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Anti gfp mab

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Anti-GFP mAb is a monoclonal antibody that specifically binds to the green fluorescent protein (GFP). This antibody can be used to detect and visualize GFP-tagged proteins in various experimental applications.

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Lab products found in correlation

Gfp trap, by Proteintech (1 mentions) Anti tubulin, by Merck Group (1 mentions) Anti v5 mab, by Thermo Fisher Scientific (1 mentions) Protease inhibitor cocktail, by Merck Group (1 mentions) Anti ea d, by Merck Group (1 mentions) Secondary peroxidase conjugated goat anti mouse antibody, by Cell Signaling Technology (1 mentions)

Close spelling variants of this product

Anti-GFP (254 citations) Mouse anti-GFP mAb (5 citations) GFP mAb (4 citations)

5 protocols using anti gfp mab

1

Immunoprecipitation and Immunoblotting Protocol

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Cells were lysed in PBS that contained 1% Triton X-100 and protease inhibitor cocktail (Sigma). Lysates were then cleared by centrifugation at 12,000 g at 4°C for 15 min. For immunoprecipitation, a specific antibody or GFP-Trap (ChromoTek) was added, and the mixture was incubated at 4°C for 1 h. Protein-A/G agarose beads (Upstate biotechnology) were added to capture the antigen-antibody complex. After washing with PBS that contained 1% Triton X-100, proteins that were bound to the beads were eluted by adding 2X electrophoresis sample buffer and analyzed by immunoblotting. For endogenous BGLF2 immunoblotting, cells were lysed in sample buffer that contained DTT. The primary antibodies were as follows: anti-Rta and anti-Zta (Argene), anti-EA-D, anti-gp110 and gp350 (Millipore), anti-Tubulin (Sigma), anti-GFP mAb (Roche), rabbit anti-V5 (Santa Cruz), anti-V5 mAb (Invitrogen), rabbit anti-V5 (GeneTex), anti p-ERK, ERK, p-p38, p38, p-JNK, JNK (Cell signaling), and rabbit anti-BGLF2 antibodies. Rabbit anti-BGLF2 antibody was produced using the synthesized peptide 21LWVLSDASTPQMKV34-cys (AngeneBiotech, Taiwan).
Hung C.H., Chiu Y.F., Wang W.H., Chen L.W., Chang P.J., Huang T.Y., Lin Y.J., Tsai W.J, & Yang C.C. (2020). Interaction Between BGLF2 and BBLF1 Is Required for the Efficient Production of Infectious Epstein–Barr Virus Particles. Frontiers in Microbiology, 10, 3021.
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2

Immunoblotting with PVDF Membranes

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Polyvinylidene difluoride (PVDF) membranes were blocked in 5% milk 0.1% Tween-20 Tris buffered saline (TBSMT), incubated with 0.2 μg/mL anti-GFP mAb (Roche, Branchburg, NJ, USA) in TBSMT followed by 1:20,000 diluted polyclonal sheep anti-mouse IgG horseradish peroxidase (HRP)-coupled antibodies (GE, Pittsburgh, PA, USA) in TBSMT and developed with SuperSignal West Femto Substrate (Pierce, Rockford, IL, USA).
, & Cavallari M. (2017). Rapid and Direct VHH and Target Identification by Staphylococcal Surface Display Libraries. International Journal of Molecular Sciences, 18(7), 1507.
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3

Purification of TIM-1-YFP Extracellular Vesicles

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Extracellular vesicles were prepared by differential centrifugation of cell cultures of TIM-1-YFP-transfected 300.19 cells (2 × 107), in media depleted of exosomes by ultracentrifugation (100,000 g, 3 h). At 24 h post-transfection, cell cultures were harvested and cells sedimented (750 g, 15 min). Dead cells and debris were removed from supernatants by centrifugation (10,000 g, 45 min). Supernatants were filtered through 0.22 μm membranes, then extracellular vesicles and exosomes were pelleted by ultracentrifugation (100,000 g, 2 h). Cells and exosomes were resuspended in lysis buffer (20 mM Tris pH 8, 150 mM NaCl, 1% NP40, 10% glicerol and protease inhibitors), and TIM-1-YFP in samples was identified in Western blot with an anti-GFP mAb (Roche).
Echbarthi M., Zonca M., Mellwig R., Schwab Y., Kaplan G., DeKruyff R.H., Roda-Navarro P, & Casasnovas J.M. (2015). Distinct trafficking of cell surface and endosomal TIM-1 to the immune synapse. Traffic (Copenhagen, Denmark), 16(11), 1193-1207.
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4

Protein Detection Techniques for PVX and GFP

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Extraction of total soluble proteins, SDS-PAGE, and Western blot analysis were performed as described [31 (link)]. For detection of PVX, proteins were extracted from systemically infected leaves of N. benthamiana plants infected with PVX or PVX recombinant constructs. The anti-CP monoclonal antibody (MAb) raised against PVX (raised in our lab, Institute of Biotechnology, Zhejiang Univiersity, Hangzhou, China) was used at a 1:8000 dilution. For detection of GFP, proteins were extracted from infiltrated patches of N. benthamiana line 16c or N. benthamiana plants. The anti-GFP MAb (Roche) was used at a 1:8000 dilution. Western blots were visualised with a secondary peroxidase-conjugated goat antimouse antibody (Cell Signaling Technology, Boston, MA, USA) and a chemiluminescence detection system (Tianneng, Shanghai, China).
Yang X., Ren Y., Sun S., Wang D., Zhang F., Li D., Li S, & Zhou X. (2018). Identification of the Potential Virulence Factors and RNA Silencing Suppressors of Mulberry Mosaic Dwarf-Associated Geminivirus. Viruses, 10(9), 472.
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5

Purification and Immunolabeling of Trophozoite Parasites

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Trophozoite stage parasites were harvested by magnetic purification and fixed in either 2.5% glutaraldehyde, or in paraformaldehyde/glutaraldehyde (2%/0.0075%) for immuno-EM. Labelling was performed by permeabilizing with ~40 μg ml−1 Equinatoxin II for 6 min, washing and fixing again with 2% paraformaldehyde. Cells were then washed and incubated with anti-GFP (mAb, Roche; 1:50) in 3% BSA in PBS, washed and incubated with gold-labelled protein A (6 nm Aurion). Cells were embedded in agarose, fixed in 2% OsO4 for 1 h, washed twice in H2O and dehydrated in an ethanol series, then acetone, and then infiltrated with Procure epoxy resin for 2 × 12 h at 60°C. Resin was polymerized with BDMA for at least 48 h at 60°C before thin and thick (100 nm and 600 nm) sections were cut. Sections were placed on 100 h copper grids, stained with uranyl acetate and lead citrate and observed on either a Tecnai Spirit (thin sections) or Tecnai F30 (STEM).
McHugh E., Batinovic S., Hanssen E., McMillan P.J., Kenny S., Griffin M.D., Crawford S., Trenholme K.R., Gardiner D.L., Dixon M.W, & Tilley L. (2015). A repeat sequence domain of the ring-exported protein-1 of Plasmodium falciparum controls export machinery architecture and virulence protein trafficking. Molecular microbiology, 98(6), 1101-1114.
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