibody (1:200; Merckmillipore). The sections were then incubated at RT for 3 h with avidin-biotinylated peroxidase complex (ABC-Elite kit, Vector, United States), which was diluted at 1:50 with 0.05 M PBS containing 0.3% (v/v) Triton X-100 (PBS-X). Finally, the bound peroxidase was developed by reaction with 0.02% (w/v) diaminobenzidine-4HCl (DAB) and 0.001% (v/v) H2O2 in 50 mM Tris-HCl (pH 7.6). The sections were mounted onto gelatin-coated glass slides, washed in water, dried, cleared in xylene, and cover-slipped.
Zhang M.M., Feng Y.P., Qiu X.T., Chen T., Bai Y., Feng J.M., Wang J.D., Chen Y., Zhang M.Z., Duan H.K., Zhao M., Teng Y.H., Cao J., Zang W.D., Yang K, & Li Y.Q. (2021). Neurotensin Attenuates Nociception by Facilitating Inhibitory Synaptic Transmission in the Mouse Spinal Cord. Frontiers in Neural Circuits, 15, 775215.
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10

Immunostaining of Drosophila Brains

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Fly brains were dissected from 3-to-5-day-old adult females and stained exactly as in Wu and Luo (2006) (link). The following primary antibodies were used: mouse anti-HA antibody (HA.11, Covance, BioLegend: 901514) and rabbit anti-GFP antibody (Abcam: ab290) were used at 1:500, and rat anti-Elav antibody (Developmental Studies Hybridoma Bank, Iowa City, IA, deposited by G. M. Ruben: 7E8A10) was used at 1:25. Cross absorbed secondary antibodies used were: goat anti-mouse IgG Alexa Fluor Plus 555 (Invitrogen: A32727), goat anti-rabbit IgG Alexa Fluor 488 (Invitrogen: A11034), and goat anti-rat IgG Alexa Fluor 647 (Invitrogen: A21247). Brains were imaged on an Inverted Zeiss LSM 780 Multiphoton Laser Scanning Confocal Microscope with a 20X objective.
Sapiro A.L., Freund E.C., Restrepo L., Qiao H.H., Bhate A., Li Q., Ni J.Q., Mosca T.J, & Li J.B. (2020). Zinc Finger RNA-Binding Protein Zn72D Regulates ADAR-Mediated RNA Editing in Neurons. Cell reports, 31(7), 107654.
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