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Anti mouse sc 2005

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Anti-mouse (sc-2005) is a secondary antibody designed for use in immunoassays. It is produced in goat and targets mouse immunoglobulins.

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Lab products found in correlation

Anti rabbit sc 2004, by Santa Cruz Biotechnology (3 mentions) Anti tub1, by Merck Group (2 mentions) Anti egfp antibody, by Rockland Immunochemicals (2 mentions) Anti ym1, by STEMCELL (2 mentions) Ecl detection system, by GE Healthcare (2 mentions) Pvdf membrane, by Bio-Rad (2 mentions) Anti goat sc 2020, by Santa Cruz Biotechnology (2 mentions) Subcellular protein fractionation kit, by Thermo Fisher Scientific (2 mentions) Polyvinylidene difluoride membrane, by Merck Group (1 mentions) Ab6302, by Abcam (1 mentions) Ab53033, by Abcam (1 mentions) Ab8069, by Abcam (1 mentions) P stat3 tyr705, by Cell Signaling Technology (1 mentions) Tris glycine gel, by Thermo Fisher Scientific (1 mentions) β actin, by Santa Cruz Biotechnology (1 mentions) Ipfl10100, by Merck Group (1 mentions) Anti actin, by Santa Cruz Biotechnology (1 mentions) Dimethyl sulfoxide (dmso), by Avantor (1 mentions) Anti gapdh ab181602, by Abcam (1 mentions) Horseradish peroxidase conjugated secondary ab, by Santa Cruz Biotechnology (1 mentions)

Close spelling variants of this product

Goat anti-mouse IgG-HRP (sc-2005) (87 citations) Sc-2005 (81 citations) Goat anti-mouse (sc-2005) (22 citations) Goat anti-mouse IgG (sc-2005) (7 citations) Goat anti-mouse IgG HRP-conjugated (sc-2005, (6 citations) Horseradish peroxidase (HRP)-conjugated goat anti-mouse IgG (sc-2005), (4 citations) Horseradish Peroxidase conjugated goat anti-mouse (sc-2005, (4 citations) Anti-mouse IgG-HRP (sc–2005 (4 citations) HRP-conjugated anti-mouse IgG (sc-2005) (3 citations) Anti-mouse HRP-conjugated secondary antibody sc-2005 (3 citations)

13 protocols using anti mouse sc 2005

1

Western Blot Analysis of EGFP

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Protein samples were separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and then transferred to polyvinylidene difluoride membranes (Merck Millipore, Burlington, MA, USA). Anti-EGFP antibody (600-101-215 ROCKLAND, Limerick, PA, USA) was used for Western blotting, and the same blot was probed with anti-Tub1 (T5168, Sigma, St.Louis, MO, USA) as a positive control. HRP-conjugated anti-goat (705-035-003, Jackson Immune Research) and anti-mouse (sc-2005, Santa Cruz Biotechnology, Dallas, TX, USA) antibodies were used as secondary antibodies for detecting EGFP and anti-Tub1, respectively.
Choi Y.J, & Song K. (2022). Nst1, Densely Associated to P-Body in the Post-Exponential Phases of Saccharomyces cerevisiae, Shows an Intrinsic Potential of Producing Liquid-Like Condensates of P-Body Components in Cells. International Journal of Molecular Sciences, 23(5), 2501.
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2

Western Blot Analysis of Cell Lysates

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Western blot analysis in protein lysates derived by cell lines was performed as previously described 19 (link). Briefly, SDS-PAGE was conducted using 8%-12% gradient Tris-Glycine gels (Invitrogen) and loaded with 30ugs of total protein lysates. Membranes were blocked in TBS + 5% nonfat milk, primary and secondary antibodies were incubated overnight at 4° C or for 2h at RT, respectively, in TBS + 0.1% Tween-20 + 5% nonfat milk (pStat3 was incubated in TBS + 0.1% Tween-20 + 5% BSA). Primaries used were: β-actin ms (1:1000, 130065; Santa Cruz Biotech, Inc), pStat3 (Tyr705) rb (1:1000, 9145S; Cell Signaling, Inc), b-catenin rb (1/3000, ab6302; Abcam, Cambridge, MA), vimentin ms (1/2000, ab8069; Abcam), E-cadherin rb (1/500, ab53033; Abcam), ZEB1 rb (1/500, SAB3500514; Sigma-Aldrich, Saint Louis, MO), CRHR2 (1/1000, ABN433; Millipore, Temecula, CA). Horseradish peroxidase (HRP)-tagged IgG secondary antibodies were anti-mouse (sc2005; Santa Cruz Biotech, Inc) or anti-rabbit (sc2004; Santa Cruz Biotech, Inc) used at 1/2000 dilution. Chemiluminescence was detected with enhanced reagent (34080; ThermoScientific, Rockford, IL) using an Eastman Kodak Co. 440 Imaging System (Kodak, Rochester, NY). Beta-actin was used as a loading control.
Rodriguez J.A., Huerta-Yepez S., Law I.K., Baay-Guzman G.J., Tirado-Rodriguez B., Hoffman J.M., Iliopoulos D., Hommes D.W., Verspaget H.W., Chang L., Pothoulakis C, & Baritaki S. (2015). Diminished Expression of Corticotropin-Releasing Hormone Receptor 2 in Human Colon Cancer Promotes Tumor Growth and Epithelial-to-Mesenchymal Transition via Persistent Interleukin-6/Stat3 Signaling. Cellular and Molecular Gastroenterology and Hepatology, 1(6), 610-630.
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3

Western Blotting Analysis of Protein Targets

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Western Blotting assay was performed in a 12% PAGE separation gel, electro-transferring 30 μg of protein sample onto a PVDF membrane (IPFL10100 Merck Millipore, Italy), blocked for 1 h at room temperature with 5% non-fat dry milk (EMR180500 Euroclone, Italy). Then blots were incubated over-night with the following specific primary antibodies: anti-MC5R (sc-28994 Santa Cruz, United States), anti-GPR14 for Urotensin II receptor detection (sc-288998 Santa Cruz, United States), anti KIR 6.1 (P0874 Sigma, Italy), and anti-actin (sc-8432 Santa Cruz, United States). This step was followed by incubation for 1 h at room temperature with horseradish peroxidase-conjugated secondary anti-rabbit (sc-2004 Santa Cruz, United States) or anti-mouse (sc-2005, Santa Cruz, United States) antibodies. The signal was expressed as Densitometric Units (D.U.).
Trotta M.C., Maisto R., Alessio N., Hermenean A., D’Amico M, & Di Filippo C. (2018). The Melanocortin MC5R as a New Target for Treatment of High Glucose-Induced Hypertrophy of the Cardiac H9c2 Cells. Frontiers in Physiology, 9, 1475.
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4

Molecular Mechanisms of YAP Regulation

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Anti-YAP (A1002) was purchased from ABclonal (Wuhan, China). Anti-mouse (sc-2005), and anti-rabbit (sc-2004) HRP conjugated secondary antibodies were purchased from Santa-Cruz Biotechnology (Dallas, TX, USA); anti-GAPDH (ab181602) was purchased from Abcam (Shanghai, China). The anti-pMLC (3674 s) was purchased from Cell Signaling Technologies (Denvers, CO, USA); anti-RhoA (ARH04) was purchased from Cytosketon (Denvers, CO, USA); anti-ARHGAP29 (sc-377022) was purchased from Santa-Cruz Biotechnology (Dallas, TX, USA); Alexa Fluor 488- or Alexa Fluor 555-conjugated secondary antibodies were obtained from Life (Carlsbad, CA, USA). Rho activator II were from Cytoskeleton. Myosin II inhibitor (blebbistatin) was from EMD_Millipore. Bromophenol Blue was generously donated by Prof. Yuxin Yin’s lab. Dimethyl sulfoxide (DMSO) was purchased from VWR (branch company in Shanghai, China). DNA transfection reagent was purchased from NEOFECT (Beijing, China).
Huang Y., Su J., Liu J., Yi X., Zhou F., Zhang J., Wang J., Meng X., Si L, & Wu C. (2022). YAP Activation in Promoting Negative Durotaxis and Acral Melanoma Progression. Cells, 11(22), 3543.
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5

Quantification of CMV-pp65 Protein

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Proteins were extracted from 5 × 106 cells, using RIPA lysing buffer (Cell Signaling Technology®, Danvers, MA) supplemented with a protease inhibitor cocktail (Sigma-Aldrich, St. Louis, MO). Fifty μg of protein were resolved by SDS-PAGE, transferred to polyvinylidene difluoride membranes (Bio-Rad, Hercules, CA) and blocked with 5% (W/V) non-fat dry milk in Tris Buffer Saline (TBS) with 0.1% (V/V) Tween-20. Blots were stained with mouse anti-CMV-pp65 (1:200, clone 1-L-11) (Santa Cruz Biotechnology, Santa Cruz, CA) and mouse anti-human β-actin (1:10000, clone C4) (Santa Cruz Biotechnology). Blots were washed with TBS containing 0.1% (V/V) Tween-20, stained with horseradish peroxidase conjugated secondary Ab (1:5000, goat anti-mouse sc-2005) (Santa Cruz Biotechnology) and incubated with SuperSignal West Femto Maximum Sensitivity Substrate (Thermo Scientific).
Caruana I., Weber G., Ballard B.C., Wood M.S., Savoldo B, & Dotti G. (2015). K562-Derived Whole-Cell Vaccine Enhances Antitumor Responses of CAR-Redirected Virus-Specific Cytotoxic-T Lymphocytes in vivo. Clinical cancer research : an official journal of the American Association for Cancer Research, 21(13), 2952-2962.
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6

GAL Promoter Induction and Protein Analysis

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Yeast GAL promoter induction was performed as described above. For CHX treatment, GAL-induced cells were incubated with 100 μg/mL CHX for 10 min. For 1,6-hexanediol treatment, the GAL-induced cells were washed three times with a medium containing 10% 1,6-hexanediol and incubated for 30 min. Western blotting was performed as described by Choi and Song [40 (link)] with anti-EGFP antibody (600-101-215 Rockland, Limerick, PA, USA) and anti-Tub1 (T5168, Sigma, St. Louis, MO, USA) positive controls. HRP-conjugated anti-goat (705-035-003, Jackson Immune Research, PA, USA) and anti-mouse (sc-2005, Santa Cruz Biotechnology, Dallas, TX, USA) antibodies were used as secondary antibodies to detect EGFP and anti-Tub1, respectively.
Choi Y.J., Lee Y., Lin Y., Heo Y., Lee Y.H, & Song K. (2022). The Multivalent Polyampholyte Domain of Nst1, a P-Body-Associated Saccharomyces cerevisiae Protein, Provides a Platform for Interacting with P-Body Components. International Journal of Molecular Sciences, 23(13), 7380.
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7

Western Blot Protocol for Protein Expression Analysis

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Western blot was performed as previously done (25 (link), 26 (link)). Samples were electrophoresed on denaturing 10% polyacrylamide SDS gels followed by transfer to nitrocellulose membranes. Membranes were blocked for 1 hour with 5% of nonfat dry milk solution (PBS 0.1% Tween-20) and incubated overnight with anti–p-ERK1/2 (1:1000 — 4377-197G2, Cell Signaling Technology), anti-MasR (MAS1L 1:500 — ab200685 Abcam), anti–Arg-1 (1:1000, sc-20150 — H52, Santa Cruz Biotechnology), anti-Ym1 (60130, 1:1000 — StemCell Technologies), or anti–β-actin (1:3000, A5316 – AC-74, MilliporeSigma). Secondary anti-rabbit (7074, Cell Signaling Technology) or anti-mouse (sc-2005, Santa Cruz Biotechnology) HRP-conjugated antibodies (1:3000) were added to the membranes for further incubation of 1 hour at room temperature. ECL detection system (GE Healthcare, now Cytiva) was used to visualize immunoreactive bands. Membranes were scanned and densitometry analysis of the bands was performed using ImageJ software. Results were expressed as arbitrary units and normalized using β-actin levels as loading controls.
Zaidan I., Tavares L.P., Sugimoto M.A., Lima K.M., Negreiros-Lima G.L., Teixeira L.C., Miranda T.C., Valiate B.V., Cramer A., Vago J.P., Campolina-Silva G.H., Souza J.A., Grossi L.C., Pinho V., Campagnole-Santos M.J., Santos R.A., Teixeira M.M., Galvão I, & Sousa L.P. (2022). Angiotensin-(1-7)/MasR axis promotes migration of monocytes/macrophages with a regulatory phenotype to perform phagocytosis and efferocytosis. JCI Insight, 7(1), e147819.
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8

Quantifying Protein Expression via Western Blot

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Western blot analyses were performed as previously described [18 (link),21 (link)]. Samples were resolved on denaturing 10% polyacrylamide SDS gels followed by transfer to nitrocellulose membranes. Membranes were blocked for 1 h in PBS (5% non-fat dry milk; 0.1% Tween-20) and incubated overnight with antibodies anti-Ym1 (#60130, 1:1000—StemCell Technologies, Vancouver, BC, Canada), anti-P-STAT3 (#9134, 1:1000–Cell Signaling Technology, Beverly, MA, USA) or anti–β-actin (1:10,000, #A5316–AC-74, Sigma-Aldrich, St. Louis, MO, USA). Secondary anti-rabbit (#7074, Cell Signaling Technology) or anti-mouse (#sc-2005, Santa Cruz Biotechnology, Dallas, TX, USA) HRP-conjugated antibodies (1:3000) were added to the membranes and incubated for 1 h at room temperature. ECL detection system (GE Healthcare, Chicago, IL, USA) was used to visualize immunoreactive bands. Autoradiographs were scanned, and densitometry analysis was conducted in ImageJ software (Bethesda, MA, USA). Results were expressed as arbitrary units and normalized using β-actin as loading controls.
Grossi L.C., Zaidan I., Souza J.A., Carvalho A.F., Sanches R.C., Cardoso C., Lara E.S., Montuori-Andrade A.C., Bruscoli S., Marchetti M.C., Riccardi C., Teixeira M.M., Tavares L.P., Vago J.P, & Sousa L.P. (2023). GILZ Modulates the Recruitment of Monocytes/Macrophages Endowed with a Resolving Phenotype and Favors Resolution of Escherichia coli Infection. Cells, 12(10), 1403.
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9

Histone Modification Profiling in Cells

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Whole-cell protein lysates were prepared using RIPA Lysis and Extraction Buffer (Thermo Scientific, Rockford, IL) supplemented with PhosSTOP phosphatase and cOmplete, Mini, protease inhibitor cocktail (Roche Diagnostics, Indianapolis, IN). Nuclear proteins were extracted using Subcellular Protein Fractionation Kit (Thermo Scientific) according to the manufacturer’s instructions. Protein lysates were quantified with DC Protein Assay (Bio-Rad Laboratories, Hercules, CA). Equal amounts of whole-cell (30 μg) or nuclear protein extracts (20 μg) were electrophoresed and transferred onto a PVDF membrane (Bio-Rad Laboratories) under standard conditions. The following primary antibodies were used: IDH1 R132H (DIA-H09, Dianova GmbH), H3K4me3 (#39159), H3K9me2 (#39683), H3K9me3 (#39161), H3K27me3 (#39155; all from Active Motif, Carlsbad, CA), Histone H3 (ab1791, Abcam, Cambridge, MA), GAPDH (#14C10, Cell Signaling Technology, Danvers, MA). The corresponding secondary antibodies anti-mouse (sc-2005) and anti-rabbit (sc-2004) IgG-horseradish peroxidase (HRP) were from Santa Cruz Biotechnology (Dallas, TX). Antibody binding was detected using Amersham ECL Western Blotting Detection Reagent (GE Healthcare Life Sciences, Pittsburgh, PA).
Johannessen T.C., Mukherjee J., Viswanath P., Ohba S., Ronen S.M., Bjerkvig R, & Pieper R.O. (2016). Rapid Conversion of Mutant IDH1 from Driver to Passenger in a Model of Human Gliomagenesis. Molecular cancer research : MCR, 14(10), 976-983.
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10

Immunoblotting Analysis of Cellular Proteins

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Cells were lysed in CelLytic M buffer (Sigma-Aldrich) or as described by Rapizzi et al. (Rapizzi et al. 2015 (link)) and protein was quantified with the Bradford assay. Proteins were separated on 4–20% sodium dodecyl sulfate polyacrylamide gels (C.B.S. Scientific) and transferred to PVDF membranes (Fisher Scientific or Immobilon, Millipore, MA, USA). Primary antibodies against actin (MAB1510R, Millipore, or sc-1615, Santa Cruz), SDHB (ab14714, Abcam), TH (NB300–109, Novus Biologicals), phospho S40-TH (ab51206, Abcam) and MCT4 (sc-50329, Santa Cruz) were used. Secondary antibodies were obtained from Santa Cruz (anti-mouse sc-2005, anti-rabbit sc-2004, anti-goat sc-2020). Membranes were blocked with 5% fat-free milk diluted in PBS with 0.1% Tween 20. Protein bands were detected with ECL reagents (femtoLUCENT peroxide solution, G-Biosciences, or Immobilon, Millipore). Densitometry was undertaken using ImageJ software.
Richter S., D’Antongiovanni V., Martinelli S., Bechmann N., Riverso M., Poitz D.M., Pacak K., Eisenhofer G., Mannelli M, & Rapizzi E. (2018). Primary fibroblast co-culture stimulates growth and metabolism in Sdhb-impaired mouse pheochromocytoma MTT cells. Cell and tissue research, 374(3), 473-485.
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