Alexa fluor 488 goat anti mouse igg secondary antibody

Manufactured by Thermo Fisher Scientific

Sourced in United States

Alexa Fluor 488 goat anti-mouse IgG secondary antibody is a fluorescent-labeled secondary antibody. It is designed to detect and visualize mouse primary antibodies in various immunoassays, such as immunohistochemistry, flow cytometry, and Western blotting.

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Alexa Fluor 488 goat anti-mouse IgG (799 citations) Alexa Fluor 488 goat anti-mouse antibody (112 citations) Alexa Fluor 488 goat anti-mouse secondary antibody (111 citations) Alexa Fluor 488 goat anti-mouse IgG antibody (64 citations) Alexa Fluor 488 anti-mouse secondary antibody (49 citations) Goat anti-mouse alexa-488 secondary antibody (25 citations) Alexa Fluor 488 anti-mouse IgG antibody (15 citations) Alexa 488® goat-anti-mouse IgG secondary antibody (8 citations) Anti-mouse IgG Alexa Fluor 488 secondary antibody (4 citations) Secondary goat anti-mouse Alexa Fluor 488 (2 citations)

65 protocols using alexa fluor 488 goat anti mouse igg secondary antibody

Histopathological Analysis of Ablated Corneas

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Beagle eyes were enucleated by the conventional trans-scleral method after euthanasia. Porcine and canine corneas were excised from the globe by cutting with a blade and tenotomy scissors 2 to 3 mm from the limbus. Samples were fixed in 10% buffered formalin and embedded in paraffin. Sections were stained with PAS according to the standard procedure. A light microscope (BX51; Olympus, Japan) equipped with a digital camera (DP71; Olympus) was used for photomicrography. The thickness of the non-ablated and ablated corneas on the histopathological section was determined by digital image analysis and the percentage of the ablated corneal thickness was calculated (panel H in Fig. 1).
Immunofluorescent staining for α-smooth muscle actin (SMA), a marker for myofibroblasts, was performed in the canine eyes using mouse monoclonal antibody for α-SMA (Dako, USA) with Alexa Fluor 488 goat anti-mouse IgG secondary antibody (Molecular Probes, USA). The immunohistochemistry slides were mounted with SlowFade Gold antifade reagent with DAPI (Molecular Probes) and imaged using a fluorescence microscope (BX51; Olympus) equipped with a digital camera (DP71; Olympus).

Kim S., Park Y.W., Lee E., Park S.W., Park S., Kim J.W., Seong J.K, & Seo K. (2015). Air assisted lamellar keratectomy for the corneal haze model. Journal of Veterinary Science, 16(3), 349-356.

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Reagents for RNA-related Experiments

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The following reagents were purchased: mouse mAb J2 (Scicons); Alexa Fluor 488-goat anti-mouse IgG secondary antibody (Molecular Probes, Life Technologies); Phi6 dsRNA (Finnzymes, Thermo Fisher Scientific); dsRNA ladder (New England Biolabs); High MW poly (A:U) and poly (I:C) (InvivoGen); GeneRuler 1 kb DNA Ladder (Thermo Fisher Scientific); Silencer negative control 1 siRNA (Ambion, Life Technologies); Strep-Tactin conjugated to horseradish peroxidase (IBA Lifesciences); pNPP (Sigma-Aldrich), mMESSAGE mMACHINE T7 transcription kit (Ambion, Life Technologies), Lumi-Light western blotting substrate (Roche Diagnostics).

Monsion B., Incarbone M., Hleibieh K., Poignavent V., Ghannam A., Dunoyer P., Daeffler L., Tilsner J, & Ritzenthaler C. (2018). Efficient Detection of Long dsRNA in Vitro and in Vivo Using the dsRNA Binding Domain from FHV B2 Protein. Frontiers in Plant Science, 9, 70.

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Immunostaining of Cultured Cells

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IMCs cultured on cover glasses were fixed in 5% neutral buffered formalin at 37°C for 5 min. After fixation, the cells were washed three times in Tris-buffered saline (TBS) for 30 min each, then with 0.1% Triton-X100 in TBS
containing 1% bovine serum albumin (BSA) for 90 sec. After membrane permeabilization, the cells were incubated with 1% BSA in TBS at room temperature for 30 min to reduce non-specific binding. Subsequently, the cells were
incubated with 1:100 diluted mouse vimentin antibody (Nichirei Co., Tokyo, Japan, H912) in TBS with 2% BSA at room temperature for 1 hr. After washing with TBS for 30 min at 4°C, the cells were incubated with 1:250 diluted Alexa
Fluor® 488 goat anti-mouse IgG secondary antibody and 1:50 diluted Rhodamine-Phalloidin (Molecular Probes, Eugene, OR, U.S.A., R-415), which is an F-actin probe conjucted to red fluorescent dye and stabilizes actin filaments, in
TBS at room temperature for 1 hr. After washing twice with TBS, the cells were incubated with DAPI (1 µg/ml) for 5 min. The cells were washed twice and mounted on glass slides. We used an Eclipse
E800 (Nikon) for observation.

MIHARA T., OTSUBO W., HORIGUCHI K., MIKAWA S., KAJI N., IINO S., OZAKI H, & HORI M. (2017). The anti-inflammatory pathway regulated via nicotinic acetylcholine receptors in rat intestinal mesothelial cells. The Journal of Veterinary Medical Science, 79(11), 1795-1802.

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Visualizing IQGAP3 and Myosin Localization

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Cells expressing endogenous IQGAP3 or myc-tagged IQGAP3 were fixed and stained with in-house anti-IQGAP3 or anti-c-myc (9E10) (Santa Cruz Biotechnologies, Santa Cruz, CA, USA), respectively. Subsequently, Alexa Fluor^® 488 goat anti-rabbit IgG secondary antibody or Alexa Fluor^® 488 goat anti-mouse IgG secondary antibody (Molecular Probes, Invitrogen, Carlsbad, CA, USA) were used for visualization. Nuclei were counterstained with 4′,6′-diamidine-2′-phenylindole dihydrochloride (DAPI). Actin cytoskeleton was visualized with Alexa Fluor^® 594 phalloidin (Molecular Probes, Invitrogen, Carlsbad, CA, USA). Monoclonal Anti-Myosin (Light Chains 20 kDa, clone MY21, Sigma-Aldrich) and Alexa Fluor^® 594 goat anti-mouse IgM (μ chain) secondary antibody (Molecular Probes, Invitrogen, Carlsbad, CA, USA) were used to localize myosin light chain in cells. Fluorescent images were obtained with a TCS SP2 AOBS Spectral Confocal Scanning System (Leica, Bensheim, Germany).

Jinawath N., Shiao M.S., Chanpanitkitchote P., Svasti J., Furukawa Y, & Nakamura Y. (2020). Enhancement of Migration and Invasion of Gastric Cancer Cells by IQGAP3. Biomolecules, 10(8), 1194.

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Antibody Sources for Cell Signaling

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Mouse monoclonal anti-flag M2 (DYKDDDDK) antibody and its agarose-conjugated form, anti-Sharpin, and anti-β-actin were purchased from Sigma. Cell Signaling (Beverly, MA, USA) provided rabbit anti-β-catenin, Novus Biologicals (Littleton, CO, USA) provided anti-pan-Versican, and Molecular Probes (Eugene, OR, USA) provided Alexa Fluor 488 goat anti-mouse IgG secondary antibody and Alexa Fluor 555 goat anti-rabbit IgG secondary antibody. Bethyl Laboratories (Montgomery, TX, USA) provided mouse anti-β-catenin antibody. Anti-mouse and rabbit IgG, horseradish peroxidase (HRP)-linked antibodies were purchased from Amersham Biosciences (Uppsala, Sweden).
Other chemicals and reagents were from Sigma unless otherwise specified.

Tanaka Y., Tateishi K., Nakatsuka T., Kudo Y., Takahashi R., Miyabayashi K., Yamamoto K., Asaoka Y., Ijichi H., Tateishi R., Shibahara J., Fukayama M., Ishizawa T., Hasegawa K., Kokudo N, & Koike K. (2016). Sharpin promotes hepatocellular carcinoma progression via transactivation of Versican expression. Oncogenesis, 5(12), e277-.

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Propagation and Titration of DENV-1

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The viral strain used in this study was a DENV-1 genotype I isolated from a patient in New Caledonia in 2014 (GenBank KY553285). The virus stock was obtained after five passages of 5 days incubation at 28 °C on Ae. albopictus C6/36 cells in Leibovitz L15 medium (Sigma-Aldrich, Saint-Louis, Missouri, USA) supplemented with 2% fetal bovine serum (FBS; Gibco BRL, Paisley, Scotland, UK) and 10% of tryptose phosphate (Gibco BRL, Paisley, Scotland, UK). The titration of the viral stock was performed using immunofluorescent assays with the anti-dengue virus complex antibody, clone D3-2H2–9-21 (Millipore, Billerica, Massachusetts, USA) and the Alexa Fluor 488 goat anti-mouse IgG secondary antibody (Life technologies, Eugene, Oregon, USA) and the results calculated in FFU/ml (Focus Forming Unit).

Calvez E., Guillaumot L., Girault D., Richard V., O’Connor O., Paoaafaite T., Teurlai M., Pocquet N., Cao-Lormeau V.M, & Dupont-Rouzeyrol M. (2017). Dengue-1 virus and vector competence of Aedes aegypti (Diptera: Culicidae) populations from New Caledonia. Parasites & Vectors, 10, 381.

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Localization of NR4A3 in GnRHa-treated LβT2 cells

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LβT2 cells were seeded on poly-L-lysine-coated coverslips and were grown for 2 days. After incubation with GnRHa (10^–8 M), the cells were fixed with 4% paraformaldehyde-PBS at room temperature for 10 minutes and then were blocked by incubating with 10% normal goat serum for 30 minutes. Immunocytochemistry was performed using an indirect immunofluorescence technique with an anti-NR4A3 primary antibody (1:2000) and an Alexa Fluor 488 goat anti-mouse IgG secondary antibody (1:200; Life Technologies) [19 ]. To visualize the actin cytoskeleton, F-actin was stained with Alexa Fluor 568 phalloidin (Life Technologies) for 30 minutes. The specimens were mounted with VECTASHIELD mounting medium with DAPI (Vector Laboratories, Burlingame, CA), and they were visualized using a confocal laser microscope (LSM710, Carl Zeiss Japan, Tokyo, Japan).

Terashima R., Saigo T., Laoharatchatathanin T., Kurusu S., Brachvogel B., Pöschl E, & Kawaminami M. (2020). Augmentation of Nr4a3 and Suppression of Fshb Expression in the Pituitary Gland of Female Annexin A5 Null Mouse. Journal of the Endocrine Society, 4(9), bvaa096.

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Cell Surface Localization of Recombinant Receptors

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The day following transfection, cells were detached with 0.25% Trypsin–EDTA (Wisent) and 2.0 × 10⁴ cells were re-plated onto a poly-l-ornithine (Sigma-Aldrich) treated clear bottom black 96-well plate (Thermo Scientific, 165305). The next day, the cells were washed once with phosphate-buffered saline (PBS) and fixed with 2% paraformaldehyde (Sigma-Aldrich) for 10 min at room temperature. Successively, the cells were blocked with a 1% bovine serum albumin (Fisher Scientific) PBS solution for 1 h at room temperature to prevent non-specific interactions of the antibodies. Cells were then incubated with a monoclonal mouse anti-HA primary antibody for 1 h (BioLegend, 1:200, previously Covance). Afterward, the cells were washed three times with PBS and an Alexa fluor-488 goat anti-mouse IgG secondary antibody (Life Technologies, 1:1,000) was used to label cells. To confirm the ability of recombinant receptors to localize to the cell surface, the Operetta High Content Imaging system (Perkin Elmer) with a 20× WD objective was used. The excitation filter was set at 475/15 nm and its corresponding emission filter at 525/25 which permitted to capture the signal produced by Alexa fluor-488.

Bourque K., Pétrin D., Sleno R., Devost D., Zhang A, & Hébert T.E. (2017). Distinct Conformational Dynamics of Three G Protein-Coupled Receptors Measured Using FlAsH-BRET Biosensors. Frontiers in Endocrinology, 8, 61.

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Immunostaining of Differentiated C2C12 Myotubes

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Following 5 days of differentiation, C2C12 myotubes were fixed with 4% PFA/PBS for 10 min. Fixed cells were permeabilised in 0.1% Trition X-100/PBS and blocked with 1% BSA/PBS for 1 h at room temperature. Cells were incubated overnight at 4°C with a primary antibody against sarcomeric myosin (MF-20, Developmental Studies Hybridoma Bank) diluted 1:50 in 1% BSA/PBS. Following this, the cells were incubated with an Alexa Fluor® 488 goat anti-mouse IgG secondary antibody (Life Technologies, Melbourne, VIC) diluted 1:1000 and 0.1 μg/ml DAPI stain (Sigma-Aldrich, Castle Hill, NSW) in 1% BSA/PBS for 1 h at room temperature. Cell images were obtained using the Olympus Fluoview FV10i confocal laser scanning microscope with dedicated software at a 20x magnification. To assess myogenic differentiation, the number of DAPI-stained nuclei within the sarcomeric myosin positive myotubes (multinucleated cells, i.e., ≥2 nuclei) was determined and expressed as a percentage of the total number of nuclei analyzed per image. A minimum of 40 images per group (from two separate experiments) were analyzed using the ImageJ Software (National Institutes of Health, Bethesda, MA).

Wallace M.A., Della Gatta P.A., Ahmad Mir B., Kowalski G.M., Kloehn J., McConville M.J., Russell A.P, & Lamon S. (2016). Overexpression of Striated Muscle Activator of Rho Signaling (STARS) Increases C2C12 Skeletal Muscle Cell Differentiation. Frontiers in Physiology, 7, 7.

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VEEV Infection and Host Factor Analysis

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HeLa cells in 12-well plates were inoculated with VEEV TC-83 (MOI = 10) for 5 h. DMSO, EHT1864, CK548, nocodazole, latrunculin A, or cytochalasin D were subsequently added at the indicated concentrations. Five or 6 h later, cells were detached with Cell Dissociation Buffer (Life Technologies) and washed with flow buffer (PBS/0.5% bovine serum albumin/2mM EDTA). Cells were incubated with mouse anti-VEEV E2 or CD44 primary antibody (1:1,000 dilution in flow buffer) for 30 min on ice and then washed twice with ice-cold flow buffer. Cells were incubated for 20 min in the dark with Alexa Fluor 488 Goat Anti-Mouse IgG secondary antibody (Life Technologies) (1:5,000 dilution in ice-cold flow buffer) and with 7-amino-actinomycin D to exclude dead cells from analysis (1:500 dilution). Following two more washes with ice-cold flow buffer, cells were fixed in 1% paraformaldehyde. Cytometric collection was performed using a FACS Canto II (BD Biosciences), and data were analyzed using Flowjo v7.6.5 (TreeStar).

Radoshitzky S.R., Pegoraro G., Chī X., Dǒng L., Chiang C.Y., Jozwick L., Clester J.C., Cooper C.L., Courier D., Langan D.P., Underwood K., Kuehl K.A., Sun M.G., Caì Y., Yú S., Burk R., Zamani R., Kota K., Kuhn J.H, & Bavari S. (2016). siRNA Screen Identifies Trafficking Host Factors that Modulate Alphavirus Infection. PLoS Pathogens, 12(3), e1005466.

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