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Promega peroxidase conjugated secondary antibody
Peroxidase Conjugated Secondary Antibody, supplied by Promega, used in various techniques. Bioz Stars score: 93/100, based on 49 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/peroxidase conjugated secondary antibody/product/Promega
Average 93 stars, based on 49 article reviews
Price from $9.99 to $1999.99
peroxidase conjugated secondary antibody - by Bioz Stars, 2020-07
93/100 stars

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Western Blot:

Article Title: Role of Connexin 43 in Helicobacter pylori VacA-Induced Cell Death
Article Snippet: .. Expression of Cx43 was assessed by Western blotting using a rabbit anti-Cx43 antibody (1:1,000; abcam) followed by a horseradish peroxidase-conjugated secondary antibody (1:10,000; Promega). .. Expression of β-actin or glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was monitored using anti-β-actin and anti-GAPDH antibodies (1:1,000; abcam) to ensure equal loading.

Article Title: A novel FLNC frameshift and an OBSCN variant in a family with distal muscular dystrophy
Article Snippet: .. Filters were washed three times with washing buffer (0.5% non-fat dry milk, 50 mM Tris-HCl pH 7.4, 150 mM NaCl, 0.2% Tween-20) for 10 min each, incubated with horseradish peroxidase-conjugated secondary antibody and detected using the ECL system (ECL Western Blot Detection Reagents, Promega) and high performance chemiluminescence films (Amesham Hyperfilm ECL, GE Healthcare). .. Densitometric analysis was performed using the ImageJ software.

Incubation:

Article Title: Triple negative breast cancers with amplification of JAK2 at the 9p24 loci demonstrate JAK2-specific dependence
Article Snippet: .. Immunoreactive bands were detected by enhanced chemiluminescence following incubation with horseradish peroxidase-conjugated secondary antibodies (Promega). .. BSK805 was obtained from Novartis and solubilized in DMSO for cell culture, or suspended in hydroxypropylmethylcellulose and tween 80.

Article Title: The Epstein-Barr Virus Immediate-Early Protein BZLF1 Induces Expression of E2F-1 and Other Proteins Involved in Cell Cycle Progression in Primary Keratinocytes and Gastric Carcinoma Cells
Article Snippet: .. The membranes were washed in wash buffer (1× PBS, 0.1% Tween 20) and incubated with horseradish peroxidase-conjugated secondary antibody (1:10,000) (Promega) at RT for 60 min. .. The membranes were washed in wash buffer, and proteins were detected by using an enhanced chemiluminescence (ECL) kit (Amersham).

Article Title: A novel FLNC frameshift and an OBSCN variant in a family with distal muscular dystrophy
Article Snippet: .. Filters were washed three times with washing buffer (0.5% non-fat dry milk, 50 mM Tris-HCl pH 7.4, 150 mM NaCl, 0.2% Tween-20) for 10 min each, incubated with horseradish peroxidase-conjugated secondary antibody and detected using the ECL system (ECL Western Blot Detection Reagents, Promega) and high performance chemiluminescence films (Amesham Hyperfilm ECL, GE Healthcare). .. Densitometric analysis was performed using the ImageJ software.

Article Title: Gas6 Promotes Oligodendrogenesis and Myelination in the Adult Central Nervous System and After Lysolecithin-Induced Demyelination
Article Snippet: .. Postincubation washing of the membrane (25 mM Tris-HCl, 150 mM NaCl, 0.05% Tween-20, pH 8.0) was followed by 1 h incubation with a horseradish peroxidase-conjugated secondary antibody (1:5000; Promega, Madison, USA; Dako, Denmark) at RT. .. Chemiluminescence detection reagent (Luminata Forte Western HRP Substrate, Millipore) was used to generate the signal, and bands were visualized using a CCD-based digital gel imaging system (Bio-Rad ChemiDoc™ MP Imaging System, Hemel Hempstead, UK).

Expressing:

Article Title: Role of Connexin 43 in Helicobacter pylori VacA-Induced Cell Death
Article Snippet: .. Expression of Cx43 was assessed by Western blotting using a rabbit anti-Cx43 antibody (1:1,000; abcam) followed by a horseradish peroxidase-conjugated secondary antibody (1:10,000; Promega). .. Expression of β-actin or glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was monitored using anti-β-actin and anti-GAPDH antibodies (1:1,000; abcam) to ensure equal loading.

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  • 88
    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
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    95
    Promega anti igg
    Humoral immune response characterization. Absolute anti-αSyn <t>IgM</t> (A) and relative anti-αSyn IgM (B) antibodies in serum from immunized mice. Absolute anti-αSyn <t>IgG</t> (C) and relative anti-αSyn IgG (D) antibodies in serum. The relative content of specific anti α-Syn IgM and IgG antibodies were calculated by dividing anti α-Syn IgM or IgG levels by the total corresponding antibody levels. AU: arbitrary units. Represented values are mean ± S.E.M. ( n = 5–7). Asterisks correspond to statistically significant differences between one particular group and the “vehicle” group. Hash signs indicate statistically significant differences between different groups. * /# P
    Anti Igg, supplied by Promega, used in various techniques. Bioz Stars score: 95/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti igg/product/Promega
    Average 95 stars, based on 9 article reviews
    Price from $9.99 to $1999.99
    anti igg - by Bioz Stars, 2020-07
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    88
    Promega peroxidase conjugated anti mouse igg secondary antibodies
    Differential secretion pattern and sub-cellular localization of APL1A-V5 alleles in hemocyte-like cell culture. A) Immunofluorescence analysis of 4a-3A hemocyte-like cells transfected with plasmids encoding V5-tagged APL1A 1 , APL1A 2 and APL1A 3 . Cells were stained with Hoechst 33342 to label nuclei (blue). Staining with a mouse anti-V5 <t>mAb</t> followed by anti-mouse Alexa 488-conjugated <t>IgG</t> (red) indicates that APL1A 1 exhibits a diffuse pattern in the cytoplasm whereas APL1A 2 and APL1A 3 are essentially localized in vesicles. Pictures were taken under equivalent exposure conditions. B) Immunoblot analysis of cells (C) and culture medium (M) of the 4a-3A hemocyte-like cell line transfected with plasmids encoding V5-tagged APL1A 1 , APL1A 2 and APL1A 3 under reducing (R) and non-reducing (NR) conditions. Immunoblots were probed with a mouse anti-V5 mAb, protein quantities on the different blots are not comparable. APL1A 1 is secreted in the culture medium as at least two protein complexes under non-reducing conditions, whereas APL1A 2 and APL1A 3 are retained in the cell cytoplasm and form only one protein complex under non-reducing conditions. Estimated sizes of monomeric APL1A forms including V5-tag are: 76 kDa (APL1A 1 ), 60 kDa (APL1A 2 ) and 51 kDa (APL1A 3 ). C) Amino acid alignment of cysteine-rich regions of the three Ngousso APL1A proteins and A. gambiae PEST APL1C. Numbers correspond to the amino acid positions. Blue stars represent stop codons, cysteine residues are highlighted in red. The cysteine residue corresponding to the position 562 in the APL1C sequence (APL1C C562 , black arrow) described by Povelones et al. [18] , is involved in the disulfide-linked complex formed between LRIM1 and APL1C and is only conserved in APL1A 1 . The same cysteine is also referred to as APL1C C551 in the APL1C protein published by Baxter et al. [34] .
    Peroxidase Conjugated Anti Mouse Igg Secondary Antibodies, 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/peroxidase conjugated anti mouse igg secondary antibodies/product/Promega
    Average 88 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
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    85
    Promega horseradish peroxidase conjugated secondary anti chicken igy antibody
    Regulation of Are2p due to alterations in heme metabolism or mutations in the HAP1 and ROX1 transcription factors. Microsomes from wild-type (BWG, lane 1; RZ253–6, lane 5), hap1 (lane 2), rox1 (lane 6), or hem1 (lanes 3 and 4 with 50 or 0.5 μg of δ-ALA per ml, respectively) cells grown to mid-logarithmic phase were prepared and resolved by denaturing gel electrophoresis (5 μg of total protein per lane). The proteins were transferred to nitrocellulose and probed with chicken <t>IgY</t> antibody generated against the NH 2 ). Detection of the immune complexes was attained by using a horseradish peroxidase-conjugated secondary anti-chicken IgY antibody (Promega) and the <t>ECL</t> Western blotting detection reagent (Amersham). Lanes 7 and 8 represent microsomes from are1 Δ are2 Δ cells carrying a vector control or ARE2 on YEpARE2. The indicated nonspecific band serves as a loading control.
    Horseradish Peroxidase Conjugated Secondary Anti Chicken Igy Antibody, supplied by Promega, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/horseradish peroxidase conjugated secondary anti chicken igy antibody/product/Promega
    Average 85 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    horseradish peroxidase conjugated secondary anti chicken igy antibody - by Bioz Stars, 2020-07
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    Image Search Results


    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

    Humoral immune response characterization. Absolute anti-αSyn IgM (A) and relative anti-αSyn IgM (B) antibodies in serum from immunized mice. Absolute anti-αSyn IgG (C) and relative anti-αSyn IgG (D) antibodies in serum. The relative content of specific anti α-Syn IgM and IgG antibodies were calculated by dividing anti α-Syn IgM or IgG levels by the total corresponding antibody levels. AU: arbitrary units. Represented values are mean ± S.E.M. ( n = 5–7). Asterisks correspond to statistically significant differences between one particular group and the “vehicle” group. Hash signs indicate statistically significant differences between different groups. * /# P

    Journal: Immunity, Inflammation and Disease

    Article Title: Chaperoned amyloid proteins for immune manipulation: α-Synuclein/Hsp70 shifts immunity toward a modulatory phenotype

    doi: 10.1002/iid3.39

    Figure Lengend Snippet: Humoral immune response characterization. Absolute anti-αSyn IgM (A) and relative anti-αSyn IgM (B) antibodies in serum from immunized mice. Absolute anti-αSyn IgG (C) and relative anti-αSyn IgG (D) antibodies in serum. The relative content of specific anti α-Syn IgM and IgG antibodies were calculated by dividing anti α-Syn IgM or IgG levels by the total corresponding antibody levels. AU: arbitrary units. Represented values are mean ± S.E.M. ( n = 5–7). Asterisks correspond to statistically significant differences between one particular group and the “vehicle” group. Hash signs indicate statistically significant differences between different groups. * /# P

    Article Snippet: After washing as in the previous step, wells were incubated for 1 h at 37°C with anti-IgM-(Miltenyi, Bergisch Gladbach, Germany) or anti-IgG- (Promega, Madison, WI, USA) -HRP conjugated secondary antibodies diluted 1:4000 in Assay Diluent (BD Biosciences, San Diego, CA, USA).

    Techniques: Mouse Assay

    Differential secretion pattern and sub-cellular localization of APL1A-V5 alleles in hemocyte-like cell culture. A) Immunofluorescence analysis of 4a-3A hemocyte-like cells transfected with plasmids encoding V5-tagged APL1A 1 , APL1A 2 and APL1A 3 . Cells were stained with Hoechst 33342 to label nuclei (blue). Staining with a mouse anti-V5 mAb followed by anti-mouse Alexa 488-conjugated IgG (red) indicates that APL1A 1 exhibits a diffuse pattern in the cytoplasm whereas APL1A 2 and APL1A 3 are essentially localized in vesicles. Pictures were taken under equivalent exposure conditions. B) Immunoblot analysis of cells (C) and culture medium (M) of the 4a-3A hemocyte-like cell line transfected with plasmids encoding V5-tagged APL1A 1 , APL1A 2 and APL1A 3 under reducing (R) and non-reducing (NR) conditions. Immunoblots were probed with a mouse anti-V5 mAb, protein quantities on the different blots are not comparable. APL1A 1 is secreted in the culture medium as at least two protein complexes under non-reducing conditions, whereas APL1A 2 and APL1A 3 are retained in the cell cytoplasm and form only one protein complex under non-reducing conditions. Estimated sizes of monomeric APL1A forms including V5-tag are: 76 kDa (APL1A 1 ), 60 kDa (APL1A 2 ) and 51 kDa (APL1A 3 ). C) Amino acid alignment of cysteine-rich regions of the three Ngousso APL1A proteins and A. gambiae PEST APL1C. Numbers correspond to the amino acid positions. Blue stars represent stop codons, cysteine residues are highlighted in red. The cysteine residue corresponding to the position 562 in the APL1C sequence (APL1C C562 , black arrow) described by Povelones et al. [18] , is involved in the disulfide-linked complex formed between LRIM1 and APL1C and is only conserved in APL1A 1 . The same cysteine is also referred to as APL1C C551 in the APL1C protein published by Baxter et al. [34] .

    Journal: PLoS ONE

    Article Title: Diverged Alleles of the Anopheles gambiae Leucine-Rich Repeat Gene APL1A Display Distinct Protective Profiles against Plasmodium falciparum

    doi: 10.1371/journal.pone.0052684

    Figure Lengend Snippet: Differential secretion pattern and sub-cellular localization of APL1A-V5 alleles in hemocyte-like cell culture. A) Immunofluorescence analysis of 4a-3A hemocyte-like cells transfected with plasmids encoding V5-tagged APL1A 1 , APL1A 2 and APL1A 3 . Cells were stained with Hoechst 33342 to label nuclei (blue). Staining with a mouse anti-V5 mAb followed by anti-mouse Alexa 488-conjugated IgG (red) indicates that APL1A 1 exhibits a diffuse pattern in the cytoplasm whereas APL1A 2 and APL1A 3 are essentially localized in vesicles. Pictures were taken under equivalent exposure conditions. B) Immunoblot analysis of cells (C) and culture medium (M) of the 4a-3A hemocyte-like cell line transfected with plasmids encoding V5-tagged APL1A 1 , APL1A 2 and APL1A 3 under reducing (R) and non-reducing (NR) conditions. Immunoblots were probed with a mouse anti-V5 mAb, protein quantities on the different blots are not comparable. APL1A 1 is secreted in the culture medium as at least two protein complexes under non-reducing conditions, whereas APL1A 2 and APL1A 3 are retained in the cell cytoplasm and form only one protein complex under non-reducing conditions. Estimated sizes of monomeric APL1A forms including V5-tag are: 76 kDa (APL1A 1 ), 60 kDa (APL1A 2 ) and 51 kDa (APL1A 3 ). C) Amino acid alignment of cysteine-rich regions of the three Ngousso APL1A proteins and A. gambiae PEST APL1C. Numbers correspond to the amino acid positions. Blue stars represent stop codons, cysteine residues are highlighted in red. The cysteine residue corresponding to the position 562 in the APL1C sequence (APL1C C562 , black arrow) described by Povelones et al. [18] , is involved in the disulfide-linked complex formed between LRIM1 and APL1C and is only conserved in APL1A 1 . The same cysteine is also referred to as APL1C C551 in the APL1C protein published by Baxter et al. [34] .

    Article Snippet: After protein transfer to PVDF membrane, immunoblots were blocked for 1 hour in 5% nonfat dry milk, probed with a mouse mAb anti-V5 antibody at 1∶5000, followed by 1 hour with horseradish peroxidase-conjugated anti-mouse IgG secondary antibodies (Promega) at 1∶10 000.

    Techniques: Cell Culture, Immunofluorescence, Transfection, Staining, Western Blot, Sequencing

    Regulation of Are2p due to alterations in heme metabolism or mutations in the HAP1 and ROX1 transcription factors. Microsomes from wild-type (BWG, lane 1; RZ253–6, lane 5), hap1 (lane 2), rox1 (lane 6), or hem1 (lanes 3 and 4 with 50 or 0.5 μg of δ-ALA per ml, respectively) cells grown to mid-logarithmic phase were prepared and resolved by denaturing gel electrophoresis (5 μg of total protein per lane). The proteins were transferred to nitrocellulose and probed with chicken IgY antibody generated against the NH 2 ). Detection of the immune complexes was attained by using a horseradish peroxidase-conjugated secondary anti-chicken IgY antibody (Promega) and the ECL Western blotting detection reagent (Amersham). Lanes 7 and 8 represent microsomes from are1 Δ are2 Δ cells carrying a vector control or ARE2 on YEpARE2. The indicated nonspecific band serves as a loading control.

    Journal: Journal of Bacteriology

    Article Title: Transcriptional Regulation of the Two Sterol Esterification Genes in the Yeast Saccharomyces cerevisiae

    doi: 10.1128/JB.183.17.4950-4957.2001

    Figure Lengend Snippet: Regulation of Are2p due to alterations in heme metabolism or mutations in the HAP1 and ROX1 transcription factors. Microsomes from wild-type (BWG, lane 1; RZ253–6, lane 5), hap1 (lane 2), rox1 (lane 6), or hem1 (lanes 3 and 4 with 50 or 0.5 μg of δ-ALA per ml, respectively) cells grown to mid-logarithmic phase were prepared and resolved by denaturing gel electrophoresis (5 μg of total protein per lane). The proteins were transferred to nitrocellulose and probed with chicken IgY antibody generated against the NH 2 ). Detection of the immune complexes was attained by using a horseradish peroxidase-conjugated secondary anti-chicken IgY antibody (Promega) and the ECL Western blotting detection reagent (Amersham). Lanes 7 and 8 represent microsomes from are1 Δ are2 Δ cells carrying a vector control or ARE2 on YEpARE2. The indicated nonspecific band serves as a loading control.

    Article Snippet: The proteins were electroblotted to nitrocellulose, blocked in 5% nonfat milk in 20 mM Tris-HCl–137 mM NaCl–0.1% Tween 20 (TBST), and probed at 3.4 μg/ml with chicken immunoglobulin Y (IgY) antibody generated against the NH2 -terminal 180 residues of Are2p ( ) in TBST–1% nonfat milk for 1 h. Detection of the immune complexes was attained by using horseradish peroxidase-conjugated secondary anti-chicken IgY antibody (Promega) and the ECL Western blotting detection reagent (Amersham).

    Techniques: Nucleic Acid Electrophoresis, Generated, Western Blot, Plasmid Preparation