horseradish peroxidase conjugated secondary antibodies  (Rockland Immunochemicals)

 
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    Structured Review

    Rockland Immunochemicals horseradish peroxidase conjugated secondary antibodies
    Horseradish Peroxidase Conjugated Secondary Antibodies, supplied by Rockland Immunochemicals, used in various techniques. Bioz Stars score: 92/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/horseradish peroxidase conjugated secondary antibodies/product/Rockland Immunochemicals
    Average 92 stars, based on 4 article reviews
    Price from $9.99 to $1999.99
    horseradish peroxidase conjugated secondary antibodies - by Bioz Stars, 2020-07
    92/100 stars

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    Related Articles

    Western Blot:

    Article Title: Klotho Gene and Protein in Human Placentas According to Birth Weight and Gestational Age
    Article Snippet: .. After extensive washing, the bands were detected with appropriate horseradish peroxidase-conjugated secondary antibodies (Rockland Immunochemical Research, Gilbertsville, PA, USA), followed by enhanced chemiluminescence (ECL plus Western Blotting Detection System, Amersham Biosciences, Bucking Hanshire, UK). .. The images were acquired and evaluated by scanning densitometry using the UltraQuant Image Acquisition and Analysis Software (Ultralum Incorporated, Claremont, CA, USA); specific times of exposure and settings were established for each protein.

    Article Title: Differences in Expression, Content, and Activity of 11 β-HSD1 in Adipose Tissue between Obese Men and Women
    Article Snippet: .. After extensive washing, bands were detected with the appropriate horseradish peroxidase-conjugated secondary antibodies (Rockland Immunochemical Research, Gilbertsville, PA, USA) followed by enhanced chemiluminescence (ECL plus Western Blotting Detection System; Amersham Biosciences, Little Chalfont, UK). .. The images were acquired and evaluated using the UltraQuant Image Acquisition and Analysis Software (Ultralum Inc., Claremont, CA, USA), normalized relative to β -actin and expressed as arbitrary units (AU).

    Incubation:

    Article Title: Mechanisms of Expression of Apoptotic Protease Activating Factor-1 (Apaf-1) in Nuclear, Mitochondrial and Cytosolic Fractions of the Cerebral Cortex of Newborn Piglets
    Article Snippet: .. Subsequently the nitrocellulose was washed with distilled water (dH2 O) and incubated with horseradish peroxidase conjugated secondary antibody (Rockland, Gilbertsville, PA, USA) in 3% milk for 1.5 h at room temperature with constant agitation. .. Following washings with dH2 O and PBS–0.05% Tween 20 the specific complexes were detected using ECL reagents (Amersham Pharmacia Biotech, Buckinghamshire, UK) for 2–3 min.

    other:

    Article Title: Mitochondrial oxidative stress is the achille's heel of melanoma cells resistant to Braf-mutant inhibitor
    Article Snippet: Horseradish peroxidase-conjugated secondary antibodies from Rockland Immunochemicals Inc. (Gilbertsville, PA) were used at 1:2,000 for 1h then detection was carried out by enhanced chemoluminescence.

    Article Title: TRAPPC9 Mediates the Interaction between p150Glued and COPII Vesicles at the Target Membrane
    Article Snippet: Horseradish Peroxidase Conjugated secondary antibodies were purchased from Rockland: anti-mouse IgG (610–1302) and anti-rabbit IgG (211–1302).

    Article Title: Hsp70 Negatively Controls Rotavirus Protein Bioavailability in Caco-2 Cells Infected by the Rotavirus RF Strain ▿
    Article Snippet: Antibodies used included monoclonal anti-Hsp70 (SPA-810); polyclonal anti-Hsp70 (SPA-812); monoclonal anti-Hsc70 (SPA-815); monoclonal anti-Hsp90 (SPA-835); monoclonal anti-Hsp110 (SPA-1103) (all of the preceding were from StressGen); monoclonal anti-VP4 from mouse ascites fluids (clone 7.7) raised against VP8*, the N-terminal cleavage product of VP4 ( , , , , ); monoclonal anti-VP2 (clone E22); monoclonal anti-VP6 (clone RV133); polyclonal anti-rotavirus strain RF (3161), which recognizes several structural viral proteins, including VP4, VP2, and VP6 (kindly provided by Jean Cohen); and horseradish peroxidase-conjugated secondary antibodies (Rockland, Gilbertsville, PA, and Jackson Immunoresearch, West Grove, PA).

    Article Title: Pseudomonas aeruginosa Outer Membrane Vesicles Modulate Host Immune Responses by Targeting the Toll-Like Receptor 4 Signaling Pathway
    Article Snippet: Horseradish peroxidase-conjugated secondary antibodies were purchased from Rockland Immunochemicals.

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  • 93
    Rockland Immunochemicals hrp conjugated mouse trueblot ultra secondary antibody
    Validation of candidate DG-binding proteins. (A) Coimmunoprecipitation (co-IP) of DG-associated scaffold proteins. Monolayers of A549 and SAEC were lysed in cold Triton X-100 containing buffer, and cleared lysates were subjected to IP with MAb VIA4 matrix (α-DG) using MAb anti-HA matrix (HA) as a control. Immunocomplexes were probed in Western blots for functional α-DG (MAb IIH6), β-DG (MAb 8D9), utrophin (MAb 20C5), α1-syntrophin (goat pAb 5941), β1-syntrophin (rabbit pAb 98977), β2-syntrophin (MAb 1351), and β-dystrobrevin (rabbit pAb 152133). Primary rabbit and goat antibodies as well as MAb IIH6 (mouse IgM) were detected as described in the legend to Fig. 1B and C . For detection of mouse MAb IgG, <t>HRP-conjugated</t> mouse <t>TrueBlot</t> <t>ULTRA</t> secondary antibody was used as detailed in Materials and Methods. For a positive control (+), total lysates of differentiated human myotubes were included. One representative example out of three independent experiments is shown. (B) Detection of sarcoglycans at the surfaces of A549 cells. Intact monolayers of A549 cells were subjected to cell surface biotinylation using the membrane-impermeable reagent sulfo-NHS-X-biotin (+) or reaction buffer only (−). After reaction quenching, cells were lysed, and biotinylated proteins were precipitated with streptavidin agarose beads. Proteins were eluted and probed in Western blots for β-DG (MAb 8D9), α-sarcoglycan (SG) (rabbit pAb R98), β-sarcoglycan (MAb 5B1), γ-sarcoglycan (MAb 21B5), δ-sarcoglycan (rabbit pAb R214), ε-sarcoglycan (rabbit pAb 155651), and sarcospan (SSN) (rabbit MAb 186730), followed by detection as described above for panel A. The positive control (+) was differentiated human myotube lysate. One representative example of two independent experiments is shown. (C) Flow chart for the live cell surface cross-linking approach. For details, please see text. (D) Chemical cross-linking of DG with sarcoglycans at the cell surface. Live intact A549 monolayers were treated with the membrane-impermeable thiol-cleavable cross-linking reagent DTSSP (+) or reaction buffer only (−). After quenching, cells were lysed, and cleared lysates were subjected to IP with MAb VIA4 matrix (α-DG) or anti-HA matrix (HA) as described above for panel A. Eluted proteins were treated with DTT and analyzed in Western blot probing for functional α-DG, β-DG, the indicated sacroglycans, and sarcospan as described above for panel B. Please note that the blots for α- and β-DG (top) correspond each to 1% of the material, and the blots for the sacroglycans and sarcospan each correspond to 15% of the sample. One representative example of two independent experiments is shown. (E) Schema of a working model of the DG complex in A549 cells (this study) compared to the DG complex in skeletal muscle (based on published data [ 40 , 41 ]). The α-DG-linked matriglycan sugar polymers and β-DG are indicated, as well as α-, β-, γ-, δ-, and ε-sarcoglycans (SG), sarcospan (SPN), α- and β-dystrobrevin (DTN), α1, β1, and β2-syntrophin (SNT), and nitric oxide synthase (nNOS).
    Hrp Conjugated Mouse Trueblot Ultra Secondary Antibody, supplied by Rockland Immunochemicals, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hrp conjugated mouse trueblot ultra secondary antibody/product/Rockland Immunochemicals
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    hrp conjugated mouse trueblot ultra secondary antibody - by Bioz Stars, 2020-07
    93/100 stars
      Buy from Supplier

    94
    Rockland Immunochemicals goat anti rabbit igg hrp conjugated
    Evaluation of the biological binding function of Hutat2:Fc and protective effects of Hutat2:Fc against HIV-1 Tat 86 -mediated toxicity in HTB-11 cells. (A) Specific binding of Hutat2:Fc to HIV-1 Tat. HIV-1 Tat 86 (Clade B) loaded nitrocellular membranes (NCM) were incubated with cell culture supernatants collected from HR-Hutat2-transduced HTB-11 (HTB-Hutat2), U937 (U937-Hutat2), or hMDM (hMDM-Hutat2) at 4°C overnight followed by incubation with rabbit anti-human <t>IgG</t> (H+L) and goat anti-rabbit IgG <t>HRP</t> conjugated antibodies. Specific binding was visualized by the color deposition on the NCM. The Tat 86 -loaded membrane incubated with rabbit anti-Tat serum served as a positive control (Pos Ctl) while incubated with cell culture supernatant from HR-A3H5 transduced HTB-11 served as a negative control (HTB-A3H5). The NCM loaded with Tat dilution buffer was used as a blank control (BLK Ctl). (B) Functional antagonization of Hutat2:Fc against HIV-1 Tat 86 -induced toxicity in HTB-11 cells by an MTT assay. The OD 570 value of untreated HTB-11 cells was arbitrarily defined as 100% cell viability. The relative cell viability (%) was expressed as a percentage relative to the untreated control cells. The cell viability was significantly higher for the cells treated with the conditioned mediums from transduced cells releasing Hutat:Fc when compared to the cultures that received Tat 86 (500 nM) alone (* P
    Goat Anti Rabbit Igg Hrp Conjugated, supplied by Rockland Immunochemicals, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/goat anti rabbit igg hrp conjugated/product/Rockland Immunochemicals
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    goat anti rabbit igg hrp conjugated - by Bioz Stars, 2020-07
    94/100 stars
      Buy from Supplier

    92
    Rockland Immunochemicals horseradish peroxidase conjugated secondary antibodies
    Evaluation of the biological binding function of Hutat2:Fc and protective effects of Hutat2:Fc against HIV-1 Tat 86 -mediated toxicity in HTB-11 cells. (A) Specific binding of Hutat2:Fc to HIV-1 Tat. HIV-1 Tat 86 (Clade B) loaded nitrocellular membranes (NCM) were incubated with cell culture supernatants collected from HR-Hutat2-transduced HTB-11 (HTB-Hutat2), U937 (U937-Hutat2), or hMDM (hMDM-Hutat2) at 4°C overnight followed by incubation with rabbit anti-human <t>IgG</t> (H+L) and goat anti-rabbit IgG <t>HRP</t> conjugated antibodies. Specific binding was visualized by the color deposition on the NCM. The Tat 86 -loaded membrane incubated with rabbit anti-Tat serum served as a positive control (Pos Ctl) while incubated with cell culture supernatant from HR-A3H5 transduced HTB-11 served as a negative control (HTB-A3H5). The NCM loaded with Tat dilution buffer was used as a blank control (BLK Ctl). (B) Functional antagonization of Hutat2:Fc against HIV-1 Tat 86 -induced toxicity in HTB-11 cells by an MTT assay. The OD 570 value of untreated HTB-11 cells was arbitrarily defined as 100% cell viability. The relative cell viability (%) was expressed as a percentage relative to the untreated control cells. The cell viability was significantly higher for the cells treated with the conditioned mediums from transduced cells releasing Hutat:Fc when compared to the cultures that received Tat 86 (500 nM) alone (* P
    Horseradish Peroxidase Conjugated Secondary Antibodies, supplied by Rockland Immunochemicals, used in various techniques. Bioz Stars score: 92/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/horseradish peroxidase conjugated secondary antibodies/product/Rockland Immunochemicals
    Average 92 stars, based on 4 article reviews
    Price from $9.99 to $1999.99
    horseradish peroxidase conjugated secondary antibodies - by Bioz Stars, 2020-07
    92/100 stars
      Buy from Supplier

    88
    Rockland Immunochemicals hrp conjugated donkey anti goat secondary antibodies
    Evaluation of the biological binding function of Hutat2:Fc and protective effects of Hutat2:Fc against HIV-1 Tat 86 -mediated toxicity in HTB-11 cells. (A) Specific binding of Hutat2:Fc to HIV-1 Tat. HIV-1 Tat 86 (Clade B) loaded nitrocellular membranes (NCM) were incubated with cell culture supernatants collected from HR-Hutat2-transduced HTB-11 (HTB-Hutat2), U937 (U937-Hutat2), or hMDM (hMDM-Hutat2) at 4°C overnight followed by incubation with rabbit anti-human <t>IgG</t> (H+L) and goat anti-rabbit IgG <t>HRP</t> conjugated antibodies. Specific binding was visualized by the color deposition on the NCM. The Tat 86 -loaded membrane incubated with rabbit anti-Tat serum served as a positive control (Pos Ctl) while incubated with cell culture supernatant from HR-A3H5 transduced HTB-11 served as a negative control (HTB-A3H5). The NCM loaded with Tat dilution buffer was used as a blank control (BLK Ctl). (B) Functional antagonization of Hutat2:Fc against HIV-1 Tat 86 -induced toxicity in HTB-11 cells by an MTT assay. The OD 570 value of untreated HTB-11 cells was arbitrarily defined as 100% cell viability. The relative cell viability (%) was expressed as a percentage relative to the untreated control cells. The cell viability was significantly higher for the cells treated with the conditioned mediums from transduced cells releasing Hutat:Fc when compared to the cultures that received Tat 86 (500 nM) alone (* P
    Hrp Conjugated Donkey Anti Goat Secondary Antibodies, supplied by Rockland Immunochemicals, used in various techniques. Bioz Stars score: 88/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hrp conjugated donkey anti goat secondary antibodies/product/Rockland Immunochemicals
    Average 88 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    hrp conjugated donkey anti goat secondary antibodies - by Bioz Stars, 2020-07
    88/100 stars
      Buy from Supplier

    Image Search Results


    Validation of candidate DG-binding proteins. (A) Coimmunoprecipitation (co-IP) of DG-associated scaffold proteins. Monolayers of A549 and SAEC were lysed in cold Triton X-100 containing buffer, and cleared lysates were subjected to IP with MAb VIA4 matrix (α-DG) using MAb anti-HA matrix (HA) as a control. Immunocomplexes were probed in Western blots for functional α-DG (MAb IIH6), β-DG (MAb 8D9), utrophin (MAb 20C5), α1-syntrophin (goat pAb 5941), β1-syntrophin (rabbit pAb 98977), β2-syntrophin (MAb 1351), and β-dystrobrevin (rabbit pAb 152133). Primary rabbit and goat antibodies as well as MAb IIH6 (mouse IgM) were detected as described in the legend to Fig. 1B and C . For detection of mouse MAb IgG, HRP-conjugated mouse TrueBlot ULTRA secondary antibody was used as detailed in Materials and Methods. For a positive control (+), total lysates of differentiated human myotubes were included. One representative example out of three independent experiments is shown. (B) Detection of sarcoglycans at the surfaces of A549 cells. Intact monolayers of A549 cells were subjected to cell surface biotinylation using the membrane-impermeable reagent sulfo-NHS-X-biotin (+) or reaction buffer only (−). After reaction quenching, cells were lysed, and biotinylated proteins were precipitated with streptavidin agarose beads. Proteins were eluted and probed in Western blots for β-DG (MAb 8D9), α-sarcoglycan (SG) (rabbit pAb R98), β-sarcoglycan (MAb 5B1), γ-sarcoglycan (MAb 21B5), δ-sarcoglycan (rabbit pAb R214), ε-sarcoglycan (rabbit pAb 155651), and sarcospan (SSN) (rabbit MAb 186730), followed by detection as described above for panel A. The positive control (+) was differentiated human myotube lysate. One representative example of two independent experiments is shown. (C) Flow chart for the live cell surface cross-linking approach. For details, please see text. (D) Chemical cross-linking of DG with sarcoglycans at the cell surface. Live intact A549 monolayers were treated with the membrane-impermeable thiol-cleavable cross-linking reagent DTSSP (+) or reaction buffer only (−). After quenching, cells were lysed, and cleared lysates were subjected to IP with MAb VIA4 matrix (α-DG) or anti-HA matrix (HA) as described above for panel A. Eluted proteins were treated with DTT and analyzed in Western blot probing for functional α-DG, β-DG, the indicated sacroglycans, and sarcospan as described above for panel B. Please note that the blots for α- and β-DG (top) correspond each to 1% of the material, and the blots for the sacroglycans and sarcospan each correspond to 15% of the sample. One representative example of two independent experiments is shown. (E) Schema of a working model of the DG complex in A549 cells (this study) compared to the DG complex in skeletal muscle (based on published data [ 40 , 41 ]). The α-DG-linked matriglycan sugar polymers and β-DG are indicated, as well as α-, β-, γ-, δ-, and ε-sarcoglycans (SG), sarcospan (SPN), α- and β-dystrobrevin (DTN), α1, β1, and β2-syntrophin (SNT), and nitric oxide synthase (nNOS).

    Journal: mBio

    Article Title: Dynamic Dystroglycan Complexes Mediate Cell Entry of Lassa Virus

    doi: 10.1128/mBio.02869-18

    Figure Lengend Snippet: Validation of candidate DG-binding proteins. (A) Coimmunoprecipitation (co-IP) of DG-associated scaffold proteins. Monolayers of A549 and SAEC were lysed in cold Triton X-100 containing buffer, and cleared lysates were subjected to IP with MAb VIA4 matrix (α-DG) using MAb anti-HA matrix (HA) as a control. Immunocomplexes were probed in Western blots for functional α-DG (MAb IIH6), β-DG (MAb 8D9), utrophin (MAb 20C5), α1-syntrophin (goat pAb 5941), β1-syntrophin (rabbit pAb 98977), β2-syntrophin (MAb 1351), and β-dystrobrevin (rabbit pAb 152133). Primary rabbit and goat antibodies as well as MAb IIH6 (mouse IgM) were detected as described in the legend to Fig. 1B and C . For detection of mouse MAb IgG, HRP-conjugated mouse TrueBlot ULTRA secondary antibody was used as detailed in Materials and Methods. For a positive control (+), total lysates of differentiated human myotubes were included. One representative example out of three independent experiments is shown. (B) Detection of sarcoglycans at the surfaces of A549 cells. Intact monolayers of A549 cells were subjected to cell surface biotinylation using the membrane-impermeable reagent sulfo-NHS-X-biotin (+) or reaction buffer only (−). After reaction quenching, cells were lysed, and biotinylated proteins were precipitated with streptavidin agarose beads. Proteins were eluted and probed in Western blots for β-DG (MAb 8D9), α-sarcoglycan (SG) (rabbit pAb R98), β-sarcoglycan (MAb 5B1), γ-sarcoglycan (MAb 21B5), δ-sarcoglycan (rabbit pAb R214), ε-sarcoglycan (rabbit pAb 155651), and sarcospan (SSN) (rabbit MAb 186730), followed by detection as described above for panel A. The positive control (+) was differentiated human myotube lysate. One representative example of two independent experiments is shown. (C) Flow chart for the live cell surface cross-linking approach. For details, please see text. (D) Chemical cross-linking of DG with sarcoglycans at the cell surface. Live intact A549 monolayers were treated with the membrane-impermeable thiol-cleavable cross-linking reagent DTSSP (+) or reaction buffer only (−). After quenching, cells were lysed, and cleared lysates were subjected to IP with MAb VIA4 matrix (α-DG) or anti-HA matrix (HA) as described above for panel A. Eluted proteins were treated with DTT and analyzed in Western blot probing for functional α-DG, β-DG, the indicated sacroglycans, and sarcospan as described above for panel B. Please note that the blots for α- and β-DG (top) correspond each to 1% of the material, and the blots for the sacroglycans and sarcospan each correspond to 15% of the sample. One representative example of two independent experiments is shown. (E) Schema of a working model of the DG complex in A549 cells (this study) compared to the DG complex in skeletal muscle (based on published data [ 40 , 41 ]). The α-DG-linked matriglycan sugar polymers and β-DG are indicated, as well as α-, β-, γ-, δ-, and ε-sarcoglycans (SG), sarcospan (SPN), α- and β-dystrobrevin (DTN), α1, β1, and β2-syntrophin (SNT), and nitric oxide synthase (nNOS).

    Article Snippet: For detection of mouse MAb IgG in IPs using mouse IgG, HRP-conjugated mouse TrueBlot ULTRA secondary antibody was used (Rockland Inc.).

    Techniques: Binding Assay, Co-Immunoprecipitation Assay, Western Blot, Functional Assay, Positive Control, Flow Cytometry

    Evaluation of the biological binding function of Hutat2:Fc and protective effects of Hutat2:Fc against HIV-1 Tat 86 -mediated toxicity in HTB-11 cells. (A) Specific binding of Hutat2:Fc to HIV-1 Tat. HIV-1 Tat 86 (Clade B) loaded nitrocellular membranes (NCM) were incubated with cell culture supernatants collected from HR-Hutat2-transduced HTB-11 (HTB-Hutat2), U937 (U937-Hutat2), or hMDM (hMDM-Hutat2) at 4°C overnight followed by incubation with rabbit anti-human IgG (H+L) and goat anti-rabbit IgG HRP conjugated antibodies. Specific binding was visualized by the color deposition on the NCM. The Tat 86 -loaded membrane incubated with rabbit anti-Tat serum served as a positive control (Pos Ctl) while incubated with cell culture supernatant from HR-A3H5 transduced HTB-11 served as a negative control (HTB-A3H5). The NCM loaded with Tat dilution buffer was used as a blank control (BLK Ctl). (B) Functional antagonization of Hutat2:Fc against HIV-1 Tat 86 -induced toxicity in HTB-11 cells by an MTT assay. The OD 570 value of untreated HTB-11 cells was arbitrarily defined as 100% cell viability. The relative cell viability (%) was expressed as a percentage relative to the untreated control cells. The cell viability was significantly higher for the cells treated with the conditioned mediums from transduced cells releasing Hutat:Fc when compared to the cultures that received Tat 86 (500 nM) alone (* P

    Journal: Journal of Neuroinflammation

    Article Title: Anti-tat Hutat2:Fc mediated protection against tat-induced neurotoxicity and HIV-1 replication in human monocyte-derived macrophages

    doi: 10.1186/s12974-014-0195-2

    Figure Lengend Snippet: Evaluation of the biological binding function of Hutat2:Fc and protective effects of Hutat2:Fc against HIV-1 Tat 86 -mediated toxicity in HTB-11 cells. (A) Specific binding of Hutat2:Fc to HIV-1 Tat. HIV-1 Tat 86 (Clade B) loaded nitrocellular membranes (NCM) were incubated with cell culture supernatants collected from HR-Hutat2-transduced HTB-11 (HTB-Hutat2), U937 (U937-Hutat2), or hMDM (hMDM-Hutat2) at 4°C overnight followed by incubation with rabbit anti-human IgG (H+L) and goat anti-rabbit IgG HRP conjugated antibodies. Specific binding was visualized by the color deposition on the NCM. The Tat 86 -loaded membrane incubated with rabbit anti-Tat serum served as a positive control (Pos Ctl) while incubated with cell culture supernatant from HR-A3H5 transduced HTB-11 served as a negative control (HTB-A3H5). The NCM loaded with Tat dilution buffer was used as a blank control (BLK Ctl). (B) Functional antagonization of Hutat2:Fc against HIV-1 Tat 86 -induced toxicity in HTB-11 cells by an MTT assay. The OD 570 value of untreated HTB-11 cells was arbitrarily defined as 100% cell viability. The relative cell viability (%) was expressed as a percentage relative to the untreated control cells. The cell viability was significantly higher for the cells treated with the conditioned mediums from transduced cells releasing Hutat:Fc when compared to the cultures that received Tat 86 (500 nM) alone (* P

    Article Snippet: Rabbit-anti-human IgG(H+L) (1:1,000 dilution) (Rockland) and goat anti-rabbit IgG HRP-conjugated (1:3,000 dilution) (Rockland) were used before the exposure to a metal enhanced DAB substrate (PIERCE).

    Techniques: Binding Assay, Incubation, Cell Culture, Positive Control, CTL Assay, Negative Control, Functional Assay, MTT Assay