Rabbit anti mcherry

Manufactured by Rockland Immunochemicals

Rabbit anti-mCherry is a laboratory reagent used for the detection and identification of the mCherry fluorescent protein in biological samples. It is a polyclonal antibody raised in rabbits against the mCherry protein. The antibody can be used in various immunoassay techniques, such as Western blotting, immunohistochemistry, and flow cytometry, to specifically recognize and bind to the mCherry protein.

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5 protocols using rabbit anti mcherry

Fluorescent Immunohistochemistry and Cytochemistry

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Fluorescent immunohistochemistry and immunocytochemistry were performed following fixation in 4% paraformaldehyde and blocking in 10% goat serum, as described (Williams et al., 2014 (link)). The following primary antibodies: rabbit anti-mCherry (Rockland, 600–401-P16), chicken anti-MAP2 (Abcam, ab5392), rat anti GFAP (ThermoFisher, 13–0300), rabbit anti-RIPK3 (Genentech), rat anti-phospho RIPK3 (Genentech), rabbit anti-IRF1 (Cell Signaling Technology, 8478S), rabbit anti-RelA (Abcam, ab16502). Secondary detection was performed with the following antibodies: goat anti-rabbit 594 (ThermoFisher, A-11012), goat anti-chicken 488 (ThermoFisher, A-11039), goat anti-rabbit 488 (Abcam, ab150077), goat anti-rat 594 (Abcam ab150160). Nuclei were visualized via staining with DAPI (ThermoFisher). Images were analyzed with ImageJ software.

Daniels B.P., Kofman S.B., Smith J.R., Norris G.T., Snyder A.G., Kolb J.P., Gao X., Locasale J.W., Martinez J., Gale M J.r., Loo Y.M, & Oberst A. (2019). The nucleotide sensor ZBP1 and kinase RIPK3 induce the enzyme IRG1 to promote an antiviral metabolic state in neurons. Immunity, 50(1), 64-76.e4.

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Labella Immunostaining in Drosophila

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Labella from 5- to 7-day-old male flies were dissected and drilled using a pin in a buffer solution (1x PBS and 0.2% Triton X-100). Tissues were incubated in fixation buffer (PFA 4%, 1X PBS, and 1% Triton X-100) for 45 min, agitated at room temperature (RT) and washed (1x PBS and 1% Triton X-100) for 15 min. In toto, labella were transferred through blocking buffer (0.5% blocking reagent, 0.15 M NaCl, and 0.1 M Tris HCl at pH 7.5) for 45 min under agitation at RT. The whole-mount fly labella was first incubated in goat anti-GFP (1:500, Rockland) and rabbit anti-mCherry (1:1000, Rockland) primary antibodies for 48 hours at 4 °C and washed 5 times for 15 min with 1x PBS and 0.2% Triton. Thereafter, tissues were incubated overnight in anti-goat-Alexa 488 (1:400 antibody, Molecular probes) and anti-rabbit-Alexa 594 (1:400 antibody, Molecular probes) secondary antibodies in the dark at 4 °C. Tissues were then washed with 1x PBS and 0.2% Triton five times for 15 min and were mounted with Vectashield H-1200 in DAPI medium. The labeling was visualized with a Leica sp8 confocal microscope and analyzed using ImageJ software (Software, NIH, Bethesda, MD, USA).

Rihani K., Fraichard S., Chauvel I., Poirier N., Delompré T., Neiers F., Tanimura T., Ferveur J.F, & Briand L. (2019). A conserved odorant binding protein is required for essential amino acid detection in Drosophila. Communications Biology, 2, 425.

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Quantifying DILP2 Release in Crop-Distended Flies

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Immunostaining was conducted according to previous protocol (Hu et al., 2019 (link)). The following antibodies were used: rabbit anti-GFP (1: 1000, Invitrogen), rabbit anti-mcherry (1:1000, Rockland) and mouse anti-nc82 (1:500, Developmental Studies Hybridoma Bank). Secondary antibodies were Alexa Fluor 555 goat anti-rabbit IgG (1: 500, Invitrogen), Alexa Fluor 488 goat anti-rabbit IgG (1: 500, Invitrogen), Alexa Fluor 647 goat anti-mouse IgG (1: 500, Invitrogen), Rabbit anti-DILP2 (gift from Yan Li at the Institute of Biophysics, China) and Alexa 555-Phalloidin (1:200, Solarbio). Images were acquired with a Zeiss LSM 780, Olympus FV1000 or Andor Dragonfly with 2 μm optical sections at a resolution of 1024 × 1024 pixels or 2048 × 2048 pixels.
To test whether fast mechanical distention of the crop triggers DILP2 release from the IPC, the DILP2 protein was quantified by antibody immunostaining against DILP2. The flies were desiccation for 4h. Each fly was manually fed with water until it stopped drinking. The fly was frozen on ice immediately after it stopped drinking. Control flies were frozen on ice without water feeding. The brains were then dissected out in PBS for DILP2 staining (1:1000). The samples were processed in parallel and using the same solution and imaged with the same laser power and scanning settings.

Wang P., Jia Y., Liu T., Jan Y.N, & Zhang W. (2020). Visceral Mechano-sensing Neurons Control Drosophila Feeding by Using Piezo as a Sensor. Neuron, 108(4), 640-650.e4.

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Immunocytochemistry for mCherry and MAP2

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Fluorescent immunocytochemistry was performed following fixation of cells in 4% paraformaldehyde for 10 minutes, followed by blocking with 10% goat serum for 15 minutes. Cells were probed with primary antibodies, including rabbit anti-mCherry (Rockland, 600–401-P16) and chicken anti-MAP2 (Abcam, ab5392), for 1 hour at room temperature. For secondary detection, goat anti-rabbit 594 (ThermoFisher, A-11012) and goat anti-chicken 488 (ThermoFisher, A-11039) antibodies were applied for 15 minutes at room temperature. Nuclei were stained with DAPI. Cells were gently washed with 1X PBS between each step to remove unbound antibodies. Imaging was carried out using an Airyscan fluorescent confocal microscope (Carl Zeiss, LSM 800).

Estevez I., Buckley B.D., Panzera N., Lindman M., Chou T.W., McCourt M., Vaglio B.J., Atkins C., Firestein B.L, & Daniels B.P. (2024). RIPK3 promotes neuronal survival by suppressing excitatory neurotransmission during CNS viral infection. bioRxiv.

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Whole-mount immunostaining of Drosophila embryos

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Whole-mount immunostainings of fixed embryos were performed as described previously [67 ]. The following primary antibodies were used: chicken anti-GFP (1:500; Abcam), mouse anti-Spectrin 3A9 (1:10; DSHB), guinea pig anti-Uif (1:500; [68 (link)]), mouse anti-Mega (1:20; [69 (link)]), mouse anti-Crumbs Cq4 (1:50; DSHB), rat anti-DE-cadherin DCAD2 (1:50; DSHB), sheep anti-human-matriptase (1:250; R&D Systems), rabbit anti-human-prostasin (1:250; GeneTex), rabbit anti-human-HAI-2 (1:200; ThermoFisher), and rabbit anti-mCherry (1:500; Rockland). The following secondary antibodies were used in 1:500 dilutions: goat anti-mouse IgG Alexa568, goat anti-mouse IgG Alexa488, goat anti-guinea pig IgG Alexa488, goat anti-rabbit IgG Alexa568, goat anti-rabbit IgG Alexa488 (Invitrogen), goat anti-chicken Alexa488 (Jackson Immuno Research), donkey anti-chicken DyLight549 (Jackson Immuno Research), and donkey anti-sheep Alexa568 (Invitrogen). Fluorescein-conjugated chitin-binding probe (NEB) was used in a 1:500 dilution to stain chitin. Stained embryos were mounted in ProLong Gold antifade reagent (Invitrogen). Image acquisitions were performed with a LSM780 confocal microscope (Zeiss) and a LD LCI Plan-Apochromat 25×/0.8 Imm Corr DIC M27 or a Plan-Apochromat 40×/1.4 Oil DIC M27 oil immersion or a 63×/1.3 Imm Corr DIC M27 LCI Plan-Neofluar (water) objective using standard settings.

Drees L., Königsmann T., Jaspers M.H., Pflanz R., Riedel D, & Schuh R. (2019). Conserved function of the matriptase-prostasin proteolytic cascade during epithelial morphogenesis. PLoS Genetics, 15(1), e1007882.

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