anti goat horseradish peroxidase conjugated immunoglobulin g igg  (Jackson Immuno)

 
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    Name:
    Goat Anti Horseradish Peroxidase
    Description:
    Whole IgG antibodies are isolated as intact molecules from antisera by immunoaffinity chromatography They have an Fc portion and two antigen binding Fab portions joined together by disulfide bonds and therefore they are divalent The average molecular weight is reported to be about 160 kDa The whole IgG form of antibodies is suitable for the majority of immunodetection procedures and is the most cost effective Based on immunoelectrophoresis and or ELISA the antibody reacts with peroxidase from horseradish roots It may cross react with peroxidase from other sources
    Catalog Number:
    123-005-021
    Price:
    79.0
    Category:
    Anti Fluorescein Anti Digoxin Anti Biotin and Anti HRP
    Conjugate:
    Unconjugated
    Size:
    2 0 mg
    Format:
    Whole IgG
    Host:
    Goat
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    Structured Review

    Jackson Immuno anti goat horseradish peroxidase conjugated immunoglobulin g igg
    (A,B) Lactoferrin (Lf) fragments accumulate in macrophages following incubation with senescent neutrophils. (A) Peritoneal macrophages were recovered 66 h post zymosan A-induced (1 mg/mouse) peritonitis initiation and incubated with apoptotic Jurkat cells (AC), senescent peritoneal neutrophils (SN), latex beads (LBs), <t>IgG-opsonized</t> LB (oLB), or anti-CD11b monoclonal antibodies as indicated. After 24 h, unbound cells were washed and macrophages were recovered. Then, the cells were lysed, and equal amounts of protein extract were blotted for Lf. Protein extracts from apoptotic neutrophils were also analyzed as indicated. Results are representative from three independent experiments (cells were pooled from three to five mice). (B) Peritoneal neutrophils were recovered 24 h PPI and treated with roscovitine (10 µM) alone or with protease inhibitor cocktail (Pi), cycloheximide (CHX), or the neutrophil elastase inhibitor, silevestat (NEi) for 20 h. Then, neutrophils were lysed, and their protein content was immunoblotted for Lf [results are representative from three experiments (cells were pooled from three to five mice)]. (C,D) Lf fragments are found in interstitial fluids (ISFs) of spleen and inguinal lymph nodes (LN) during peritonitis. Spleen (C) and inguinal LN (D) were harvested 24 and 66 h after initiation of peritonitis ( n = 4–5) and mashed in equal volumes of PBS employing a nylon grid. Equal amounts of ISF protein were run by 10% sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS–PAGE), followed by Western blotting for Lf. Results are representative blots from three experiments. (E–G) Peritoneal resolution phase macrophages are essential for the differential production of splenic Lf fragments. Mice were injected intraperitoneally (i.p.) with clodronate-containing or empty liposomes 42 h PPI or before the initiation of peritonitis. After additional 24 h, the spleens were recovered and mashed in equal volumes of PBS employing a nylon grid. Equal amounts of ISF protein were run by 12% SDS-PAGE, followed by Western blotting for Lf. Results are a representative blot (E) and averages of densitometric analysis of the 23- (F) and 17 (G) -kDa bands from three experiments ( n = 3–6 mice per group). **/*indicate statistically significant differences of P ≤ 0.01/ P ≤ 0.05, respectively, by ANOVA with Tukey post hoc analysis. (H) Lf fragments are found in dairy cow milk during the onset and resolution of mastitis. Milk samples from dairy cows with mastitis (days 1–7) were defatted and separated into soluble and cellular fractions by centrifugation. The cellular fraction was lysed and the cytoplasmic proteins were recovered. Equal amounts of protein from both fractions were analyzed by Western blotting for Lf. Results show representative blots from three sample sets taken daily from three different cows.
    Whole IgG antibodies are isolated as intact molecules from antisera by immunoaffinity chromatography They have an Fc portion and two antigen binding Fab portions joined together by disulfide bonds and therefore they are divalent The average molecular weight is reported to be about 160 kDa The whole IgG form of antibodies is suitable for the majority of immunodetection procedures and is the most cost effective Based on immunoelectrophoresis and or ELISA the antibody reacts with peroxidase from horseradish roots It may cross react with peroxidase from other sources
    https://www.bioz.com/result/anti goat horseradish peroxidase conjugated immunoglobulin g igg/product/Jackson Immuno
    Average 98 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti goat horseradish peroxidase conjugated immunoglobulin g igg - by Bioz Stars, 2021-06
    98/100 stars

    Images

    1) Product Images from "A 17-kDa Fragment of Lactoferrin Associates With the Termination of Inflammation and Peptides Within Promote Resolution"

    Article Title: A 17-kDa Fragment of Lactoferrin Associates With the Termination of Inflammation and Peptides Within Promote Resolution

    Journal: Frontiers in Immunology

    doi: 10.3389/fimmu.2018.00644

    (A,B) Lactoferrin (Lf) fragments accumulate in macrophages following incubation with senescent neutrophils. (A) Peritoneal macrophages were recovered 66 h post zymosan A-induced (1 mg/mouse) peritonitis initiation and incubated with apoptotic Jurkat cells (AC), senescent peritoneal neutrophils (SN), latex beads (LBs), IgG-opsonized LB (oLB), or anti-CD11b monoclonal antibodies as indicated. After 24 h, unbound cells were washed and macrophages were recovered. Then, the cells were lysed, and equal amounts of protein extract were blotted for Lf. Protein extracts from apoptotic neutrophils were also analyzed as indicated. Results are representative from three independent experiments (cells were pooled from three to five mice). (B) Peritoneal neutrophils were recovered 24 h PPI and treated with roscovitine (10 µM) alone or with protease inhibitor cocktail (Pi), cycloheximide (CHX), or the neutrophil elastase inhibitor, silevestat (NEi) for 20 h. Then, neutrophils were lysed, and their protein content was immunoblotted for Lf [results are representative from three experiments (cells were pooled from three to five mice)]. (C,D) Lf fragments are found in interstitial fluids (ISFs) of spleen and inguinal lymph nodes (LN) during peritonitis. Spleen (C) and inguinal LN (D) were harvested 24 and 66 h after initiation of peritonitis ( n = 4–5) and mashed in equal volumes of PBS employing a nylon grid. Equal amounts of ISF protein were run by 10% sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS–PAGE), followed by Western blotting for Lf. Results are representative blots from three experiments. (E–G) Peritoneal resolution phase macrophages are essential for the differential production of splenic Lf fragments. Mice were injected intraperitoneally (i.p.) with clodronate-containing or empty liposomes 42 h PPI or before the initiation of peritonitis. After additional 24 h, the spleens were recovered and mashed in equal volumes of PBS employing a nylon grid. Equal amounts of ISF protein were run by 12% SDS-PAGE, followed by Western blotting for Lf. Results are a representative blot (E) and averages of densitometric analysis of the 23- (F) and 17 (G) -kDa bands from three experiments ( n = 3–6 mice per group). **/*indicate statistically significant differences of P ≤ 0.01/ P ≤ 0.05, respectively, by ANOVA with Tukey post hoc analysis. (H) Lf fragments are found in dairy cow milk during the onset and resolution of mastitis. Milk samples from dairy cows with mastitis (days 1–7) were defatted and separated into soluble and cellular fractions by centrifugation. The cellular fraction was lysed and the cytoplasmic proteins were recovered. Equal amounts of protein from both fractions were analyzed by Western blotting for Lf. Results show representative blots from three sample sets taken daily from three different cows.
    Figure Legend Snippet: (A,B) Lactoferrin (Lf) fragments accumulate in macrophages following incubation with senescent neutrophils. (A) Peritoneal macrophages were recovered 66 h post zymosan A-induced (1 mg/mouse) peritonitis initiation and incubated with apoptotic Jurkat cells (AC), senescent peritoneal neutrophils (SN), latex beads (LBs), IgG-opsonized LB (oLB), or anti-CD11b monoclonal antibodies as indicated. After 24 h, unbound cells were washed and macrophages were recovered. Then, the cells were lysed, and equal amounts of protein extract were blotted for Lf. Protein extracts from apoptotic neutrophils were also analyzed as indicated. Results are representative from three independent experiments (cells were pooled from three to five mice). (B) Peritoneal neutrophils were recovered 24 h PPI and treated with roscovitine (10 µM) alone or with protease inhibitor cocktail (Pi), cycloheximide (CHX), or the neutrophil elastase inhibitor, silevestat (NEi) for 20 h. Then, neutrophils were lysed, and their protein content was immunoblotted for Lf [results are representative from three experiments (cells were pooled from three to five mice)]. (C,D) Lf fragments are found in interstitial fluids (ISFs) of spleen and inguinal lymph nodes (LN) during peritonitis. Spleen (C) and inguinal LN (D) were harvested 24 and 66 h after initiation of peritonitis ( n = 4–5) and mashed in equal volumes of PBS employing a nylon grid. Equal amounts of ISF protein were run by 10% sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS–PAGE), followed by Western blotting for Lf. Results are representative blots from three experiments. (E–G) Peritoneal resolution phase macrophages are essential for the differential production of splenic Lf fragments. Mice were injected intraperitoneally (i.p.) with clodronate-containing or empty liposomes 42 h PPI or before the initiation of peritonitis. After additional 24 h, the spleens were recovered and mashed in equal volumes of PBS employing a nylon grid. Equal amounts of ISF protein were run by 12% SDS-PAGE, followed by Western blotting for Lf. Results are a representative blot (E) and averages of densitometric analysis of the 23- (F) and 17 (G) -kDa bands from three experiments ( n = 3–6 mice per group). **/*indicate statistically significant differences of P ≤ 0.01/ P ≤ 0.05, respectively, by ANOVA with Tukey post hoc analysis. (H) Lf fragments are found in dairy cow milk during the onset and resolution of mastitis. Milk samples from dairy cows with mastitis (days 1–7) were defatted and separated into soluble and cellular fractions by centrifugation. The cellular fraction was lysed and the cytoplasmic proteins were recovered. Equal amounts of protein from both fractions were analyzed by Western blotting for Lf. Results show representative blots from three sample sets taken daily from three different cows.

    Techniques Used: Incubation, Mouse Assay, Protease Inhibitor, Polyacrylamide Gel Electrophoresis, SDS Page, Western Blot, Injection, Centrifugation

    Related Articles

    Enzyme-linked Immunosorbent Assay:

    Article Title: A 17-kDa Fragment of Lactoferrin Associates With the Termination of Inflammation and Peptides Within Promote Resolution
    Article Snippet: .. Reagents The following reagents were purchased as detailed: acrylamide/bis-acrylamide, fibronectin, lipopolysaccharide (LPS) (from Escherichia coli , clone 055:B5), staurosporine, TEMED, Tween-20, the neutrophil elastase inhibitor silevestat, and zymosan A from Sigma-Aldrich; clodronate from Liposoma BV; anti-goat horseradish peroxidase-conjugated immunoglobulin G (IgG) and anti-rabbit horseradish peroxidase-conjugated IgG from Jackson Immuno Research Laboratories; WesternBright™ ECL from Advansta, fetal calf serum (FCS), L-glutamine, penicillin–streptomycin, RPMI 1640 and trypan blue from Biological Industries, Kibbutz Beit Haemek; goat anti-mouse CD11b (M-19) polyclonal IgG and rabbit anti-human Lf (H-65) polyclonal IgG from SantaCruz Biotechnology; FITC-conjugated anti-mouse Gr-1, PE-conjugated anti-mouse F4/80, PerCP-conjugated anti-mouse CD11b, APC-conjugated anti-mouse CXCR4 (clone BL6-146508) and enzyme-linked immunosorbent assay (ELISA) kits for TNFα, IL-6, IL-12, and IL-10 from Biolegend; cycloheximide (CHX) from Cayman Chemical; PE selection kit was purchased from Stem Cell Technologies; and Protease Inhibitors Cocktail was purchased from Roche. .. FKD and FKE peptides were organically synthesized by GL Biochem (Shanghai) Ltd.

    Selection:

    Article Title: A 17-kDa Fragment of Lactoferrin Associates With the Termination of Inflammation and Peptides Within Promote Resolution
    Article Snippet: .. Reagents The following reagents were purchased as detailed: acrylamide/bis-acrylamide, fibronectin, lipopolysaccharide (LPS) (from Escherichia coli , clone 055:B5), staurosporine, TEMED, Tween-20, the neutrophil elastase inhibitor silevestat, and zymosan A from Sigma-Aldrich; clodronate from Liposoma BV; anti-goat horseradish peroxidase-conjugated immunoglobulin G (IgG) and anti-rabbit horseradish peroxidase-conjugated IgG from Jackson Immuno Research Laboratories; WesternBright™ ECL from Advansta, fetal calf serum (FCS), L-glutamine, penicillin–streptomycin, RPMI 1640 and trypan blue from Biological Industries, Kibbutz Beit Haemek; goat anti-mouse CD11b (M-19) polyclonal IgG and rabbit anti-human Lf (H-65) polyclonal IgG from SantaCruz Biotechnology; FITC-conjugated anti-mouse Gr-1, PE-conjugated anti-mouse F4/80, PerCP-conjugated anti-mouse CD11b, APC-conjugated anti-mouse CXCR4 (clone BL6-146508) and enzyme-linked immunosorbent assay (ELISA) kits for TNFα, IL-6, IL-12, and IL-10 from Biolegend; cycloheximide (CHX) from Cayman Chemical; PE selection kit was purchased from Stem Cell Technologies; and Protease Inhibitors Cocktail was purchased from Roche. .. FKD and FKE peptides were organically synthesized by GL Biochem (Shanghai) Ltd.

    Western Blot:

    Article Title: Trafficking-Competent KCNQ1 Variably Influences the Function of HERG Long QT Alleles
    Article Snippet: 700 μgs of each extract were immunoprecipitated with EZview Red Anti-FLAG M2 or anti-HA Affinity Gel (Sigma). .. Immunoprecipitates were washed three times with 1xTBS (0.9% NaCl, 20 mM Tris, pH 7.4), followed by resuspension in SDS sample buffer, and prepared for Western blotting with a rabbit anti-HERG antibody (1:400 dilution, Alomone), goat anti-KCNQ1 antibody (1:200 dilution, Santa Cruz), or anti-KCNA5 (1:400, Alomone) in combination with an HRP-linked anti-goat secondary antibody (1:5,000 Jackson ImmunoResearch) or anti-rabbit secondary antibody (1:10,000 dilution, GE Healthcare Bio-Sciences Corp.) using ECL (GE Healthcare Bio-Sciences Corp.). .. To assess the effects of KCNQ1 on HERG, we transfected CHO cells with both cDNAs.

    Article Title: MT5-MMP controls APP and β-CTF/C99 metabolism through proteolytic-dependent and -independent mechanisms relevant for Alzheimer’s disease
    Article Snippet: For the immunoprecipitation (IP) assay, 250 μg of protein (cell lysates) in 500 μL of RIPA buffer were incubated overnight at 4°C with unspecific mouse/rabbit/rat IgG antibodies (Jackson Immunoresearch) or rat anti-HA-tag (Roche Diagnostics) or mouse anti-FlagM2 and rabbit anti-APP-CTF (Sigma-Aldrich) at 4 ng/μL and then pulled-down for 2 h using protein G-coupled dynabeads (50 μL, Thermo Fisher Scientific). .. After washing 3 times with 0.3 M NaCl solution, samples were denatured and subjected to western blot (WB) using APP-CTF, anti-FlagM2 or anti-HA antibodies, and the corresponding horseradish peroxidase-conjugated secondary IgG antibodies (Jackson Immunoresearch). .. The EasyBlocker kit was used to limit unspecific signal according to the manufacturer’s recommendations (GeneTex, Euromedex, Souffelweyersheim, France).

    Article Title: Generation of H7N9-specific human polyclonal antibodies from a transchromosomic goat (caprine) system
    Article Snippet: The purified human IgG has a IgG concentration of 0.75 mg/ml in a sterile-filtered PBS buffer. .. Western blotting Immunoglobulin heavy and light chains of purified human IgG and goat IgG were separated by SDS PAGE using 4–12% precast Bis-Tris gels (Invitrogen) and transferred to polyvinylidene difluoride membranes that were directly probed with donkey anti-hIgG (H + L) specific horseradish peroxidase (HRP)-conjugated antibody (Jackson ImmunoResearch) for hIgG heavy chain and light chain detection. .. H7N9 HA-specific human IgG ELISA To determine H7N9 HA-specific hIgG titers, 96-well Nunc Maxisorp ELISA plates were coated overnight at 4 °C with 100 μl/well of 2 μg/mL recombinant H7N9 HA1 (H7N9 HA1-rFc) in PBS.

    Purification:

    Article Title: Generation of H7N9-specific human polyclonal antibodies from a transchromosomic goat (caprine) system
    Article Snippet: The purified human IgG has a IgG concentration of 0.75 mg/ml in a sterile-filtered PBS buffer. .. Immunoglobulin heavy and light chains of purified human IgG and goat IgG were separated by SDS PAGE using 4–12% precast Bis-Tris gels (Invitrogen) and transferred to polyvinylidene difluoride membranes that were directly probed with donkey anti-hIgG (H + L) specific horseradish peroxidase (HRP)-conjugated antibody (Jackson ImmunoResearch) for hIgG heavy chain and light chain detection. .. To determine H7N9 HA-specific hIgG titers, 96-well Nunc Maxisorp ELISA plates were coated overnight at 4 °C with 100 μl/well of 2 μg/mL recombinant H7N9 HA1 (H7N9 HA1-rFc) in PBS.

    Article Title: Generation of H7N9-specific human polyclonal antibodies from a transchromosomic goat (caprine) system
    Article Snippet: The purified human IgG has a IgG concentration of 0.75 mg/ml in a sterile-filtered PBS buffer. .. Western blotting Immunoglobulin heavy and light chains of purified human IgG and goat IgG were separated by SDS PAGE using 4–12% precast Bis-Tris gels (Invitrogen) and transferred to polyvinylidene difluoride membranes that were directly probed with donkey anti-hIgG (H + L) specific horseradish peroxidase (HRP)-conjugated antibody (Jackson ImmunoResearch) for hIgG heavy chain and light chain detection. .. H7N9 HA-specific human IgG ELISA To determine H7N9 HA-specific hIgG titers, 96-well Nunc Maxisorp ELISA plates were coated overnight at 4 °C with 100 μl/well of 2 μg/mL recombinant H7N9 HA1 (H7N9 HA1-rFc) in PBS.

    SDS Page:

    Article Title: Generation of H7N9-specific human polyclonal antibodies from a transchromosomic goat (caprine) system
    Article Snippet: The purified human IgG has a IgG concentration of 0.75 mg/ml in a sterile-filtered PBS buffer. .. Immunoglobulin heavy and light chains of purified human IgG and goat IgG were separated by SDS PAGE using 4–12% precast Bis-Tris gels (Invitrogen) and transferred to polyvinylidene difluoride membranes that were directly probed with donkey anti-hIgG (H + L) specific horseradish peroxidase (HRP)-conjugated antibody (Jackson ImmunoResearch) for hIgG heavy chain and light chain detection. .. To determine H7N9 HA-specific hIgG titers, 96-well Nunc Maxisorp ELISA plates were coated overnight at 4 °C with 100 μl/well of 2 μg/mL recombinant H7N9 HA1 (H7N9 HA1-rFc) in PBS.

    Article Title: Generation of H7N9-specific human polyclonal antibodies from a transchromosomic goat (caprine) system
    Article Snippet: The purified human IgG has a IgG concentration of 0.75 mg/ml in a sterile-filtered PBS buffer. .. Western blotting Immunoglobulin heavy and light chains of purified human IgG and goat IgG were separated by SDS PAGE using 4–12% precast Bis-Tris gels (Invitrogen) and transferred to polyvinylidene difluoride membranes that were directly probed with donkey anti-hIgG (H + L) specific horseradish peroxidase (HRP)-conjugated antibody (Jackson ImmunoResearch) for hIgG heavy chain and light chain detection. .. H7N9 HA-specific human IgG ELISA To determine H7N9 HA-specific hIgG titers, 96-well Nunc Maxisorp ELISA plates were coated overnight at 4 °C with 100 μl/well of 2 μg/mL recombinant H7N9 HA1 (H7N9 HA1-rFc) in PBS.

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  • 98
    Jackson Immuno anti goat horseradish peroxidase conjugated immunoglobulin g igg
    (A,B) Lactoferrin (Lf) fragments accumulate in macrophages following incubation with senescent neutrophils. (A) Peritoneal macrophages were recovered 66 h post zymosan A-induced (1 mg/mouse) peritonitis initiation and incubated with apoptotic Jurkat cells (AC), senescent peritoneal neutrophils (SN), latex beads (LBs), <t>IgG-opsonized</t> LB (oLB), or anti-CD11b monoclonal antibodies as indicated. After 24 h, unbound cells were washed and macrophages were recovered. Then, the cells were lysed, and equal amounts of protein extract were blotted for Lf. Protein extracts from apoptotic neutrophils were also analyzed as indicated. Results are representative from three independent experiments (cells were pooled from three to five mice). (B) Peritoneal neutrophils were recovered 24 h PPI and treated with roscovitine (10 µM) alone or with protease inhibitor cocktail (Pi), cycloheximide (CHX), or the neutrophil elastase inhibitor, silevestat (NEi) for 20 h. Then, neutrophils were lysed, and their protein content was immunoblotted for Lf [results are representative from three experiments (cells were pooled from three to five mice)]. (C,D) Lf fragments are found in interstitial fluids (ISFs) of spleen and inguinal lymph nodes (LN) during peritonitis. Spleen (C) and inguinal LN (D) were harvested 24 and 66 h after initiation of peritonitis ( n = 4–5) and mashed in equal volumes of PBS employing a nylon grid. Equal amounts of ISF protein were run by 10% sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS–PAGE), followed by Western blotting for Lf. Results are representative blots from three experiments. (E–G) Peritoneal resolution phase macrophages are essential for the differential production of splenic Lf fragments. Mice were injected intraperitoneally (i.p.) with clodronate-containing or empty liposomes 42 h PPI or before the initiation of peritonitis. After additional 24 h, the spleens were recovered and mashed in equal volumes of PBS employing a nylon grid. Equal amounts of ISF protein were run by 12% SDS-PAGE, followed by Western blotting for Lf. Results are a representative blot (E) and averages of densitometric analysis of the 23- (F) and 17 (G) -kDa bands from three experiments ( n = 3–6 mice per group). **/*indicate statistically significant differences of P ≤ 0.01/ P ≤ 0.05, respectively, by ANOVA with Tukey post hoc analysis. (H) Lf fragments are found in dairy cow milk during the onset and resolution of mastitis. Milk samples from dairy cows with mastitis (days 1–7) were defatted and separated into soluble and cellular fractions by centrifugation. The cellular fraction was lysed and the cytoplasmic proteins were recovered. Equal amounts of protein from both fractions were analyzed by Western blotting for Lf. Results show representative blots from three sample sets taken daily from three different cows.
    Anti Goat Horseradish Peroxidase Conjugated Immunoglobulin G Igg, supplied by Jackson Immuno, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti goat horseradish peroxidase conjugated immunoglobulin g igg/product/Jackson Immuno
    Average 98 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti goat horseradish peroxidase conjugated immunoglobulin g igg - by Bioz Stars, 2021-06
    98/100 stars
      Buy from Supplier

    96
    Jackson Immuno peroxidase conjugated anti mouse immunoglobulin g igg antibody
    Monoclonal antibodies specifically detect properdin in human serum. ( A ) Purified human properdin, human serum, recombinant mouse properdin, human embryonic kidney (HEK) cell supernatant and fetal calf serum were immobilized on an ELISA plate. In house mAb 1340 (1 µg/mL) and commercial mAb A235 (1 µg/mL) detected only purified human properdin or human serum, respectively. MAb A233 (1 µg/mL) detected all antigens tested. Shown are the respective means (± s.e.m.) for two independent experiments. After background subtraction data were normalized to mAb 1340 reactivity against properdin (set to 100%). ( B ) Human properdin was isolated from human serum by immunoprecipitation (IP) using mAb 1340 (left lane). The precipitated proteins and purified control properdin (right lane) were separated by non-reducing, denatured SDS-PAGE. Western blot detection was performed with mAb 1340 and a peroxidase conjugated anti-mouse <t>IgG</t> antibody. The generated mAb precipitated and detected properdin monomer (∼55 kDa), dimer (∼110 kDa) and trimer (∼165 kDa), respectively.
    Peroxidase Conjugated Anti Mouse Immunoglobulin G Igg Antibody, supplied by Jackson Immuno, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/peroxidase conjugated anti mouse immunoglobulin g igg antibody/product/Jackson Immuno
    Average 96 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    peroxidase conjugated anti mouse immunoglobulin g igg antibody - by Bioz Stars, 2021-06
    96/100 stars
      Buy from Supplier

    86
    Jackson Immuno goat anti mouse immunoglobulin g igg horseradish peroxidase conjugate
    Serum <t>IgG</t> subclass profiles from C57BL/6 (A) and C3H (B) mice vaccinated with rROP2, rGRA4, R + G (mix of rROP2 and rGRA4), or PBS combined with alum were determined 2 weeks after the last booster (day 28) and 4 weeks after oral infection with
    Goat Anti Mouse Immunoglobulin G Igg Horseradish Peroxidase Conjugate, supplied by Jackson Immuno, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/goat anti mouse immunoglobulin g igg horseradish peroxidase conjugate/product/Jackson Immuno
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    goat anti mouse immunoglobulin g igg horseradish peroxidase conjugate - by Bioz Stars, 2021-06
    86/100 stars
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    Image Search Results


    (A,B) Lactoferrin (Lf) fragments accumulate in macrophages following incubation with senescent neutrophils. (A) Peritoneal macrophages were recovered 66 h post zymosan A-induced (1 mg/mouse) peritonitis initiation and incubated with apoptotic Jurkat cells (AC), senescent peritoneal neutrophils (SN), latex beads (LBs), IgG-opsonized LB (oLB), or anti-CD11b monoclonal antibodies as indicated. After 24 h, unbound cells were washed and macrophages were recovered. Then, the cells were lysed, and equal amounts of protein extract were blotted for Lf. Protein extracts from apoptotic neutrophils were also analyzed as indicated. Results are representative from three independent experiments (cells were pooled from three to five mice). (B) Peritoneal neutrophils were recovered 24 h PPI and treated with roscovitine (10 µM) alone or with protease inhibitor cocktail (Pi), cycloheximide (CHX), or the neutrophil elastase inhibitor, silevestat (NEi) for 20 h. Then, neutrophils were lysed, and their protein content was immunoblotted for Lf [results are representative from three experiments (cells were pooled from three to five mice)]. (C,D) Lf fragments are found in interstitial fluids (ISFs) of spleen and inguinal lymph nodes (LN) during peritonitis. Spleen (C) and inguinal LN (D) were harvested 24 and 66 h after initiation of peritonitis ( n = 4–5) and mashed in equal volumes of PBS employing a nylon grid. Equal amounts of ISF protein were run by 10% sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS–PAGE), followed by Western blotting for Lf. Results are representative blots from three experiments. (E–G) Peritoneal resolution phase macrophages are essential for the differential production of splenic Lf fragments. Mice were injected intraperitoneally (i.p.) with clodronate-containing or empty liposomes 42 h PPI or before the initiation of peritonitis. After additional 24 h, the spleens were recovered and mashed in equal volumes of PBS employing a nylon grid. Equal amounts of ISF protein were run by 12% SDS-PAGE, followed by Western blotting for Lf. Results are a representative blot (E) and averages of densitometric analysis of the 23- (F) and 17 (G) -kDa bands from three experiments ( n = 3–6 mice per group). **/*indicate statistically significant differences of P ≤ 0.01/ P ≤ 0.05, respectively, by ANOVA with Tukey post hoc analysis. (H) Lf fragments are found in dairy cow milk during the onset and resolution of mastitis. Milk samples from dairy cows with mastitis (days 1–7) were defatted and separated into soluble and cellular fractions by centrifugation. The cellular fraction was lysed and the cytoplasmic proteins were recovered. Equal amounts of protein from both fractions were analyzed by Western blotting for Lf. Results show representative blots from three sample sets taken daily from three different cows.

    Journal: Frontiers in Immunology

    Article Title: A 17-kDa Fragment of Lactoferrin Associates With the Termination of Inflammation and Peptides Within Promote Resolution

    doi: 10.3389/fimmu.2018.00644

    Figure Lengend Snippet: (A,B) Lactoferrin (Lf) fragments accumulate in macrophages following incubation with senescent neutrophils. (A) Peritoneal macrophages were recovered 66 h post zymosan A-induced (1 mg/mouse) peritonitis initiation and incubated with apoptotic Jurkat cells (AC), senescent peritoneal neutrophils (SN), latex beads (LBs), IgG-opsonized LB (oLB), or anti-CD11b monoclonal antibodies as indicated. After 24 h, unbound cells were washed and macrophages were recovered. Then, the cells were lysed, and equal amounts of protein extract were blotted for Lf. Protein extracts from apoptotic neutrophils were also analyzed as indicated. Results are representative from three independent experiments (cells were pooled from three to five mice). (B) Peritoneal neutrophils were recovered 24 h PPI and treated with roscovitine (10 µM) alone or with protease inhibitor cocktail (Pi), cycloheximide (CHX), or the neutrophil elastase inhibitor, silevestat (NEi) for 20 h. Then, neutrophils were lysed, and their protein content was immunoblotted for Lf [results are representative from three experiments (cells were pooled from three to five mice)]. (C,D) Lf fragments are found in interstitial fluids (ISFs) of spleen and inguinal lymph nodes (LN) during peritonitis. Spleen (C) and inguinal LN (D) were harvested 24 and 66 h after initiation of peritonitis ( n = 4–5) and mashed in equal volumes of PBS employing a nylon grid. Equal amounts of ISF protein were run by 10% sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS–PAGE), followed by Western blotting for Lf. Results are representative blots from three experiments. (E–G) Peritoneal resolution phase macrophages are essential for the differential production of splenic Lf fragments. Mice were injected intraperitoneally (i.p.) with clodronate-containing or empty liposomes 42 h PPI or before the initiation of peritonitis. After additional 24 h, the spleens were recovered and mashed in equal volumes of PBS employing a nylon grid. Equal amounts of ISF protein were run by 12% SDS-PAGE, followed by Western blotting for Lf. Results are a representative blot (E) and averages of densitometric analysis of the 23- (F) and 17 (G) -kDa bands from three experiments ( n = 3–6 mice per group). **/*indicate statistically significant differences of P ≤ 0.01/ P ≤ 0.05, respectively, by ANOVA with Tukey post hoc analysis. (H) Lf fragments are found in dairy cow milk during the onset and resolution of mastitis. Milk samples from dairy cows with mastitis (days 1–7) were defatted and separated into soluble and cellular fractions by centrifugation. The cellular fraction was lysed and the cytoplasmic proteins were recovered. Equal amounts of protein from both fractions were analyzed by Western blotting for Lf. Results show representative blots from three sample sets taken daily from three different cows.

    Article Snippet: Reagents The following reagents were purchased as detailed: acrylamide/bis-acrylamide, fibronectin, lipopolysaccharide (LPS) (from Escherichia coli , clone 055:B5), staurosporine, TEMED, Tween-20, the neutrophil elastase inhibitor silevestat, and zymosan A from Sigma-Aldrich; clodronate from Liposoma BV; anti-goat horseradish peroxidase-conjugated immunoglobulin G (IgG) and anti-rabbit horseradish peroxidase-conjugated IgG from Jackson Immuno Research Laboratories; WesternBright™ ECL from Advansta, fetal calf serum (FCS), L-glutamine, penicillin–streptomycin, RPMI 1640 and trypan blue from Biological Industries, Kibbutz Beit Haemek; goat anti-mouse CD11b (M-19) polyclonal IgG and rabbit anti-human Lf (H-65) polyclonal IgG from SantaCruz Biotechnology; FITC-conjugated anti-mouse Gr-1, PE-conjugated anti-mouse F4/80, PerCP-conjugated anti-mouse CD11b, APC-conjugated anti-mouse CXCR4 (clone BL6-146508) and enzyme-linked immunosorbent assay (ELISA) kits for TNFα, IL-6, IL-12, and IL-10 from Biolegend; cycloheximide (CHX) from Cayman Chemical; PE selection kit was purchased from Stem Cell Technologies; and Protease Inhibitors Cocktail was purchased from Roche.

    Techniques: Incubation, Mouse Assay, Protease Inhibitor, Polyacrylamide Gel Electrophoresis, SDS Page, Western Blot, Injection, Centrifugation

    Monoclonal antibodies specifically detect properdin in human serum. ( A ) Purified human properdin, human serum, recombinant mouse properdin, human embryonic kidney (HEK) cell supernatant and fetal calf serum were immobilized on an ELISA plate. In house mAb 1340 (1 µg/mL) and commercial mAb A235 (1 µg/mL) detected only purified human properdin or human serum, respectively. MAb A233 (1 µg/mL) detected all antigens tested. Shown are the respective means (± s.e.m.) for two independent experiments. After background subtraction data were normalized to mAb 1340 reactivity against properdin (set to 100%). ( B ) Human properdin was isolated from human serum by immunoprecipitation (IP) using mAb 1340 (left lane). The precipitated proteins and purified control properdin (right lane) were separated by non-reducing, denatured SDS-PAGE. Western blot detection was performed with mAb 1340 and a peroxidase conjugated anti-mouse IgG antibody. The generated mAb precipitated and detected properdin monomer (∼55 kDa), dimer (∼110 kDa) and trimer (∼165 kDa), respectively.

    Journal: PLoS ONE

    Article Title: A Novel Antibody against Human Properdin Inhibits the Alternative Complement System and Specifically Detects Properdin from Blood Samples

    doi: 10.1371/journal.pone.0096371

    Figure Lengend Snippet: Monoclonal antibodies specifically detect properdin in human serum. ( A ) Purified human properdin, human serum, recombinant mouse properdin, human embryonic kidney (HEK) cell supernatant and fetal calf serum were immobilized on an ELISA plate. In house mAb 1340 (1 µg/mL) and commercial mAb A235 (1 µg/mL) detected only purified human properdin or human serum, respectively. MAb A233 (1 µg/mL) detected all antigens tested. Shown are the respective means (± s.e.m.) for two independent experiments. After background subtraction data were normalized to mAb 1340 reactivity against properdin (set to 100%). ( B ) Human properdin was isolated from human serum by immunoprecipitation (IP) using mAb 1340 (left lane). The precipitated proteins and purified control properdin (right lane) were separated by non-reducing, denatured SDS-PAGE. Western blot detection was performed with mAb 1340 and a peroxidase conjugated anti-mouse IgG antibody. The generated mAb precipitated and detected properdin monomer (∼55 kDa), dimer (∼110 kDa) and trimer (∼165 kDa), respectively.

    Article Snippet: Detection was performed with a peroxidase-conjugated anti-mouse immunoglobulin G (IgG) antibody (Jackson ImmunoResearch Laboratories, West Groove, USA) and 3,3′,5,5′-tetramethylbenzidine (TMB, Seramun, Wolzig, Germany).

    Techniques: Purification, Recombinant, Enzyme-linked Immunosorbent Assay, Isolation, Immunoprecipitation, SDS Page, Western Blot, Generated

    Anti-properdin antibodies show high avidity towards human properdin. The binding strengths of newly generated mAb 1340 as well as commercially available mAb A233 and mAb A235 were tested in an indirect ELISA. MAbs were serially diluted (1,000–0.1 ng/mL) and properdin binding was detected with a peroxidase conjugated anti-mouse IgG antibody. MAb 1340 (EC50 25 ng/mL), mAb A233 (EC50 11 ng/mL) and mAb A235 (EC50 15 ng/mL) showed comparable binding strengths towards immobilized human properdin. Shown are means (n = 9±s.e.m.) out of three independent experiments each with three replicates. After background subtraction, data were normalized to 1,000 ng/mL mAb 1340 reactivity against properdin (set to 100%).

    Journal: PLoS ONE

    Article Title: A Novel Antibody against Human Properdin Inhibits the Alternative Complement System and Specifically Detects Properdin from Blood Samples

    doi: 10.1371/journal.pone.0096371

    Figure Lengend Snippet: Anti-properdin antibodies show high avidity towards human properdin. The binding strengths of newly generated mAb 1340 as well as commercially available mAb A233 and mAb A235 were tested in an indirect ELISA. MAbs were serially diluted (1,000–0.1 ng/mL) and properdin binding was detected with a peroxidase conjugated anti-mouse IgG antibody. MAb 1340 (EC50 25 ng/mL), mAb A233 (EC50 11 ng/mL) and mAb A235 (EC50 15 ng/mL) showed comparable binding strengths towards immobilized human properdin. Shown are means (n = 9±s.e.m.) out of three independent experiments each with three replicates. After background subtraction, data were normalized to 1,000 ng/mL mAb 1340 reactivity against properdin (set to 100%).

    Article Snippet: Detection was performed with a peroxidase-conjugated anti-mouse immunoglobulin G (IgG) antibody (Jackson ImmunoResearch Laboratories, West Groove, USA) and 3,3′,5,5′-tetramethylbenzidine (TMB, Seramun, Wolzig, Germany).

    Techniques: Binding Assay, Generated, Indirect ELISA

    CLSM of RK13 cells transfected with ETIF expression plasmid pc-ETIF (A), RK-ETIF cells (B), and RK13 cells (C). ETIF was detected with MAb L3ab and visualized with anti-mouse IgG-Alexa Fluor 568 conjugate.

    Journal: Journal of Virology

    Article Title: The ?-TIF (VP16) Homologue (ETIF) of Equine Herpesvirus 1 Is Essential for Secondary Envelopment and Virus Egress

    doi: 10.1128/JVI.80.6.2609-2620.2006

    Figure Lengend Snippet: CLSM of RK13 cells transfected with ETIF expression plasmid pc-ETIF (A), RK-ETIF cells (B), and RK13 cells (C). ETIF was detected with MAb L3ab and visualized with anti-mouse IgG-Alexa Fluor 568 conjugate.

    Article Snippet: Bound antibodies were detected with anti-mouse immunoglobulin G (IgG)-peroxidase conjugates (Jackson Immunoresearch Laboratories) or anti-rabbit IgG-peroxidase conjugates (Pharmacia-Amersham) and visualized by enhanced chemiluminescence (ECL Kit; Pharmacia-Amersham).

    Techniques: Confocal Laser Scanning Microscopy, Transfection, Expressing, Plasmid Preparation

    IIF analysis of RK13 cells transfected with vL11ΔETIF DNA, RK-ETIF cells transfected with vL11ΔETIF DNA, and RK13 cells. Cells were fixed with acetone on day 3 after transfection and incubated with anti-gM MAb E2, which was visualized by using anti-mouse IgG Alexa 488 antibody (Molecular Probes). Individual panels represent views 1,000 by 1,000 μm in size.

    Journal: Journal of Virology

    Article Title: The ?-TIF (VP16) Homologue (ETIF) of Equine Herpesvirus 1 Is Essential for Secondary Envelopment and Virus Egress

    doi: 10.1128/JVI.80.6.2609-2620.2006

    Figure Lengend Snippet: IIF analysis of RK13 cells transfected with vL11ΔETIF DNA, RK-ETIF cells transfected with vL11ΔETIF DNA, and RK13 cells. Cells were fixed with acetone on day 3 after transfection and incubated with anti-gM MAb E2, which was visualized by using anti-mouse IgG Alexa 488 antibody (Molecular Probes). Individual panels represent views 1,000 by 1,000 μm in size.

    Article Snippet: Bound antibodies were detected with anti-mouse immunoglobulin G (IgG)-peroxidase conjugates (Jackson Immunoresearch Laboratories) or anti-rabbit IgG-peroxidase conjugates (Pharmacia-Amersham) and visualized by enhanced chemiluminescence (ECL Kit; Pharmacia-Amersham).

    Techniques: Transfection, Incubation

    Serum IgG subclass profiles from C57BL/6 (A) and C3H (B) mice vaccinated with rROP2, rGRA4, R + G (mix of rROP2 and rGRA4), or PBS combined with alum were determined 2 weeks after the last booster (day 28) and 4 weeks after oral infection with

    Journal: Clinical and Diagnostic Laboratory Immunology

    Article Title: Recombinant GRA4 or ROP2 Protein Combined with Alum or the gra4 Gene Provides Partial Protection in Chronic Murine Models of Toxoplasmosis

    doi: 10.1128/CDLI.11.4.704-710.2004

    Figure Lengend Snippet: Serum IgG subclass profiles from C57BL/6 (A) and C3H (B) mice vaccinated with rROP2, rGRA4, R + G (mix of rROP2 and rGRA4), or PBS combined with alum were determined 2 weeks after the last booster (day 28) and 4 weeks after oral infection with

    Article Snippet: Mouse sera were diluted in PBS and applied to the wells, followed by goat anti-mouse immunoglobulin G (IgG)-horseradish peroxidase conjugate as a secondary antibody (Jackson Immunoresearch Laboratories) diluted 1:4,000.

    Techniques: Mouse Assay, Infection