goat anti mouse igg hrp  (Santa Cruz Biotechnology)

 
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    goat anti mouse IgG HRP
    Description:
    supplied at 200 µg in 0 5 ml volume horseradish peroxidase conjugated secondary antibody recommended for use in Western blotting at a dilution of 1 500 1 10000 Starting dilution 1 2000
    Catalog Number:
    SC-2005
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    Category:
    Antibodies Conventional Secondary IgGs goat anti mouse IgG HRP
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    Structured Review

    Santa Cruz Biotechnology goat anti mouse igg hrp
    supplied at 200 µg in 0 5 ml volume horseradish peroxidase conjugated secondary antibody recommended for use in Western blotting at a dilution of 1 500 1 10000 Starting dilution 1 2000
    https://www.bioz.com/result/goat anti mouse igg hrp/product/Santa Cruz Biotechnology
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    goat anti mouse igg hrp - by Bioz Stars, 2021-04
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    Article Title: The transcription factor c-Myb regulates CD8+ T cell stemness and antitumor immunity
    Article Snippet: .. Immunoblot analysis Proteins were separated by 4–12% SDS-PAGE, followed by standard immunoblot analysis with anti-Myb (Millipore, clone 1–1), anti-GAPDH (6C5; Santa Cruz Biotechnology), horseradish peroxidase–conjugated goat anti–mouse IgG (sc-2031; Santa Cruz Biotechnology) and horseradish peroxidase–conjugated goat anti–rabbit IgG (sc-2030; Santa Cruz Biotechnology). ..

    Western Blot:

    Article Title: Towards the development of an enzyme replacement therapy for the metabolic disorder propionic acidemia
    Article Snippet: Gels were subsequently stained with InstantBlue™ (Expedeon Ltd., Cambridge, UK) to visualize the protein bands. .. Western blot analysis was performed using anti-PCCB mouse polyclonal (I-DNA Biotechnology Pte-Ltd., Singapore, Singapore), anti-PCCA chicken polyclonal (Sigma-Aldrich, St. Louis, MO) and anti-E1α (Invitrogen, Carlsbad, CA) as primary antibodies and anti-mouse HRP conjugated IgG (goat), and anti-chicken HRP conjugated IgG (bovine) (Santa Cruz Biotechnology, Santa Cruz, CA) as secondary antibodies at 1:1000 dilutions. .. Densitometric analysis of western blot's bands of target PCC subunits was conducted using National Institutes of Health (NIH) ImageJ 1.47 software.

    Enzyme-linked Immunosorbent Assay:

    Article Title: Modular adeno-associated virus (rAAV) vectors used for cellular virus-directed enzyme prodrug therapy
    Article Snippet: Unspecific binding was blocked using 0.8% BSA/PBS for 1 h. Subsequently, cells were incubated with 1.8 × 109 viral particles for 2 h. Unbound capsids were removed via washing twice with PBS/0.05% Tween 20 (v/v). .. Intact rAVVs were detected as described under ELISA using a HRP-coupled anti-mouse antibody (sc-2005, SantaCruz, dilution 1:3,000) to detect bound A20 antibodies. .. Caspase 3/7 assay In order to assess apoptosis induction, 2,000 A431 or HeLa cells, respectively, were seeded per well of a 96 well culture plate and transduced with 3 × 108 genomic viral particles on day one.

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    Santa Cruz Biotechnology hrp conjugated goat anti mouse antibody
    <t>PKCε</t> in rat brain extract. (A) 15 µg of rat brain extract was separated on a SDS-PAGE gel. PKCε was detected with anti-PKCε and <t>HRP-conjugated</t> goat anti-mouse antibodies. (B) Immunoprecipitations were performed with rat brain extract using a commercial anti-PKCε antibody (IgG Ab) and VHHs. PKCε (marked with an arrowhead) is visible at 90 kDa on lane 1. The bands at 55 kDa and 25 kDa on lane 1 represent the heavy and light chains of the anti-PKCε antibody. The bands at 16 kDa for A10, C1, D1, E6 and G8 represent the VHHs. A sample of uncoated protein A sepharose beads was included as a negative control (lane 2 = ctrl).
    Hrp Conjugated Goat Anti Mouse Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hrp conjugated goat anti mouse antibody/product/Santa Cruz Biotechnology
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    hrp conjugated goat anti mouse antibody - by Bioz Stars, 2021-04
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    99
    Santa Cruz Biotechnology horseradish peroxidase hrp conjugated anti rabbit igg
    Exposure to apoptotic thymocytes induces transient tyrosine phosphorylation of MerTK. A, B. Immunoprecipitation using antibody against phosphotyrosine (anti-pTyr). Equal numbers of PMø (A) or J774 (B) were incubated with a 10-fold greater number of apoptotic thymocytes for the indicated time (in minutes), washed extensively, and then lysed in RIPA buffer. After preclearing, Mø lysates were immunoprecipitated using anti-pTyr antibody and then immunoblotted using goat anti-MerTK. After incubation with <t>HRP-conjugated</t> donkey anti-goat <t>IgG</t> in Tween-PBS containing 5% milk, signal was detected by chemiluminescence. C', control; Thy, thymocytes (10 7 ) alone. Similar results were seen in an independent experiment of this design using each Mø cell type. C. Immunoprecipitation using goat antibody against MerTK. PMø were incubated with apoptotic thymocytes for the indicated time, washed extensively, and then lysed in RIPA buffer. After preclearing, Mø lysates were immunoprecipitated using goat antibody against MerTK, and then immunoblotted using anti-pTyr antibody. After incubation with HRP-conjugated donkey anti-rabbit IgG in BSA, signal was detected by chemiluminescence. The membrane was then stripped and reblotted using goat antibody against MerTK to demonstrate loading. Similar results were seen in four independent experiments of this design using PMø.
    Horseradish Peroxidase Hrp Conjugated Anti Rabbit Igg, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/horseradish peroxidase hrp conjugated anti rabbit igg/product/Santa Cruz Biotechnology
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    PKCε in rat brain extract. (A) 15 µg of rat brain extract was separated on a SDS-PAGE gel. PKCε was detected with anti-PKCε and HRP-conjugated goat anti-mouse antibodies. (B) Immunoprecipitations were performed with rat brain extract using a commercial anti-PKCε antibody (IgG Ab) and VHHs. PKCε (marked with an arrowhead) is visible at 90 kDa on lane 1. The bands at 55 kDa and 25 kDa on lane 1 represent the heavy and light chains of the anti-PKCε antibody. The bands at 16 kDa for A10, C1, D1, E6 and G8 represent the VHHs. A sample of uncoated protein A sepharose beads was included as a negative control (lane 2 = ctrl).

    Journal: PLoS ONE

    Article Title: Kinetics of PKC? Activating and Inhibiting Llama Single Chain Antibodies and Their Effect on PKC? Translocation in HeLa Cells

    doi: 10.1371/journal.pone.0035630

    Figure Lengend Snippet: PKCε in rat brain extract. (A) 15 µg of rat brain extract was separated on a SDS-PAGE gel. PKCε was detected with anti-PKCε and HRP-conjugated goat anti-mouse antibodies. (B) Immunoprecipitations were performed with rat brain extract using a commercial anti-PKCε antibody (IgG Ab) and VHHs. PKCε (marked with an arrowhead) is visible at 90 kDa on lane 1. The bands at 55 kDa and 25 kDa on lane 1 represent the heavy and light chains of the anti-PKCε antibody. The bands at 16 kDa for A10, C1, D1, E6 and G8 represent the VHHs. A sample of uncoated protein A sepharose beads was included as a negative control (lane 2 = ctrl).

    Article Snippet: The blot was probed with 1∶1000 dilution of mouse anti-PKCε antibody (BD Biosciences, NJ), followed by a 1∶4000 dilution of HRP-conjugated goat anti-mouse antibody (Santa Cruz Biotechnology, CA).

    Techniques: SDS Page, Negative Control

    TLR3 modulates early CHIKV-specific IgG response in mice WT and Tlr3 −/− mice ( n = 6 per group) were infected with CHIKV (10 6 PFU) by joint footpad inoculation. A, B Total CHIKV-specific IgM (A) and IgG (B) levels were determined from serum samples collected at 0, 3, 6, 9, 12 and 15 dpi at a dilution of 1:100 and 1:2,000, respectively, using purified CHIKV virion-based ELISA. Data are representative of two independent experiments and presented as mean ± SD (two-tailed Mann–Whitney U -test, ** P = 0.0087 6 dpi IgG). C, D Neutralizing capacity of pooled sera collected at 6 dpi (C) and 15 dpi (D) from WT mice is significantly higher than from Tlr3 −/− mice. Pooled sera were diluted 1:50–1:5,000 and mixed with CHIKV (MOI 10) for 2 h before infection of HEK 293T cells for 6 h. Assays were performed in quintuplicate, and data are expressed relative to virus-only-infected samples without sera. Dotted line indicates the detection limit of assay determined from mock-infected samples. Data are representative of two independent experiments and presented as mean ± SD (two-tailed Mann–Whitney U -test, ** P = 0.0079 6 dpi 1:500 serum dilution, ** P = 0.0079 6 dpi 1:5,000 serum dilution, * P = 0.0286 15 dpi 1:50 serum dilution, * P = 0.0286 15 dpi 1:500 serum dilution, * P = 0.0286 15 dpi 1:5,000 serum dilution). E, F Mapping antibody reactivity to linear B-cell epitopes within CHIKV E2 proteome. CHIKV E2 epitopes recognized at 6 dpi (E) and 15 dpi (F) were determined in pooled sera collected from infected mice using ELISA specific for overlapping 18-mer linear peptides spanning the CHIKV E2 proteome. The peptide numbers correspond to the position of the 18-mer linear peptides along the CHIKV E2 proteome. Structural data were retrieved from PDB (id: 3N44 and 2XFB) and visualized using the software CHIMERA (Pettersen et al , 2004 ). Assays were performed in triplicate and expressed as relative fold change after normalizing to OD 450 from non-infected sera. Data are representative of two independent experiments and presented as mean ± SD (two-tailed unpaired t -test, * P = 0.0191 6 dpi epitope 381, * P = 0.038 6 dpi epitope E2EP3, *** P = 0.0004 15 dpi epitope 381, *** P = 0.0001 15 dpi epitope E2EP3). G Localization of identified CHIKV B-cell epitopes (381; blue, 388; green, E2EP3; red) within CHIKV proteome. Epitopes in the E2 glycoprotein were located based on the structural data obtained from PDB records: 3N42. Number corresponds to the region of amino acid sequences in our overlapping 18-mer linear peptides library, along the CHIKV viral genome. All representations are shown in frontal and back view.

    Journal: EMBO Molecular Medicine

    Article Title: Loss of TLR3 aggravates CHIKV replication and pathology due to an altered virus-specific neutralizing antibody response

    doi: 10.15252/emmm.201404459

    Figure Lengend Snippet: TLR3 modulates early CHIKV-specific IgG response in mice WT and Tlr3 −/− mice ( n = 6 per group) were infected with CHIKV (10 6 PFU) by joint footpad inoculation. A, B Total CHIKV-specific IgM (A) and IgG (B) levels were determined from serum samples collected at 0, 3, 6, 9, 12 and 15 dpi at a dilution of 1:100 and 1:2,000, respectively, using purified CHIKV virion-based ELISA. Data are representative of two independent experiments and presented as mean ± SD (two-tailed Mann–Whitney U -test, ** P = 0.0087 6 dpi IgG). C, D Neutralizing capacity of pooled sera collected at 6 dpi (C) and 15 dpi (D) from WT mice is significantly higher than from Tlr3 −/− mice. Pooled sera were diluted 1:50–1:5,000 and mixed with CHIKV (MOI 10) for 2 h before infection of HEK 293T cells for 6 h. Assays were performed in quintuplicate, and data are expressed relative to virus-only-infected samples without sera. Dotted line indicates the detection limit of assay determined from mock-infected samples. Data are representative of two independent experiments and presented as mean ± SD (two-tailed Mann–Whitney U -test, ** P = 0.0079 6 dpi 1:500 serum dilution, ** P = 0.0079 6 dpi 1:5,000 serum dilution, * P = 0.0286 15 dpi 1:50 serum dilution, * P = 0.0286 15 dpi 1:500 serum dilution, * P = 0.0286 15 dpi 1:5,000 serum dilution). E, F Mapping antibody reactivity to linear B-cell epitopes within CHIKV E2 proteome. CHIKV E2 epitopes recognized at 6 dpi (E) and 15 dpi (F) were determined in pooled sera collected from infected mice using ELISA specific for overlapping 18-mer linear peptides spanning the CHIKV E2 proteome. The peptide numbers correspond to the position of the 18-mer linear peptides along the CHIKV E2 proteome. Structural data were retrieved from PDB (id: 3N44 and 2XFB) and visualized using the software CHIMERA (Pettersen et al , 2004 ). Assays were performed in triplicate and expressed as relative fold change after normalizing to OD 450 from non-infected sera. Data are representative of two independent experiments and presented as mean ± SD (two-tailed unpaired t -test, * P = 0.0191 6 dpi epitope 381, * P = 0.038 6 dpi epitope E2EP3, *** P = 0.0004 15 dpi epitope 381, *** P = 0.0001 15 dpi epitope E2EP3). G Localization of identified CHIKV B-cell epitopes (381; blue, 388; green, E2EP3; red) within CHIKV proteome. Epitopes in the E2 glycoprotein were located based on the structural data obtained from PDB records: 3N42. Number corresponds to the region of amino acid sequences in our overlapping 18-mer linear peptides library, along the CHIKV viral genome. All representations are shown in frontal and back view.

    Article Snippet: Separately, HRP-conjugated goat anti-mouse IgM (Santa Crus, cat# sc-2064) or IgG (Santa Cruz, cat# sc-2005) were used to detect mouse antibodies bound to virus-coated wells.

    Techniques: Mouse Assay, Infection, Purification, Enzyme-linked Immunosorbent Assay, Two Tailed Test, MANN-WHITNEY, Software

    EZH2 and β-catenin are novel target genes of FOXN1. Quantitative chromatin immunoprecipitation experiment was performed in (A) A549 or (B) H1299 cells using an antibody against FOXN1 or normal IgG (negative control). The binding of FOXN1 on EZH2 and β-catenin promoters were measured. A549 or H1299 cells were transfected with EZH2 or β-catenin promoter luciferase constructs along with (C) FOXN1 silencing molecules or NC shRNA, or (D) FOXN1 overexpression construct or pcDNA3.1 plasmids. The luciferase activities were measured and normalized to those of Renilla . Values are represented as the mean ± standard deviation of three independent experiments. *P

    Journal: Oncology Letters

    Article Title: Forkhead box N1 inhibits the progression of non-small cell lung cancer and serves as a tumor suppressor

    doi: 10.3892/ol.2018.8210

    Figure Lengend Snippet: EZH2 and β-catenin are novel target genes of FOXN1. Quantitative chromatin immunoprecipitation experiment was performed in (A) A549 or (B) H1299 cells using an antibody against FOXN1 or normal IgG (negative control). The binding of FOXN1 on EZH2 and β-catenin promoters were measured. A549 or H1299 cells were transfected with EZH2 or β-catenin promoter luciferase constructs along with (C) FOXN1 silencing molecules or NC shRNA, or (D) FOXN1 overexpression construct or pcDNA3.1 plasmids. The luciferase activities were measured and normalized to those of Renilla . Values are represented as the mean ± standard deviation of three independent experiments. *P

    Article Snippet: Mouse anti-human FOXN1 polyclonal antibody (cat no. sc-271256; 1:500), rabbit anti-human enhancer of zeste homolog 2 (EZH2) polyclonal antibody (cat no. sc-25383; 1:1,000), mouse anti-human β-actin monoclonal antibody (cat. no. SC47778; 1:2,000) horseradish peroxidase-labeled secondary antibodies including goat anti-mouse IgG-horseradish peroxidase (cat no. sc-2005; 1:3,000) and anti-rabbit IgG-horseradish peroxidase (cat no. sc-2004; 1:3,000) were purchased from Santa Cruz Biotechnology, Inc. (Dallas, TX, USA).

    Techniques: Chromatin Immunoprecipitation, Negative Control, Binding Assay, Transfection, Luciferase, Construct, shRNA, Over Expression, Standard Deviation

    Exposure to apoptotic thymocytes induces transient tyrosine phosphorylation of MerTK. A, B. Immunoprecipitation using antibody against phosphotyrosine (anti-pTyr). Equal numbers of PMø (A) or J774 (B) were incubated with a 10-fold greater number of apoptotic thymocytes for the indicated time (in minutes), washed extensively, and then lysed in RIPA buffer. After preclearing, Mø lysates were immunoprecipitated using anti-pTyr antibody and then immunoblotted using goat anti-MerTK. After incubation with HRP-conjugated donkey anti-goat IgG in Tween-PBS containing 5% milk, signal was detected by chemiluminescence. C', control; Thy, thymocytes (10 7 ) alone. Similar results were seen in an independent experiment of this design using each Mø cell type. C. Immunoprecipitation using goat antibody against MerTK. PMø were incubated with apoptotic thymocytes for the indicated time, washed extensively, and then lysed in RIPA buffer. After preclearing, Mø lysates were immunoprecipitated using goat antibody against MerTK, and then immunoblotted using anti-pTyr antibody. After incubation with HRP-conjugated donkey anti-rabbit IgG in BSA, signal was detected by chemiluminescence. The membrane was then stripped and reblotted using goat antibody against MerTK to demonstrate loading. Similar results were seen in four independent experiments of this design using PMø.

    Journal: Journal of leukocyte biology

    Article Title: The receptor tyrosine kinase MerTK activates phospholipase C ?2 during recognition of apoptotic thymocytes by murine macrophages

    doi: 10.1189/jlb.0903439

    Figure Lengend Snippet: Exposure to apoptotic thymocytes induces transient tyrosine phosphorylation of MerTK. A, B. Immunoprecipitation using antibody against phosphotyrosine (anti-pTyr). Equal numbers of PMø (A) or J774 (B) were incubated with a 10-fold greater number of apoptotic thymocytes for the indicated time (in minutes), washed extensively, and then lysed in RIPA buffer. After preclearing, Mø lysates were immunoprecipitated using anti-pTyr antibody and then immunoblotted using goat anti-MerTK. After incubation with HRP-conjugated donkey anti-goat IgG in Tween-PBS containing 5% milk, signal was detected by chemiluminescence. C', control; Thy, thymocytes (10 7 ) alone. Similar results were seen in an independent experiment of this design using each Mø cell type. C. Immunoprecipitation using goat antibody against MerTK. PMø were incubated with apoptotic thymocytes for the indicated time, washed extensively, and then lysed in RIPA buffer. After preclearing, Mø lysates were immunoprecipitated using goat antibody against MerTK, and then immunoblotted using anti-pTyr antibody. After incubation with HRP-conjugated donkey anti-rabbit IgG in BSA, signal was detected by chemiluminescence. The membrane was then stripped and reblotted using goat antibody against MerTK to demonstrate loading. Similar results were seen in four independent experiments of this design using PMø.

    Article Snippet: The following reagents were purchased from the indicated vendors: PBS, RPMI 1640, DMEM, FBS, HEPES, pyruvate, and penicillin/streptomycin from Invitrogen Life Technologies (Carlsbad, CA); dimethysulfoxide (DMSO), dexamethasone, 2-mercaptoethanol, sodium deoxycholate, glycerol, NaCl, Tris HCl, Triton X-100, and phosphatase inhibitor cocktail II from Sigma (St. Louis, MO); , , and 1-O-Octadecyl-2-O-methyl-sn-glycero-3-phosphorylcholine (Et-18-OCH3) from BIOMOL Research Laboratories (Plymouth Meeting, PA); rat anti-MerTK antibody and goat anti-MerTK antibody from R & D Systems (Minneapolis, MN); polyclonal rabbit anti-PLC γ1 antibody (sc-81), polyclonal rabbit anti-PLC γ2 antibody (sc-407), and blocking peptide (sc-407P), goat anti-actin antibody, mouse IgG, goat IgG, Protein L-agarose, Protein A/G agarose (50% slurry), and horseradish peroxidase (HRP)-conjugated anti-rabbit IgG from Santa Cruz Biotechnology (Santa Cruz, CA); anti-rat IgG {F(ab')2 -fragment specific} antibody and anti-goat IgG {F(ab')2 -fragment specific} antibody from Jackson ImmunoResearch Laboratories (West Grove, PA); complete mini-protease inhibitor tablets from Roche (Indianapolis, IN); sodium dodecyl sulfate (SDS), 0.2 μm polyvinylidene difluoride (PVDF) membrane, non-fat dry milk blocker, and 7.5% Ready Acrylamide gels from BioRad (Hercules, CA); Supersignal West Pico and Supersignal West Femto Maximum Sensitivity substrates from Pierce (Rockford, IL); and Kodak X-Omat AR film and 8-well Lab-Tek slides from Fisher Scientific (Chicago, IL).

    Techniques: Immunoprecipitation, Incubation

    Expression of PLC γ isoforms. Resident PMø and apoptotic thymocytes from normal mice and J774 were lysed, and equal amounts of protein were run on a 7.5% acrylamide gel under reducing conditions and transferred to PVDF membranes. Blots were probed first either with specific anti-PLC γ2 or anti-PLC γ2 plus blocking PLC γ2 peptide (A, C, top row), or with anti-PLC γ1 (B, D, top row). Blots were then washed for 15 min using Tween-PBS, incubated with HRP-conjugated donkey anti-rabbit IgG diluted in Tween-PBS containing 5% milk, and signal was detected by chemiluminescence. Blots were then stripped and re-probed using anti-actin antibody (A-D, bottom) to demonstrate protein loading.

    Journal: Journal of leukocyte biology

    Article Title: The receptor tyrosine kinase MerTK activates phospholipase C ?2 during recognition of apoptotic thymocytes by murine macrophages

    doi: 10.1189/jlb.0903439

    Figure Lengend Snippet: Expression of PLC γ isoforms. Resident PMø and apoptotic thymocytes from normal mice and J774 were lysed, and equal amounts of protein were run on a 7.5% acrylamide gel under reducing conditions and transferred to PVDF membranes. Blots were probed first either with specific anti-PLC γ2 or anti-PLC γ2 plus blocking PLC γ2 peptide (A, C, top row), or with anti-PLC γ1 (B, D, top row). Blots were then washed for 15 min using Tween-PBS, incubated with HRP-conjugated donkey anti-rabbit IgG diluted in Tween-PBS containing 5% milk, and signal was detected by chemiluminescence. Blots were then stripped and re-probed using anti-actin antibody (A-D, bottom) to demonstrate protein loading.

    Article Snippet: The following reagents were purchased from the indicated vendors: PBS, RPMI 1640, DMEM, FBS, HEPES, pyruvate, and penicillin/streptomycin from Invitrogen Life Technologies (Carlsbad, CA); dimethysulfoxide (DMSO), dexamethasone, 2-mercaptoethanol, sodium deoxycholate, glycerol, NaCl, Tris HCl, Triton X-100, and phosphatase inhibitor cocktail II from Sigma (St. Louis, MO); , , and 1-O-Octadecyl-2-O-methyl-sn-glycero-3-phosphorylcholine (Et-18-OCH3) from BIOMOL Research Laboratories (Plymouth Meeting, PA); rat anti-MerTK antibody and goat anti-MerTK antibody from R & D Systems (Minneapolis, MN); polyclonal rabbit anti-PLC γ1 antibody (sc-81), polyclonal rabbit anti-PLC γ2 antibody (sc-407), and blocking peptide (sc-407P), goat anti-actin antibody, mouse IgG, goat IgG, Protein L-agarose, Protein A/G agarose (50% slurry), and horseradish peroxidase (HRP)-conjugated anti-rabbit IgG from Santa Cruz Biotechnology (Santa Cruz, CA); anti-rat IgG {F(ab')2 -fragment specific} antibody and anti-goat IgG {F(ab')2 -fragment specific} antibody from Jackson ImmunoResearch Laboratories (West Grove, PA); complete mini-protease inhibitor tablets from Roche (Indianapolis, IN); sodium dodecyl sulfate (SDS), 0.2 μm polyvinylidene difluoride (PVDF) membrane, non-fat dry milk blocker, and 7.5% Ready Acrylamide gels from BioRad (Hercules, CA); Supersignal West Pico and Supersignal West Femto Maximum Sensitivity substrates from Pierce (Rockford, IL); and Kodak X-Omat AR film and 8-well Lab-Tek slides from Fisher Scientific (Chicago, IL).

    Techniques: Expressing, Planar Chromatography, Mouse Assay, Acrylamide Gel Assay, Blocking Assay, Incubation