Anti mouse igg hrp

Manufactured by Merck Group

Sourced in United States, Germany

Anti-mouse IgG-HRP is a secondary antibody conjugated with Horseradish Peroxidase (HRP). It is designed to detect and bind to primary antibodies raised against mouse immunoglobulin G (IgG).

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Lab products found in correlation

Anti rabbit igg hrp, by Merck Group (25 mentions) Anti α tubulin, by Merck Group (3 mentions) Anti human igg hrp, by Merck Group (3 mentions) Pvdf membrane, by Merck Group (3 mentions) Tmb substrate, by Thermo Fisher Scientific (3 mentions) Anti rabbit igg hrp, by Santa Cruz Biotechnology (3 mentions) Clarity western ecl substrate, by Bio-Rad (3 mentions) Anti β actin, by Merck Group (3 mentions) Protease inhibitor, by Roche (2 mentions) Bradford assay, by Bio-Rad (2 mentions) Anti flag m2, by Merck Group (2 mentions) Nitrocellulose membrane, by Bio-Rad (2 mentions) Ecl prime, by GE Healthcare (2 mentions) Immobilon pvdf membrane, by Merck Group (2 mentions) Protease inhibitor cocktail, by Merck Group (2 mentions) Anti mouse igm hrp, by Merck Group (2 mentions) Anti rabbit igg hrp, by Cell Signaling Technology (2 mentions) Nunc maxisorp plate, by Thermo Fisher Scientific (2 mentions) Goat anti mouse igg, by Southern Biotech (2 mentions) Anti rabbit igg horseradish peroxidase hrp, by Cell Signaling Technology (2 mentions)

Spelling variants of this product

HRP anti-mouse (6 citations) Anti-IgG mouse (5 citations) IgG mouse (3 citations)

85 protocols using anti mouse igg hrp

Protein Extraction and Western Blot Analysis

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Whole cells extract was isolated using RIPA buffer (NaCl 150 mM - Tris HCL pH7.35 50 mM - DOC 1% - NP40 1%) supplemented with protease inhibitor (Ref #04693116001, Roche). Concentration of isolated proteins was determined using Bradford assay (500-0006, Bio-Rad).
Western Blot analysis were performed using the following primary antibodies: anti-GATA3 (1/1000; Ozyme #5852), anti-PHOX2B (1/1000, Ozyme #PA-5115754), anti-c-JUN (1/1000, Cell Signaling #9165), anti-MAML2 (1/500, Sigma–Aldrich clone 4A1 # WH0084441M3), anti-RUNX1 (1/500, Santa Cruz SC-365644), anti-GAPDH (1/500, Sigma–Aldrich #G9545). Anti-mouse IgG HRP (1/10000, Sigma #A4416), anti-rabbit IgG HRP (1/10000, Sigma–Aldrich #A9169) and anti-goat IgG HRP (1/10000, Sigma #A5420) were used as secondary antibodies. Densitometric analyses of western blots were performed using Image J software.

Ben Amar D., Thoinet K., Villalard B., Imbaud O., Costechareyre C., Jarrosson L., Reynaud F., Novion Ducassou J., Couté Y., Brunet J.F., Combaret V., Corradini N., Delloye-Bourgeois C, & Castellani V. (2022). Environmental cues from neural crest derivatives act as metastatic triggers in an embryonic neuroblastoma model. Nature Communications, 13, 2549.

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Expression Profiling of XafT from pTLC Plasmids

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Expression profiles of XafT from either integrated or replicative forms of pTLC plasmids were performed in V. cholerae EPV369 (lacZ-dif1 reporter at the lacZ locus) by immunoblotting against XafT with C-terminal 3xFLAG epitopes. Clones harbouring integrated or replicative forms of the pTLC variants were selected on LB-agar supplemented with Cm and X-gal, with integrated forms giving rise to white colonies, and non-integrated replicative forms giving rise to blue colonies. Total cellular protein extracts were separated on precast 8–16% gradient acrylamide TGX ‘Stain-Free’ gels (Bio-Rad) in Tris-glycine–SDS electrophoresis buffer. Gels were electroblotted by wet-transfer onto nitrocellulose. The following antibodies were used for immunoprobing: 1:10 000 anti-FLAG M2 (F1804, Sigma), and 1:10 000 anti-mouse IgG-HRP (A9044, Sigma), both diluted in 5% fat-free milk TBS-T (20 mM Tris pH 7.6, 150 mM NaCl, 0.01% Tween-20). Chemiluminescence was performed using SuperSignal™ West Pico PLUS (ThermoFisher) ECL, and captured over a 60-min exposure with a ChemiDoc imager (Bio-Rad). Supplementary Figure S6 contains uncropped source images of the original SDS-PAGE, transfer, and immunoblot. Supplementary method contains an extended explanation of the plasmid construction and sample preparation used for this immunoblot.

Miele S., Provan J.I., Vergne J., Possoz C., Ochsenbein F, & Barre F.X. (2022). The Xer activation factor of TLCΦ expands the possibilities for Xer recombination. Nucleic Acids Research, 50(11), 6368-6383.

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Western Blot Analysis of Transcription Factors

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For Western blotting analysis, cells were washed twice with cold PBS and then whole cell lysates were prepared by direct lysis of cell pellets in heated 2X SDS sample buffer. Samples were resolved on 4–12% Tris-Glycine gels (Life Technologies, Carlsbad, CA) followed by transferring onto nitrocellulose membranes (Bio-Rad, Hercules, CA). Primary antibodies used include anti-Setbp1 (16841-1AP, Proteintech, Chicago, IL), anti-Myb (05–175, Millipore, Temecula, CA), anti-Hoxa9 (07–178, Millipore, Temecula, CA), and Anti-β-Actin (ab8224, Abcam, Cambridge, MA). Secondary antibodies used include goat anti-rabbit IgG-HRP (SC-2004, Santa Cruz Biotechnology, Dallas, TX) and anti-mouse IgG-HRP (A-9044, Sigma Aldrich). Protein bands were visualized by incubation with SuperSignal West chemiluminescent substrate (Pierce, Thermo Fisher Scientific, Rockford, IL) and quantified using Image Lab software (Bio-Rad, Hercules, CA).

Nguyen N., Vishwakarma B.A., Oakley K., Han Y., Przychodzen B., Maciejewski J.P, & Du Y. (2016). Myb expression is critical for myeloid leukemia development induced by Setbp1 activation. Oncotarget, 7(52), 86300-86312.

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Western Blot Quantification Protocol

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Protein concentrations were measured using the Bio-Rad Bradford protein assay. The proteins were separated by 12% SDS-polyacrylamide gel electrophoresis, transferred to IMMOBILON PVDF membranes (Millipore) and incubated overnight at 4°C in blocking buffer containing 2% ECL blocking reagent (GE Healthcare) and 0.1% Tween 20 in PBS. The membranes were probed with either anti TFPI-2 (1:500, SantaCruzBiotechnology) or anti α-tubulin (1:1000, Sigma-Aldrich) antibody for 1h at room temperature. Antibody binding was detected with anti-mouse IgG-HRP (1:10,000, Sigma Aldrich) for 45min at room temperature. The signals were detected with ECL Prime (GE-Healthcare). Densitometry of protein bands was analysed with GelPro Analyzer Software (Media Cybernetics).

Ghilardi C., Silini A., Figini S., Anastasia A., Lupi M., Fruscio R., Giavazzi R, & Bani M. (2015). Trypsinogen 4 boosts tumor endothelial cells migration through proteolysis of tissue factor pathway inhibitor-2. Oncotarget, 6(29), 28389-28400.

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Western Blot Analysis of Nrf2 Protein

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After treatment, whole cell lysates were prepared in RIPA lysis buffer containing protease inhibitors, subjected to SDS-PAGE on an 8% mini-gel and transferred to Immobilon™-P transfer membrane as previously described [33 (link)]. The membrane was blocked and cut at 75 kDa marker. The upper part of membrane was incubated with 1 µg/mL anti-Nrf2 antibody (R&D Systems Tools for Cell Biology Research) [72 (link)] and the bottom part of membrane was incubated with anti-α tubulin (Sigma) as a loading control at a 1:10,000 dilution for overnight in a 4 °C cold room. After three consecutive washes with TBS plus 0.1% Tween 20 (10 min for each), the membranes were incubated with 1:10,000 secondary antibody (anti-mouse IgG-HRP, Sigma) for 1 h at room temperature. Prestained SDS-PAGE protein standards (Bio-Rad, Hercules, CA, USA) were used to determine the size of detected proteins. Proteins were visualized by chemiluminescence with SuperSignal West Pico (Pierce, Grand Island, NY, USA) and exposed to X-ray film.

Wang Q., Chuikov S., Taitano S., Wu Q., Rastogi A., Tuck S.J., Corey J.M., Lundy S.K, & Mao-Draayer Y. (2015). Dimethyl Fumarate Protects Neural Stem/Progenitor Cells and Neurons from Oxidative Damage through Nrf2-ERK1/2 MAPK Pathway. International Journal of Molecular Sciences, 16(6), 13885-13907.

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Rspo1 Knockdown Protocol Using shRNA

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Short hairpin RNA (shRNA) directed against Rspo1 was purchased from Thermo (U.S.). The Rspo1 shRNA1 target sequence was 5^′-TACACTTGGTGCAGAAGTT-3^′, the Rspo1 shRNA2 target sequence was 5^′-TGCACTTGTTCATGTCGGG-3^′, and the nonsense shRNA sequence was 5^′-TACGCATCCGCAACTGCAG-3^′. The rabbit anti-Rspo1 antibodies used for Western blotting, immunoprecipitation and immunohistochemical assays were purchased from Abcam. The mouse anti-β-actin antibodies used for the immunoblotting assay were purchased from Sigma. The secondary antibodies anti-mouse IgG-HRP and anti-rabbit IgG-HRP were purchased from Sigma.

Gu X., Wang X., Xiao H., Ma G., Cui L., Li Y., Zhou H., Liang W., Zhao B, & Li K. (2015). Silencing of R-Spondin1 increases radiosensitivity of glioma cells. Oncotarget, 6(12), 9756-9765.

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Quantitative ELISA for Antibody Titration

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MaxiSORP 96-well plates (Nunc, Roskilde, Denmark) were coated with 50 μL/well of 0.5-μg/mL recombinant protein and incubated overnight at 4 °C. Plates were washed 7 times with PBS 0.05% Tween-20 (PBS-T) and blocked with 100 μL of 1% bovine serum albumin (BSA) 0.3% Tween-20 (B-PBS-T) at 37 °C for 1 h. One hundred microlitres of serum dilutions in B-PBS-T were added to the plates and incubated at 37 °C for 2 h. The plates were washed 7 times and 100-μL anti-mouse IgG-HRP (Sigma, St. Louis, MO, USA, A9044, diluted 1/20,000), or anti-human IgG-HRP (Sigma, St. Louis, MO, USA, A8792, diluted 1/5000) was added to the plates and incubated at 37 °C for 1 h. The plates were washed 7 times, and 100-μL TMB substrate (3,3′,5,5′-tetramethylbenzidine, Thermo Fisher Scientific, Waltham, MA, USA) was added and incubated at RT for 15 min, and the reaction was stopped with 100 μL of 1-M sulphuric acid. The plates were read at 450 nm on a SoftMax Pro plate reader. The antibody titre was determined as the serum dilution giving an OD 0.5 using the interpolation of a sigmoidal curve in GraphPad Prism.

Shaw H.A., Ozanne J., Burns K, & Mawas F. (2021). Multicomponent Vaccines against Group A Streptococcus Can Effectively Target Broad Disease Presentations. Vaccines, 9(9), 1025.

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Immunoblotting Reagents and Protocols

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MAM was purchased from Midwestern Research Institute (Kansas City, MO, USA). Fluriso™ (Isoflurane, USP) was purchased from MWI Animal Health (Boise, ID, USA). Chloral hydrate, protease inhibitor cocktail (P8340) and anti-mouse IgG-HRP (A4416) was sourced from Sigma-Aldrich (St. Louis, MO, USA). Alexa Fluor® 594 goat anti-rabbit IgG (A11012) and ProLong® Gold antifade reagent with DAPI (P36931) were purchased from Life Technologies (USA). Anti-Parvalbumin antibody (Rb pAb to PV; abll427), Anti-GAPDH antibody (Ms mAb to GAPDH; ab9484) and goat pAb to Rb IgG-HRP (ab6721) were purchased from Abeam (Cambridge, MA, USA). Laemmli sample buffer (#161-0737), 10× Tris/glycine/SDS buffer (#161-0732), Mini-Protean TGX Any kD gels (#456-9035) and nitrocellulose/filter paper sandwiches, 0.2μm (#162-0213) were purchased from Bio-Rad (California, USA). Pierce ECL western blotting substrate (#32106) and Restore western blot stripping buffer (#21059) were purchased from Thermo Fisher Scientific (USA). High-performance chemiluminescence film (Amersham hyperfilm ECL; 28906839) was purchased from GE Healthcare. All other chemicals and reagents were of either analytical or laboratory grade, and purchased from standard suppliers.

Perez S.M., Donegan J.J, & Lodge D.J. (2019). Effect of estrous cycle on schizophrenia-like behaviors in MAM exposed rats. Behavioural brain research, 362, 258-265.

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Immunodetection of FLAG-tagged Proteins

Cited 1 time

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Overnight cultures were back-diluted 1:100 and grown in LB at 30˚C for 6h. Lysates were prepared by suspending harvested cells in an appropriate volume of 2x Laemmli buffer (100 μL buffer per O.D. unit) and boiling at 95˚C for 15 min. Proteins were resolved by SDS-PAGE, blotted onto PVDF membranes using a wet-transfer apparatus and immuno-detection was performed as described previously [54 (link)]. Primary anti-FLAG antibodies (Monoclonal ANTI-FLAG M2, Sigma; Cat# F1804) were used at a dilution of 1:2000. Anti-Mouse IgG HRP (Sigma; Cat# A5278) diluted 1:5000 was used as a secondary antibody. Sample loading was verified with Direct-Blot HRP anti-E. coli RNA Sigma70 (BioLegend; Cat# 663205) diluted 1:10,000.

Adams D.W., Pereira J.M., Stoudmann C., Stutzmann S, & Blokesch M. (2019). The type IV pilus protein PilU functions as a PilT-dependent retraction ATPase. PLoS Genetics, 15(9), e1008393.

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Protein-Lipid Interaction Screening

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Overlay assays were carried out using His-tagged fragments of Tks4 (PX–SH3₁, PX–SH3₂, PX–PRR, and PX–SH3₃). PIP strips were purchased from Echelon (catalog number: P-6001). All experiments were carried out according to the manufacturer’s instructions. Briefly, the strips were blocked in TBS-T (0.1% v/v TWEEN 20) with 3% fatty acid-free BSA (Sigma-Aldrich, St. Louis, MO, USA, A-6003) for 1 h at ambient temperature. The membrane was incubated with 10 ug/mL of the given protein for 1 h at room temperature, and then washed three times over 30 min with gentle agitation. The bound protein was detected via a 1-h incubation with anti-His antibody (Millipore, Burlington, MA, USA, 05-949). Following a washing step, the membranes were incubated with anti-mouse IgG-HRP (Sigma-Aldrich A-9044) for 1 h prior to detection of bound proteins using enhanced chemiluminescence.

Merő B., Koprivanacz K., Cserkaszky A., Radnai L., Vas V., Kudlik G., Gógl G., Sok P., Póti Á.L., Szeder B., Nyitray L., Reményi A., Geiszt M, & Buday L. (2021). Characterization of the Intramolecular Interactions and Regulatory Mechanisms of the Scaffold Protein Tks4. International Journal of Molecular Sciences, 22(15), 8103.

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