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Horse anti mouse

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Horse anti-mouse is a laboratory reagent used in immunochemical techniques. It is a polyclonal antibody produced in horses that specifically recognizes mouse immunoglobulins. This product is intended for use as a detection or capture agent in various immunoassay applications.

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Lab products found in correlation

Goat anti rabbit, by Thermo Fisher Scientific (3 mentions) Vectastain abc kit, by Vector Laboratories (2 mentions) Goat anti rabbit, by Cell Signaling Technology (1 mentions) Mouse monoclonal anti th, by Merck Group (1 mentions) Actin, by Merck Group (1 mentions) Kaleidoscope prestained standard, by Bio-Rad (1 mentions) Alexa fluor 594 donkey anti goat igg, by Thermo Fisher Scientific (1 mentions) Alexa fluor 488 donkey anti rabbit igg h l, by Thermo Fisher Scientific (1 mentions) Mouse anti cd68, by Abcam (1 mentions) Rabbit anti ferritin, by Abcam (1 mentions) Goat anti iba1, by Abcam (1 mentions) 4 6 diamidino 2 phenylindole (dapi), by Merck Group (1 mentions) Mouse anti th, by Immunostar (1 mentions) Dpx mounting medium, by Merck Group (1 mentions) Rabbit anti th, by Merck Group (1 mentions) Goat anti mouse, by Vector Laboratories (1 mentions) Sm2010r, by Leica camera (1 mentions) Abc elite, by Vector Laboratories (1 mentions) Protease and phosphatase inhibitor cocktail, by Merck Group (1 mentions) Rabbit anti fibronectin, by Abcam (1 mentions)

11 protocols using horse anti mouse

1

Membrane Protein Analysis in Oocytes

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Crude membrane fractions were isolated from oocytes (Bröer, 2003 (link)). Protein samples(40 μg), separated on a 4-15% gradient SDS gel, and transferred to nitrocellulose paper, were probed overnight at 4°C with primary antibody as indicated: we used chicken anti-Slack IgY (1:5000 (Bhattacharjee et al., 2002 (link))), rabbit anti-Na+/K+ ATPase IgG (1:1000; #3010, Cell Signaling), and horse anti-mouse (#PI-2000, Vector Labs) or goat anti-rabbit (#7074, Cell Signaling) HRP-conjugated secondary antibodies. Densitometry values from developed and imaged blots were determined using ImageJ.
Kim G.E., Kronengold J., Barcia G., Quraishi I.H., Martin H.C., Blair E., Taylor J.C., Dulac O., Colleaux L., Nabbout R, & Kaczmarek L.K. (2014). Human Slack potassium channel mutations increase positive cooperativity between individual channels. Cell reports, 9(5), 1661-1672.
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2

Immunohistochemical Analysis of Dopaminergic Neurons

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Rats processed for immunohistochemistry were perfused with 0.9% saline and then with cold 4% paraformaldehyde in 0.1 M phosphate buffer, pH 7.4. The brain was removed and then washed and cryoprotected in the same buffer containing 20% sucrose. Brains were then cut into 40 μm sections on a freezing microtome. The sections were incubated for 1 h in 10% normal swine serum with 0.25% Triton X-100 in 20 mM potassium phosphate-buffered saline, containing 1% bovine serum albumin (KPBS-BSA), and subsequently incubated overnight (at 4 °C) with anti-tyrosine hydroxylase (TH) as the dopaminergic marker (mouse monoclonal anti-TH, Sigma-Aldrich Cat# T2928, RRID: AB_477569; 1:10,000). Sections were then incubated with the corresponding biotinylated secondary antibody (horse anti-mouse, Vector Laboratories, Inc., Newark, CA, USA; Cat# BA-2001, RRID: AB_2336180; 1:200) for 60 min, and then with an avidin–biotin–peroxidase complex (ABC, 1:100, Vector) for 90 min. Finally, sections were revealed with 0.04% hydrogen peroxide and 0.05% 3-3′diaminobenzidine (DAB, D5637, Sigma-Aldrich). All experiment control sections in which the primary antibody was omitted were immune-negative for TH.
Lopez-Lopez A., Valenzuela R., Rodriguez-Perez A.I., Guerra M.J., Labandeira-Garcia J.L, & Muñoz A. (2023). Interactions between Angiotensin Type-1 Antagonists, Statins, and ROCK Inhibitors in a Rat Model of L-DOPA-Induced Dyskinesia. Antioxidants, 12(7), 1454.
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3

Protein Expression Analysis of egr1 by Western Blot

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Tissue prepared for BDNF ELISA assays was additionally used for egr1 western blot analyses. 40ug of protein was separated on an 8% gel along with a Kaleidoscope-prestained standard (Bio-Rad, Hercules, CA). Blots were incubated in primary antibody (egr1 1:400, Cell Signaling, Danvers, MA; actin 1:20,000, Millipore, Billerica, MA) for 12-16 hours at 4°C. Secondary antibody incubations were performed at room temperature in blocking buffer for 1 hour (horseradish peroxidase-linked IgG conjugated goat anti-rabbit 1:2500 for egr1, or horse anti-mouse 1:30,000 for actin, Vector Laboratories, Burlingame, CA). Membranes were visualized with Western Lightning Chemiluminescence solution (Perkin Elmer Life Science, Boston, MA). Optical density from films was analyzed using NIH Image (NIH, Bethesda, MD).
Kabir Z.D., Kennedy B., Katzman A., Lahvis G, & Kosofsky B.E. (2014). Effects of prenatal cocaine exposure on social development in mice. Developmental neuroscience, 36(0), 338-346.
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4

Immunohistochemistry and Immunofluorescence Staining Protocols

Cited 1 time
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The protocols of immunohistochemistry and immunofluorescence staining have been described previously(Xi et al., 1999 (link), Wan et al., 2020 (link)). The primary antibodies were rabbit anti-heme oxygenase-1 (HO-1, 1:400 dilution; Enzo, New York, NY), goat anti-Iba1 (1:400 dilution; Abcam, Cambridge, MI), mouse anti-CD68 (1:200 dilution; Abcam), rabbit anti-ferritin (1:200 dilution; Abcam). Negative controls were conducted by omitting the primary antibody. Secondary antibodies were horse anti-mouse (1:500 dilution, Vector Laboratories Inc, Burlingame, CA), goat anti-rabbit (1:500 dilution, Invitrogen, Eugene, OR), rabbit anti-goat (1:500 dilution, Invitrogen), Alexa Fluor 594 donkey anti-goat IgG (1:500 dilution; Invitrogen), Alexa Fluor 488 donkey anti-rabbit IgG (H+L) (1:500 dilution; Invitrogen). Nuclei were stained with 4′, 6-diamidino-2-phenylindole (DAPI) (Sigma-Aldrich, St. Louis, MO) in immunofluorescence studies and hematoxylin for immunohistochemistry.
Ye F., Hua Y., Keep R.F., Xi G, & Garton H.J. (2021). CD47 Blocking Antibody Accelerates Hematoma Clearance and Alleviates Hydrocephalus After Experimental Intraventricular Hemorrhage. Neurobiology of disease, 155, 105384.
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5

Immunohistochemical Staining Protocol for Dopaminergic Neurons

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The left hemispheres of the dissected brains were sectioned coronally on a freezing microtome (Leica SM2010R) at 40 μm. Immunohistochemical stainings were performed on free-floating sections. The SNpc sections, were given an initial antigen-retrieval incubation in Tris/EDTA (pH 9.0) at 80 °C for 45 min. All the sections were quenched with 3% H2O2/10% MetOH for 30 min then blocked with 5% Normal Horse Serum (NHS) for SNpc and Normal Goat Serum29 (link) for Striatum before overnight RT incubation with primary antibody (mouse anti-TH 1:10000 for SNpc, Immunostar, Wisconsin for SNpc; rabbit anti-TH 1:4000, Millipore, California for Striatum). On the second day, sections were incubated with the corresponding biotinylated secondary antibody (horse anti-mouse 1:200; goat anti-mouse 1:200, Vector Laboratories) for 1 h at RT. This was followed by a 30-min incubation with an avidin-biotin peroxidase solution (ABC Elite, Vector Laboratories), and the antigen was visualized using 3,3-diaminobenzidine (DAB) as a chromogen. Sections were mounted on glass slides, dehydrated with increasing concentrations of ethanol and pure xylene, and finally coverslipped using DPX mounting medium (Sigma-Aldrich, Gillingham). Sections with uneven, blurry, not penetrating staining were excluded from analyses.
Kurowska Z., Jewett M., Brattås P.L., Jimenez-Ferrer I., Kenéz X., Björklund T., Nordström U., Brundin P, & Swanberg M. (2016). Identification of Multiple QTLs Linked to Neuropathology in the Engrailed-1 Heterozygous Mouse Model of Parkinson’s Disease. Scientific Reports, 6, 31701.
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6

Western Blot Analysis of Signaling Proteins

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Cells were lysed in RIPA buffer complemented with phosphatase and protease inhibitor cocktails (Sigma) for protein extraction. Protein concentrations were determined by Bradford assays, and ~ 30 μg per sample was used for Western blotting. For non-phosphorylated protein detection, membranes were blocked and antibodies were added in 5 % milk tris-buffered saline with 0.1 % Tween 20 (TBST), and for phosphorylated protein detection, 5 % bovine serum albumin (BSA) TBST was used. Membranes were incubated with primary antibodies at 4 °C overnight and then with secondary antibody at room temperature for one hour. Primary antibodies: 1:1000 mouse anti-SMA (Sigma, A5228), 1:1000 rabbit anti-phospho-Ser 465/467 SMAD2 (pSMAD2) (Cell Signaling, 3108), 1:1000 rabbit anti-phospho-Ser 423/425 SMAD3 (pSMAD3) (Millipore, 0713-89), 1:1000 rabbit anti-SMAD2 (Cell Signaling, 5339), 1:1000 rabbit anti-SMAD2/3 (Cell Signaling, 8685), 1:1000 rabbit anti-fibronectin (Abcam, ab2413), 1:1000 rabbit anti-bFGF (Sigma), 1:1000 rabbit anti-phospho-Thr 202/204 ERK (pERK) 1/2 (Cell Signaling, 4370), 1:2000 rabbit anti-ERK1/2 (Cell Signaling, 9102), 1:1000 rabbit anti-VEGF receptor 2 (VEGFR2) (Cell Signaling, 55B11), and 1:2500 rabbit anti-GAPDH (Cell Signaling, 5174). Secondary HRP-conjugated antibodies: 1:10,000 horse anti-mouse and 1:10,000 goat anti-rabbit antibodies (Vector Laboratories).
Xiao L., Kim D.J., Davis C.L., McCann J.V., Dunleavey J.M., Vanderlinden A., Xu N., Pattenden S.G., Frye S.V., Xu X., Onaitis M., Monaghan-Benson E., Burridge K, & Dudley A.C. (2015). Tumor endothelial cells with distinct patterns of TGFβ-driven endothelial-to-mesenchymal transition. Cancer research, 75(7), 1244-1254.
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7

Multiplex Immunofluorescence Staining for CD4+ and CD8+ T Cells

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All specimens were sectioned into 5 μm sections from formalin-fixed, paraffin-embedded tissue. Sections were dewaxed in xylene and rehydrated using serial ethanol baths in decreasing concentrations. Specimens were histopathologically evaluated with conventional hematoxylin and eosin (H&E) staining. Further evaluation was performed via immunofluorescence staining. Antigen retrieval was performed with citrate buffer pH 6 (Agilent Dako) in a pressure cooker (BioCare Medical) programmed at 110°C for 15 min. Sections were incubated with primary antibodies rabbit-anti-human CD4 (Novus Biologicals) at 1:200 and mouse-anti-human CD8 (Abcam) at 1:50 overnight at 4°C. Afterward, biotinylated secondary antibodies goat-anti-rabbit (Vector) and horse-anti-mouse (Vector) were both incubated at 1:200 for 1 h at room temperature followed by Streptavidin-AF546 conjugate (Invitrogen) and Streptavidin-AF647 conjugate (Invitrogen), respectively, for 30 min at room temperature. Sections were mounted with ProLong Gold Antifade Reagent with DAPI (Invitrogen) and coverslipped. Immunofluorescence-stained sections were photographed using a fluorescence microscope (EVOS FL Auto 2, Invitrogen) and processed with ImageJ software.
Borges T.J., Abarzua P., Gassen R.B., Kollar B., Lima-Filho M., Aoyama B.T., Gluhova D., Clark R.A., Islam S.A., Pomahac B., Murphy G.F., Lian C.G., Talbot S.G, & Riella L.V. (2022). T cell-attracting CCL18 chemokine is a dominant rejection signal during limb transplantation. Cell Reports Medicine, 3(3), 100559.
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8

Immunostaining for Viral Antigen in CNS

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Brains and spinal cords from PBS-perfused mice were fixed with 10% neutral zinc-buffered formalin and embedded in paraffin. Sections were stained with either haematoxylin & eosin or luxol fast blue (LFB) to determine inflammation and myelin integrity, respectively, as described previously.9 (link) Distribution of viral antigen was determined by immunoperoxidase staining (Vectastain-ABC kit; Vector Laboratory, Burlingame, CA) using the anti-JHMV mAb J3.3 specific for the C-terminus of the viral N protein as the primary antibody, and horse anti-mouse as the secondary antibody (Vector Laboratory) as described elsewhere.9 (link),16 (link),17 (link)
Hwang M., Phares T.W., Hinton D.R., Stohlman S.A., Bergmann C.C, & Min B. (2015). Distinct CD4 T-cell effects on primary versus recall CD8 T-cell responses during viral encephalomyelitis. Immunology, 144(3), 374-386.
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9

Immunohistochemical Analysis of HO-1, MSR1, and MBP

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Immunohistochemistry staining was performed as described previously23 (link). In brief, the sections were deparaffinized in xylene and rehydrated in a graded series of alcohol dilutions. Antigen retrieval was performed by the microwave method with citrate buffer (10 mmol/L, pH 6.0). Immunohistochemistry studies were performed with avidin-biotin complex techniques. The primary antibodies were polyclonal rabbit anti-heme oxygenase-1 (HO-1, Enzo, ADI-SPA-895-F, 1:400 dilution), rabbit anti-macrophage scavenger receptor 1 (MSR1) (NOVUS, NBP1–00092, 1:200 dilution), and mouse anti-myelin basic protein (MBP) (Abcam, ab62631, 1:1000 dilution). Secondary antibodies were horse anti-mouse (1:500 dilution, Vector Laboratories Inc.) and goat anti-rabbit (1:500 dilution, Invitrogen). Eliminating primary antibodies were used as negative controls.
Chen J., Koduri S., Dai S., Toyota Y., Hua Y., Chaudhary N., Pandey A.S., Keep R.F, & Xi G. (2020). Intra-hematomal white matter tracts act as a scaffold for macrophage infiltration after intracerebral hemorrhage. Translational stroke research, 12(5), 858-865.
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10

Western Blot Protein Detection

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Cells were lysed with NP40 cell lysis buffer supplemented with protease inhibitor cocktail (P2714, Sigma-Aldrich). Cells were centrifuged for 15 min at 12,000g at 4°C. Supernatant was saved and kept frozen until further use. DC protein assay (Bio-Rad) was used to quantify protein. The cell lysate was placed in SDS sample buffer and run in a precasted gel at 100 V. Proteins were transferred into nitrocellulose using the trans-Blot turbo (Bio-Rad). Primary antibodies are described above. Secondary antibodies were goat anti-Rb horseradish peroxidase (1:10,000; Abcam, ab6721) and horse anti-mouse (VectorLabs, PI-2000-1). Detection was performed using SuperSignal Atto (Thermo Fisher Scientific) using a G box documentation system (Syngene).
Cortes D.E., Escudero M., Korgan A.C., Mitra A., Edwards A., Aydin S.C., Munger S.C., Charland K., Zhang Z.W., O'Connell K.M., Reinholdt L.G, & Pera M.F. (2024). An in vitro neurogenetics platform for precision disease modeling in the mouse. Science Advances, 10(14), eadj9305.
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