Goat anti c myc

Manufactured by Novus Biologicals

Goat anti-c-Myc is a primary antibody that recognizes the c-Myc epitope. It is commonly used in various research applications that involve the detection and analysis of c-Myc proteins.

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Lab products found in correlation

Pierce bca protein assay kit, by Thermo Fisher Scientific (2 mentions) Vectashield fluorescence mounting medium, by Vector Laboratories (1 mentions) Chicken anti green fluorescent protein gfp, by Aves Labs (1 mentions) Mouse anti c myc antibody, by Santa Cruz Biotechnology (1 mentions) Bx51wi upright microscope, by Olympus (1 mentions) Alexa fluor 568, by Thermo Fisher Scientific (1 mentions) P3xflag cmv 10 vector, by Merck Group (1 mentions) Alexa fluor 647, by Thermo Fisher Scientific (1 mentions) Alexa fluor 488, by Thermo Fisher Scientific (1 mentions) Q5 site directed mutagenesis kit, by New England Biolabs (1 mentions) Plasmid mini kit, by Qiagen (1 mentions) Goat anti gli3, by R&D Systems (1 mentions) Mouse anti β actin, by Proteintech (1 mentions) Pvdf membrane, by Bio-Rad (1 mentions) Protease inhibitor, by Roche (1 mentions) Clarity western ecl substrate, by Bio-Rad (1 mentions) Hrp conjugated secondary antibody, by Jackson ImmunoResearch (1 mentions) Mouse anti gapdh, by Proteintech (1 mentions)

Close spelling variants of this product

Anti-c-MYC C-Myc Anti-myc

4 protocols using goat anti c myc

Cornea Visualization and Immunohistochemistry

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Reporter visualization. Mice were sacrificed by CO2 asphyxiation, and their eyes were isolated and typically fixed in 2% paraformaldehyde in sodium acetate buffer, pH 6.0 [12 (link)]. The corneas surgically dissected from the P0-Cre;R26-tdTomato animals were fixed in 4% paraformaldehyde and examined directly following mounting, without antibody-mediated enhancement. In the case of the MADM mice, whole corneas were incubated overnight at 4 °C in combined primary antibodies (chicken anti-green fluorescent protein [GFP]; Aves Labs, Tigard, OR; 1:500, and goat anti-c-Myc; Novus Biologicals, Littleton, CO; 1:200) diluted in Tris-buffered saline (TBS), pH 7.3, with 1.0% bovine serum albumin (BSA) and 0.4% Triton X-100. Anti-c-Myc antibody was preabsorbed with fixed wild-type tissue before use [13 (link)]. The following day, the slides were labeled serially with fluorescein isothiocyanate (FITC)–conjugated and Alexa Fluor 555–conjugated secondary antibodies (1:200 and 1:400 dilution, respectively) to enhance visualization of GFP and c-Myc-RFP, respectively. After several buffer rinses, four radial incisions were made in each cornea to produce “petals,” and the resulting flatmounts were placed on glass slides with the endothelium facing up and then coverslipped using Vectashield fluorescence mounting medium (Vector Labs, Burlingame, CA) [14 (link)].

Harrison T.A., He Z., Boggs K., Thuret G., Liu H.X, & Defoe D.M. (2016). Corneal endothelial cells possess an elaborate multipolar shape to maximize the basolateral to apical membrane area. Molecular Vision, 22, 31-39.

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Primary Cortical Neuron Transfection Workflow

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Primary cortical neuronal cultures were prepared from embryonic day 17 (E17) Sprague Dawley rats (Envigo and Charles River Laboratories). Neurons were plated at 450,000 cells/well in 12-well plates. On day in vitro (DIV) 12 the neurons were transfected with CACNB4/Myc (OriGene; Catalog #: RR204310) and GFP (gift of Ryan Logan, University of Pittsburgh, PA). Thus, in the same plate some neurons were transfected with both constructs and some with only one. Neurons were fixed on DIV 15 for imaging with mouse anti-c-Myc antibody (1:1000, monoclonal 9E10; Santa Cruz Biotechnology, Inc.) or with mouse anti-CACNB4 (1:100, monoclonal S10-7; antibodies-online Inc.), and goat anti-c-Myc (1:100, polyclonal; Novus Biologicals). Image acquisition was performed on an Olympus (Center Valley, PA) BX51 WI upright microscope equipped with an Olympus spinning disk confocal (SDCM) using an Olympus PlanAPO N 10X 0.40 NA air objective and a 1.42 numerical aperture 60X oil supercorrected objective.
Neurons were first categorized as either CACNB4-overexpressing or GFP-only controls based on c-Myc intensity. GFP-positive neurons on coverslips stained for both c-Myc and CACNB4 were imaged at 10x. Exposure times for the 488 channel were optimized whereas the 568 and 647 channels were shot at fixed exposures of 447 ms and 3000 ms, respectively.

MacDonald M.L., Alhassan J., Newman J.T., Richard M., Gu H., Kelly R.M., Sampson A.R., Fish K.N., Penzes P., Wills Z.P., Lewis D.A, & Sweet R.A. (2017). Selective Loss of Smaller Spines in Schizophrenia. The American journal of psychiatry, 174(6), 586-594.

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Site-Directed Mutagenesis of hCTR1 Plasmid

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hCTR1 was cloned in p3XFLAG CMV10 vector (Sigma #E7658, a kind gift from Dr Rupasri Ain, CSIR-IICB) using HinDIII and EcoRI Restriction sites. Cytosolic myc-tagging and amino-terminal mutations were generated by following the Q5 Site-Directed Mutagenesis Kit (NEB #E0554) protocol. Primers for the site-directed mutagenesis were designed as per kit protocol and obtained from GCC biotech; their sequence details are provided in (Table S1). mEGFP-ATP7B and mKO2-ATP7A constructs were available in the lab. Following are the antibodies, used for different experiments: rabbit anti-FLAG M2 (CST #14793), mouse anti-FLAG (CST #8146), Goat anti-c-Myc(Novus #NB600-335), Mouse anti-Na/K ATPase (Invitrogen #MA3-929), anti-phalloidin 647 (Abcam #ab176759), Donkey anti-Rabbit IgG (H + L) Alexa Fluor 488 (Invitrogen #A-21206), Donkey anti-Mouse IgG (H + L) Alexa Fluor 568 (Invitrogen #A10037), Donkey anti-Goat IgG (H + L) Alexa Fluor 647 (Invitrogen #A21447), Rabbit anti-GAPDH (BioBharti #BB-AB0060), goat anti-rabbit IgG-HRP conjugated secondary antibody (BioBharti #BB-SAB01A). Plasmid isolations were done by QIAGEN plasmid mini kit (QIAGEN #27104).

Kar S., Sen S., Maji S., Saraf D., R.u.t.u.r.a.j., Paul R., Dutt S., Mondal B., Rodriguez-Boulan E., Schreiner R., Sengupta D, & Gupta A. (2022). Copper(II) import and reduction are dependent on His-Met clusters in the extracellular amino terminus of human copper transporter-1. The Journal of Biological Chemistry, 298(3), 101631.

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Protein Extraction and Immunoblotting Protocol

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Cells were lysed using RIPA buffer (150nm NaCl, 50mM Tris, pH 7.6, 0.1% SDS, 0.1% NP-40 and 0.5% sodium deoxycholate) supplemented with protease inhibitors (Roche). Protein concentration was determined using a Pierce BCA Protein Assay Kit (Thermo Fisher Scientific). Zebrafish embryos were deyolked before lysis in RIPA buffer supplemented with protease inhibitors, as previously described (Link et al., 2006 (link)). All lysates were boiled for 5 minutes in 4x SDS-PAGE loading buffer, except prior to immunoblotting for DREADD expression, for which lysates were incubated at room temperature for 45 minutes. Protein samples were separated on 4–15% gradient TGX precast gels (Bio-Rad) and transferred to PVDF membrane (Bio-Rad). 5% non-fat dried milk in TBS with 0.1% Tween was used to block membranes and to dilute antibodies. HRP signal was detected using Clarity Western ECL substrate (Bio-Rad). Primary antibodies used were goat anti-GFP (1:1,000, Rockland, RRID:AB_218182), mouse anti-GAPDH (1:100,000, Proteintech, RRID:AB_2107436), goat anti-GLI3 (1:200, R&D Systems, Cat #AF3690), goat anti-c-Myc (1:5,000, Novus, RRID:AB_10004121) and mouse anti-β-actin (1:100,000, Proteintech, RRID:AB_2687938). We used HRP-conjugated secondary antibodies at 1:5,000 dilution (Jackson ImmunoResearch Laboratories, Inc).

Truong M.E., Bilekova S., Choksi S.P., Li W., Bugaj L.J., Xu K, & Reiter J.F. (2021). Vertebrate cells differentially interpret ciliary and extraciliary cAMP. Cell, 184(11), 2911-2926.e18.

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