horseradish peroxidase conjugated secondary antibodies  (Promega)

 
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    Structured Review

    Promega horseradish peroxidase conjugated secondary antibodies
    Horseradish Peroxidase Conjugated Secondary Antibodies, supplied by Promega, used in various techniques. Bioz Stars score: 99/100, based on 38 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/horseradish peroxidase conjugated secondary antibodies/product/Promega
    Average 99 stars, based on 38 article reviews
    Price from $9.99 to $1999.99
    horseradish peroxidase conjugated secondary antibodies - by Bioz Stars, 2020-07
    99/100 stars

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    Transduction:

    Article Title: Protein kinase A-anchoring (AKAP) domains in brefeldin A-inhibited guanine nucleotide-exchange protein 2 (BIG2)
    Article Snippet: .. Mouse monoclonal antibodies against RIα, RIIα, and C subunits were purchased from BD Signal Transduction (Lexington, KY), chicken polyclonal anti-RIα antibody from Biomol (Plymouth Meeting, PA), horseradish peroxidase-conjugated anti-rabbit IgG, anti-mouse IgG, and anti-chicken IgY from Promega, normal mouse and rabbit IgG from Vector Laboratories, monoclonal LexA and c-myc antibodies from CLONTECH, polyclonal anti-c-myc and anti-hemagglutinin (HA) antibodies from Santa Cruz Biotechnology, and anti-FLAG antibodies from Sigma. ..

    Western Blot:

    Article Title: A TSG101/MDM2 regulatory loop modulates MDM2 degradation and MDM2/p53 feedback control
    Article Snippet: .. Antibodies used for Western blots were rabbit anti-TSG101 (1:200, CLONTECH), anti-p53 (DO-1, 1:1000, Santa Cruz Biotechnology), anti-HA (1:500, HRP-labeled, Roche), and anti-Flag (1:500, M2, Kodak), anti-α-tubulin (1:20000, Neomark), anti-rabbit IgG (1:5000, HRP-labeled, Promega) and anti-mouse IgG (1:10,000, HRP-labeled, Santa Cruz Biotechnology). .. Anti-GFP antibody was obtained from CLONTECH and was used at 1:500 dilution.

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    Promega horseradish peroxidise conjugated secondary antibodies
    Characterisation and purification of the royal jelly (RJ) component responsible for elevated MMP-9 production. ( A ) Heat and proteinase K treatment was performed by incubation of water royal jelly extract (WRJE) at 100 °C for 5 min and incubation with 150 μg/ml proteinase K for 1 h at 40 °C followed by heating to 98 °C for 10 min to inactivate the enzyme. Treated WRJE was incubated with HaCaT cells and conditioned equal volumes of the culture media were collected and subjected to gelatine zymography. Densitometric quantification of MMP-9 activity in culture media is presented. ( B ) Heat-treated WRJE was fractionated by a reverse phase-high performance liquid chromatography (RP-HPLC) on a C18 column (250 × 4.6 mm, 5 μm) at a flow rate 0.3 ml/min, with elution using a 10–90% gradient of acetonitrile (containing 0.1% (v/v) trifluoroacetic acid) for 85 min. ( C ) The HPLC fractions were assayed for MMP-9 induction. ( D ) HPLC fractions with maximal MMP-9 activity (51 to 59 min) were used for identification of MMP-9 inducer and were subjected to 16.5% Tricine-SDS-PAGE gels. Defensin-1 (5.5 kDa) was detected by Western blotting using a rabbit polyclonal anti-honeybee defensin-1 antibody diluted 1:2000 in blocking buffer. Horseradish <t>peroxidise-conjugated</t> secondary antibodies were applied. (The gels/blots with indicated cropping lines are shown in Supplementary Fig. S3 ). White line in gel indicates the place where two gels were spliced together. Data are expressed as means and SEMs of three independent measurements. Asterisks indicate a significant difference from the untreated group, * P
    Horseradish Peroxidise Conjugated Secondary Antibodies, supplied by Promega, used in various techniques. Bioz Stars score: 88/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/horseradish peroxidise conjugated secondary antibodies/product/Promega
    Average 88 stars, based on 3 article reviews
    Price from $9.99 to $1999.99
    horseradish peroxidise conjugated secondary antibodies - by Bioz Stars, 2020-07
    88/100 stars
      Buy from Supplier

    92
    Promega goat anti rabbit igg hrp conjugate
    Cleavage of caspase 3 (A) and 8 (B) in pancreatic cancer cell lines following rfhSP-D treatment. Pancreatic cancer cell lines were analyzed for caspase 8 and 3 activation via western blot using anti-rabbit cleaved caspase 3 and 8 (1:1,000) at 4°C overnight, followed by incubation with secondary anti-rabbit <t>IgG</t> <t>HRP-conjugate</t> (1:1,000) for 1 h at room temperature. The membrane was washed with PBST (PBS + 0.05% Tween 20) three times, 10 min each between each step. The bands were developed using 3,3′-diaminobenzidine substrate kit. The cleaved caspase 3 and 8 were detected only in the rfhSP-D treated samples of all cell lines, whereas no bands appeared in the untreated cell samples. Full-length caspase 8 bands are visible around 43 kDa. (C) Anti-GAPDH was used as a loading control.
    Goat Anti Rabbit Igg Hrp Conjugate, supplied by Promega, used in various techniques. Bioz Stars score: 92/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/goat anti rabbit igg hrp conjugate/product/Promega
    Average 92 stars, based on 3 article reviews
    Price from $9.99 to $1999.99
    goat anti rabbit igg hrp conjugate - by Bioz Stars, 2020-07
    92/100 stars
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    88
    Promega goat anti mouse hrp conjugate secondary antibody
    Western blots of Ste2p enriched samples that were probed for Ste2p using an <t>Anti-FLAG</t> antibody (anti-Ste2p blots – top panels) and for the receptor-ligand complex using <t>NeutrAvidin-HRP</t> (biotin signal blots – lower panels) when incubated
    Goat Anti Mouse Hrp Conjugate Secondary Antibody, supplied by Promega, 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/goat anti mouse hrp conjugate secondary antibody/product/Promega
    Average 88 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    goat anti mouse hrp conjugate secondary antibody - by Bioz Stars, 2020-07
    88/100 stars
      Buy from Supplier

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    Characterisation and purification of the royal jelly (RJ) component responsible for elevated MMP-9 production. ( A ) Heat and proteinase K treatment was performed by incubation of water royal jelly extract (WRJE) at 100 °C for 5 min and incubation with 150 μg/ml proteinase K for 1 h at 40 °C followed by heating to 98 °C for 10 min to inactivate the enzyme. Treated WRJE was incubated with HaCaT cells and conditioned equal volumes of the culture media were collected and subjected to gelatine zymography. Densitometric quantification of MMP-9 activity in culture media is presented. ( B ) Heat-treated WRJE was fractionated by a reverse phase-high performance liquid chromatography (RP-HPLC) on a C18 column (250 × 4.6 mm, 5 μm) at a flow rate 0.3 ml/min, with elution using a 10–90% gradient of acetonitrile (containing 0.1% (v/v) trifluoroacetic acid) for 85 min. ( C ) The HPLC fractions were assayed for MMP-9 induction. ( D ) HPLC fractions with maximal MMP-9 activity (51 to 59 min) were used for identification of MMP-9 inducer and were subjected to 16.5% Tricine-SDS-PAGE gels. Defensin-1 (5.5 kDa) was detected by Western blotting using a rabbit polyclonal anti-honeybee defensin-1 antibody diluted 1:2000 in blocking buffer. Horseradish peroxidise-conjugated secondary antibodies were applied. (The gels/blots with indicated cropping lines are shown in Supplementary Fig. S3 ). White line in gel indicates the place where two gels were spliced together. Data are expressed as means and SEMs of three independent measurements. Asterisks indicate a significant difference from the untreated group, * P

    Journal: Scientific Reports

    Article Title: Bee-derived antibacterial peptide, defensin-1, promotes wound re-epithelialisation in vitro and in vivo

    doi: 10.1038/s41598-017-07494-0

    Figure Lengend Snippet: Characterisation and purification of the royal jelly (RJ) component responsible for elevated MMP-9 production. ( A ) Heat and proteinase K treatment was performed by incubation of water royal jelly extract (WRJE) at 100 °C for 5 min and incubation with 150 μg/ml proteinase K for 1 h at 40 °C followed by heating to 98 °C for 10 min to inactivate the enzyme. Treated WRJE was incubated with HaCaT cells and conditioned equal volumes of the culture media were collected and subjected to gelatine zymography. Densitometric quantification of MMP-9 activity in culture media is presented. ( B ) Heat-treated WRJE was fractionated by a reverse phase-high performance liquid chromatography (RP-HPLC) on a C18 column (250 × 4.6 mm, 5 μm) at a flow rate 0.3 ml/min, with elution using a 10–90% gradient of acetonitrile (containing 0.1% (v/v) trifluoroacetic acid) for 85 min. ( C ) The HPLC fractions were assayed for MMP-9 induction. ( D ) HPLC fractions with maximal MMP-9 activity (51 to 59 min) were used for identification of MMP-9 inducer and were subjected to 16.5% Tricine-SDS-PAGE gels. Defensin-1 (5.5 kDa) was detected by Western blotting using a rabbit polyclonal anti-honeybee defensin-1 antibody diluted 1:2000 in blocking buffer. Horseradish peroxidise-conjugated secondary antibodies were applied. (The gels/blots with indicated cropping lines are shown in Supplementary Fig. S3 ). White line in gel indicates the place where two gels were spliced together. Data are expressed as means and SEMs of three independent measurements. Asterisks indicate a significant difference from the untreated group, * P

    Article Snippet: Rabbit polyclonal anti-bee defensin-1 (Def-1) was purchased from GenCust Europe (Luxembourg), and horseradish peroxidise-conjugated secondary antibodies were obtained from Promega (USA).

    Techniques: Purification, Incubation, Zymography, Activity Assay, High Performance Liquid Chromatography, Flow Cytometry, SDS Page, Western Blot, Blocking Assay

    Cleavage of caspase 3 (A) and 8 (B) in pancreatic cancer cell lines following rfhSP-D treatment. Pancreatic cancer cell lines were analyzed for caspase 8 and 3 activation via western blot using anti-rabbit cleaved caspase 3 and 8 (1:1,000) at 4°C overnight, followed by incubation with secondary anti-rabbit IgG HRP-conjugate (1:1,000) for 1 h at room temperature. The membrane was washed with PBST (PBS + 0.05% Tween 20) three times, 10 min each between each step. The bands were developed using 3,3′-diaminobenzidine substrate kit. The cleaved caspase 3 and 8 were detected only in the rfhSP-D treated samples of all cell lines, whereas no bands appeared in the untreated cell samples. Full-length caspase 8 bands are visible around 43 kDa. (C) Anti-GAPDH was used as a loading control.

    Journal: Frontiers in Immunology

    Article Title: A Recombinant Fragment of Human Surfactant Protein D induces Apoptosis in Pancreatic Cancer Cell Lines via Fas-Mediated Pathway

    doi: 10.3389/fimmu.2018.01126

    Figure Lengend Snippet: Cleavage of caspase 3 (A) and 8 (B) in pancreatic cancer cell lines following rfhSP-D treatment. Pancreatic cancer cell lines were analyzed for caspase 8 and 3 activation via western blot using anti-rabbit cleaved caspase 3 and 8 (1:1,000) at 4°C overnight, followed by incubation with secondary anti-rabbit IgG HRP-conjugate (1:1,000) for 1 h at room temperature. The membrane was washed with PBST (PBS + 0.05% Tween 20) three times, 10 min each between each step. The bands were developed using 3,3′-diaminobenzidine substrate kit. The cleaved caspase 3 and 8 were detected only in the rfhSP-D treated samples of all cell lines, whereas no bands appeared in the untreated cell samples. Full-length caspase 8 bands are visible around 43 kDa. (C) Anti-GAPDH was used as a loading control.

    Article Snippet: The membrane was incubated with rabbit anti-human caspase primary antibodies (anti-cleaved caspase 3; anti-cleaved caspase 8; Cell Signaling) at 4°C overnight, followed by incubation with secondary Goat anti-rabbit IgG HRP-conjugate (1:1,000; Promega) for 1 h at room temperature.

    Techniques: Activation Assay, Western Blot, Incubation

    Cleavage of caspase 3 (A) and 8 (B) in pancreatic cancer cell lines following rfhSP-D treatment. Pancreatic cancer cell lines were analyzed for caspase 8 and 3 activation via western blot using anti-rabbit cleaved caspase 3 and 8 (1:1,000) at 4°C overnight, followed by incubation with secondary anti-rabbit IgG HRP-conjugate (1:1,000) for 1 h at room temperature. The membrane was washed with PBST (PBS + 0.05% Tween 20) three times, 10 min each between each step. The bands were developed using 3,3′-diaminobenzidine substrate kit. The cleaved caspase 3 and 8 were detected only in the rfhSP-D treated samples of all cell lines, whereas no bands appeared in the untreated cell samples. Full-length caspase 8 bands are visible around 43 kDa. (C) Anti-GAPDH was used as a loading control.

    Journal: Frontiers in Immunology

    Article Title: A Recombinant Fragment of Human Surfactant Protein D induces Apoptosis in Pancreatic Cancer Cell Lines via Fas-Mediated Pathway

    doi: 10.3389/fimmu.2018.01126

    Figure Lengend Snippet: Cleavage of caspase 3 (A) and 8 (B) in pancreatic cancer cell lines following rfhSP-D treatment. Pancreatic cancer cell lines were analyzed for caspase 8 and 3 activation via western blot using anti-rabbit cleaved caspase 3 and 8 (1:1,000) at 4°C overnight, followed by incubation with secondary anti-rabbit IgG HRP-conjugate (1:1,000) for 1 h at room temperature. The membrane was washed with PBST (PBS + 0.05% Tween 20) three times, 10 min each between each step. The bands were developed using 3,3′-diaminobenzidine substrate kit. The cleaved caspase 3 and 8 were detected only in the rfhSP-D treated samples of all cell lines, whereas no bands appeared in the untreated cell samples. Full-length caspase 8 bands are visible around 43 kDa. (C) Anti-GAPDH was used as a loading control.

    Article Snippet: The membrane was incubated with rabbit anti-human caspase primary antibodies (anti-cleaved caspase 3; anti-cleaved caspase 8; Cell Signaling) at 4°C overnight, followed by incubation with secondary Goat anti-rabbit IgG HRP-conjugate (1:1,000; Promega) for 1 h at room temperature.

    Techniques: Activation Assay, Western Blot, Incubation

    Western blots of Ste2p enriched samples that were probed for Ste2p using an Anti-FLAG antibody (anti-Ste2p blots – top panels) and for the receptor-ligand complex using NeutrAvidin-HRP (biotin signal blots – lower panels) when incubated

    Journal: Biochimica et biophysica acta

    Article Title: Novobiocin and Peptide Analogs of α-factor are Positive Allosteric Modulators of the Yeast G Protein-Coupled Receptor Ste2p

    doi: 10.1016/j.bbamem.2014.12.024

    Figure Lengend Snippet: Western blots of Ste2p enriched samples that were probed for Ste2p using an Anti-FLAG antibody (anti-Ste2p blots – top panels) and for the receptor-ligand complex using NeutrAvidin-HRP (biotin signal blots – lower panels) when incubated

    Article Snippet: The FLAG blot was washed and then incubated with a goat anti-mouse HRP conjugate secondary antibody (Promega, Madison, WI) diluted 1:15,000 in TBST for three hours.

    Techniques: Western Blot, Incubation