Anti mouse cy3

Manufactured by Merck Group

Sourced in United States

The Anti-mouse Cy3 is a fluorescent labeling reagent that can be used to detect and visualize mouse proteins in various experimental applications. It is a cyanine dye that emits light in the red-orange region of the visible spectrum when excited by an appropriate light source.

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Lab products found in correlation

Anti rabbit cy3, by Merck Group (2 mentions) Lsm 710, by Zeiss (2 mentions) Alexa fluor 488 anti rabbit igg, by Thermo Fisher Scientific (2 mentions) 4 6 diamidino 2 phenylindole (dapi), by Vector Laboratories (1 mentions) Fitc conjugated lectin, by Merck Group (1 mentions) Fluoview fv1000, by Olympus (1 mentions) Serotonin, by Merck Group (1 mentions) Acetylated α tubulin, by Merck Group (1 mentions) Alexa 488 conjugated phalloidin, by Thermo Fisher Scientific (1 mentions) Anti mouse alexa555, by Thermo Fisher Scientific (1 mentions) Anti p21 f 5, by Santa Cruz Biotechnology (1 mentions) Anti phospho h2ax ser139, by Merck Group (1 mentions) Anti 53bp1, by Abcam (1 mentions) Anti phospho rpa32 s33, by Fortis Life Sciences (1 mentions) Anti rabbit cy5, by Thermo Fisher Scientific (1 mentions) Anti rabbit cy3, by Jackson ImmunoResearch (1 mentions) Ab51052, by Abcam (1 mentions) Hrp conjugated antibodies, by Agilent Technologies (1 mentions) α sma 14 9760 82, by Thermo Fisher Scientific (1 mentions) β actin, by Cell Signaling Technology (1 mentions)

Close spelling variants of this product

Cy3-conjugated anti-mouse secondary antibody (5 citations) Cy3-conjugated goat anti-mouse IgG (5 citations) Mouse anti-α-smooth muscle actin-Cy3 (4 citations) Cy3-conjugated anti-mouse alpha smooth muscle actin antibody (4 citations) Mouse Cy3 conjugated anti-c-Myc antibody [9E10] (3 citations) Sheep anti-mouse Cy3 (3 citations) Cy3-conjugated mouse monoclonal anti-α-smooth muscle actin antibody (3 citations) Cy3-conjugated anti-mouse antibody (3 citations) Mouse anti-αSMA-Cy3 (3 citations) Goat anti-mouse Cy3 secondary antibody (3 citations)

8 protocols using anti mouse cy3

Quantifying Epithelial-Mesenchymal Transition by ICC

Cited 2 times

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AECs phenotype was defined by analyzing the epithelial (E-Cadherin and CYTO8) and mesenchymal (VIM) protein expression and localization by immunocytochemistry (ICC) as previously reported [21 (link)]. Nuclear counterstaining was obtained with DAPI (Vectastain) at the final dilution of 1:2000 in PBS. The omission of primary antibodies (Abs) was used as negative control. Details on Abs and dilutions are specified in Table 2. The reaction was carried out in triplicate on each biological replicate (n = 3) for each experimental condition.Table 2

Primary and secondary antibodies used for ICC and WB. (Ref(a) [21 (link)]; Ref(b) [40 (link)]).

Table 2

Investigation	Primary Antibody	Dilution	Secondary Antibody	Dilution
ICC	E-Cadherin^a (LS Bio, Massachusetts, USA)	1:100	Anti-rabbit Alexa Fluor (Sigma-Aldrich, St. Louis, MO, USA)	1:200
	CYTO8^a,b (Abcam, Cambridge, UK)	1:200	Anti-mouse Alexa Fluor (Sigma-Aldrich, St. Louis, MO, USA)	1:500
	VIM^a,b (Agilent Technologies, California, USA)	1:200	Anti-mouse Cy3 (Sigma-Aldrich, St. Louis, MO, USA)	1:750
WB	Rabbit pSMAD2^a (3108 Cell Signalling)	1:500	Anti-rabbit HRP conjugated (31461, Pierce™ Antibody)	1:2000
	Rabbit SMAD2/3^a (3102 Cell Signalling)	1:500	Anti-rabbit HRP conjugated (31461, Pierce™ Antibody)	1:2000
	Mouse α-TUBULIN^a (SIGMAT5168)	1:1000	Anti-mouse HRP conjugated (Santa Cruz sc 516102)	1:10000

Cerverò-Varona A., Canciello A., Peserico A., Haidar Montes A.A., Citeroni M.R., Mauro A., Russo V., Moffa S., Pilato S., Di Giacomo S., Dufrusine B., Dainese E., Fontana A, & Barboni B. (2023). Graphene oxide accelerates TGFβ-mediated epithelial-mesenchymal transition and stimulates pro-inflammatory immune response in amniotic epithelial cells. Materials Today Bio, 22, 100758.

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Immunocytochemical Analysis of Microglial Signaling Pathways

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BV2 microglial cells were grown on poly-L-lysine coated coverslips. Following transfection and/or treatment, cells were fixed with 4% paraformaldehyde for 15min at room temperature. Permeabilization of cell membranes was achieved using 0.1% Triton-X containing PBS. Following this, the slides were blocked using 5% normal goat serum and incubated overnight at 4°C with the following antibodies- SMAD4-1:100 (Santa Cruz, sc-7966), pSMAD2/3-1:200 (Cell signaling technology, Cat No: 8828) and SMAD2/3-1:200 (Cell Signaling Technology, Cat No: 8685). Following this, cells were incubated with fluorophore tagged secondary antibodies: anti-rabbit Cy3 (Sigma, Cat No: c2306), anti-mouse Cy3 (Sigma, Cat No: C2181) and FITC conjugated lectin (Sigma, Cat No: L0401) was used as a marker for microglial cells. Cell nuclei were counterstained with DAPI for visualization. Fluorescence images were captured using a confocal microscope (Olympus, FV1000 Fluoview).

Karthikeyan A., Gupta N., Tang C., Mallilankaraman K., Silambarasan M., Shi M., Lu L., Ang B.T., Ling E.A, & Dheen S.T. (2018). Microglial SMAD4 regulated by microRNA-146a promotes migration of microglia which support tumor progression in a glioma environment. Oncotarget, 9(38), 24950-24969.

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Multimodal Imaging of Cellular Architecture

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Immunohistochemistry followed standard protocols (Sive et al., 2000 (link)), using antibodies specific for acetylated-α-tubulin (mouse, 1:700; Sigma), ATP4a (1:500; Walentek et al., 2012 (link)), anti-mouse Cy3 (sheep, 1:250; Sigma); serotonin (rabbit, 1:500; Merck), anti-rabbit Alexa-555 (1:250; Invitrogen), anti-mouse Alexa-555 (1:250; Invitrogen), anti-mouse Alexa-405 (1:250; Invitrogen). Cell boundaries were visualized by Alexa 488-conjugated phalloidin (Invitrogen), which stained the actin cytoskeleton. Imaging was performed on a Zeiss LSM710. Lateral projections of confocal z-scans were computed using Zeiss Zen software. Maximum intensity projections of confocal z-scans were computed using ImageJ (Schindelin et al., 2012 (link)). Scanning electron microscopy was as previously described (Beyer et al., 2012 (link)).

Walentek P., Beyer T., Hagenlocher C., Müller C., Feistel K., Schweickert A., Harland R.M, & Blum M. (2015). ATP4a is required for development and function of the Xenopus mucociliary epidermis - a potential model to study proton pump inhibitor-associated pneumonia. Developmental biology, 408(2), 292-304.

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Immunofluorescence and Telomere FISH Analysis

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Cells were grown on coverslips, fixed with 4% PFA, followed by 2 washes with cold PBS, permeabilized with 0.25% Triton X-100 in PBS, 3× washed with PBS, and blocked with 1% BSA in PBST at room temperature. Coverslips were then incubated with antibody solution in 1% BSA PBST. Antibodies were anti-phospho-H2AX (Ser139) (Millipore; 07-164), anti-53BP1 (Abcam; ab36823), anti-p21 (F-5) (Santa Cruz; sc-6246), anti-BLM (Sigma-Aldrich; HPA005689) and anti-Phospho RPA32 (S33) (Bethyl; A300-246A). Cells were incubated with antibody solution over night at 4°C followed by 3 washes in PBS, 1 h incubation with an appropriate secondary antibody labeled with fluorophore, anti-mouse Cy3 (Sigma, C2181), anti-rabbit Cy3 (Jackson ImmunoResearch, 111-165-006) and anti-rabbit Cy5 (Invitrogen, 81-6116) and 3 washes in PBS. Finally, samples were mounted with DAPI fluorescence mounting medium and analyzed under a fluorescence microscope. For IF-FISH, immunofluorescence stainings were done as described above, and slides were shortly fixed in 2% PFA at room temperature. And then, slides were processed for telomere qFISH as described before.

Meena J.K., Cerutti A., Beichler C., Morita Y., Bruhn C., Kumar M., Kraus J.M., Speicher M.R., Wang Z.Q., Kestler H.A., d’Adda di Fagagna F., Günes C, & Rudolph K.L. (2015). Telomerase abrogates aneuploidy-induced telomere replication stress, senescence and cell depletion. The EMBO Journal, 34(10), 1371-1384.

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Western Blot Antibody Validation Protocol

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Primary antibodies against Furin (70393), Vimentin (5741), N-cadherin (14215), and β-Actin (4970) were purchased from Cell Signalling Technology (Danvers, MA, USA). Those against β-Catenin (ab32572), hsc70 (ab51052), and GAPDH (ab8245) were from Abcam (Cambridge, UK). Other primary antibodies used were: E-cadherin (80182) from BD Biosciences (Bedford, MA, USA) and α-SMA (14-9760-82) from Invitrogen™ (Waltham, MA, USA). All the HRP-conjugated antibodies were from DAKO (Nowy Sącz, Poland) and for immunofluorescence detection Alexa Fluor 488 anti-rabbit IgG (Invitrogen™) and Cy3 anti-mouse (Sigma-Aldrich, St. Louis, MO, USA) were used. For the ChIP assay, antibodies against RARα (sc-515796) and non-specific IgG (sc-2025) were used, both from Santa Cruz Biotechnology (Dallas, TX, USA).

Cabezuelo M.T., Torres L., Ortiz-Zapater E., López-Rodas G., Marín M.P., Timoneda J., Viña J.R., Zaragozá R, & Barber T. (2024). Vitamin A Status Modulates Epithelial Mesenchymal Transition in the Lung: The Role of Furin. Nutrients, 16(8), 1177.

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Antibody Panel for WB and IF

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For Western blot (WB) and immnufluorescence, we employed: rabbit anti-LRP1β (Sigma–Aldrich Canada), rabbit anti-LC3B (Sigma–Aldrich), mouse anti-β-actin (GenScript), mouse anti-GM130 (Sigma), anti-rabbit HRP (Sigma), mouse anti-HRP (Sigma), Alexa Flour 488 anti-rabbit (Sigma), Cy3 anti-rabbit (Sigma), Cy3 anti-mouse, and Alexa Flour 594 anti-rabbit (Sigma).

Grosso R.A., Caldarone P.V., Sánchez M.C., Chiabrando G.A., Colombo M.I, & Fader C.M. (2019). Hemin induces autophagy in a leukemic erythroblast cell line through the LRP1 receptor. Bioscience Reports, 39(1), BSR20181156.

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Immunofluorescence Staining of HeLa Cells

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HeLa cells were prepared using combinations of the above techniques, typically involving synchronization and/or TNFα stimulation of cells seeded at appropriate density into 35 mm glass-bottomed dishes. Dishes were subsequently washed three times with PBS and fixed with 1 ml 4% paraformaldehyde for 15 min. Dishes were then washed three times with PBS, and ‘blocked’ to prevent non-specific antibody binding with the addition of 1–2 ml of 1% BSA, 0.1% Triton X-100 (in PBS) from 20 min up to overnight. The primary antibody (or antibodies for dual-staining), dissolved in Ab Buffer (1% BSA, 0.1% Triton X-100 in PBS), were added to the dishes for 60/90 min at a 1:2000 dilution. Dishes were then washed (3x1 ml) with Ab buffer for 10 min. Secondary Antibody(s) were subsequently added to the dishes (Cy3-anti-mouse, 1:200 dilution (Sigma), FITC Rabbit, 1:200 [AbCam]) for 30/45 min respectively, prior to 3 sequential washes of PBS blocking buffer (described above). Following the addition of fluorescent secondary antibodies, dishes were covered in aluminium foil and left in 2 ml PBS prior to imaging.

Ankers J.M., Awais R., Jones N.A., Boyd J., Ryan S., Adamson A.D., Harper C.V., Bridge L., Spiller D.G., Jackson D.A., Paszek P., Sée V, & White M.R. (2016). Dynamic NF-κB and E2F interactions control the priority and timing of inflammatory signalling and cell proliferation. eLife, 5, e10473.

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Calpain Modulation in Cellular Processes

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Primary antibodies against calpain-1 (ab39170), Nucleolin (ab22758) and α-Tubulin (ab52866) were purchased from Abcam. Other antibodies used were: α-Calpain-2 (Cell Signaling), α-Fibrillarin (Novus Biologicals), Alexa Fluor 488 anti-rabbit IgG (Invitrogen), and Cy3 anti-mouse (Sigma). Inhibitors of PI3K (LY294002) and RNA Pol I (CX5461) were both from Calbiochem. Inhibitors of MEK (UO126) and calpain activity (calpeptin) were purchased from Promega and Sigma, respectively. Epidermal Growth Factor (EGF) was obtained from R&D Systems.

Telechea-Fernández M., Rodríguez-Fernández L., García C., Zaragozá R., Viña J., Cervantes A, & García-Trevijano E.R. (2018). New localization and function of calpain-2 in nucleoli of colorectal cancer cells in ribosomal biogenesis: effect of KRAS status. Oncotarget, 9(10), 9100-9113.

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