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rabbit anti cpe antibodies  (Bio-Rad)


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    Structured Review

    Bio-Rad rabbit anti cpe antibodies
    Rabbit Anti Cpe Antibodies, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 96/100, based on 1746 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rabbit+polyclonal+anti+cpe/pm40618853-62-15-19?v=Bio-Rad
    Average 96 stars, based on 1746 article reviews
    rabbit anti cpe antibodies - by Bioz Stars, 2026-07
    96/100 stars

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    C. <t>perfringens</t> toxinotype and <t>CPE</t> expressed in CP1 and CP_2. ( A ). CP1 and CP_2 DNA was toxinotyped by PCR. Showed were the PCR gel image. ( B ). CP1 and CP_2 were vegetatively grown in FTG or induced sporulation in DSSM, and the soluble proteins were isolated by precipitating using ammonium sulfate method. After dissolved in pH 6.8 PBS, the soluble supernatant proteins were subjected to Western Blot analysis with anti-CPE primary Ab. ( C ). WB quantification using ImageJ. The Western Blot image of CPE expression is shown. Different letters mean significant.
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    C. <t>perfringens</t> toxinotype and <t>CPE</t> expressed in CP1 and CP_2. ( A ). CP1 and CP_2 DNA was toxinotyped by PCR. Showed were the PCR gel image. ( B ). CP1 and CP_2 were vegetatively grown in FTG or induced sporulation in DSSM, and the soluble proteins were isolated by precipitating using ammonium sulfate method. After dissolved in pH 6.8 PBS, the soluble supernatant proteins were subjected to Western Blot analysis with anti-CPE primary Ab. ( C ). WB quantification using ImageJ. The Western Blot image of CPE expression is shown. Different letters mean significant.
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    C. <t>perfringens</t> toxinotype and <t>CPE</t> expressed in CP1 and CP_2. ( A ). CP1 and CP_2 DNA was toxinotyped by PCR. Showed were the PCR gel image. ( B ). CP1 and CP_2 were vegetatively grown in FTG or induced sporulation in DSSM, and the soluble proteins were isolated by precipitating using ammonium sulfate method. After dissolved in pH 6.8 PBS, the soluble supernatant proteins were subjected to Western Blot analysis with anti-CPE primary Ab. ( C ). WB quantification using ImageJ. The Western Blot image of CPE expression is shown. Different letters mean significant.
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    C. <t>perfringens</t> toxinotype and <t>CPE</t> expressed in CP1 and CP_2. ( A ). CP1 and CP_2 DNA was toxinotyped by PCR. Showed were the PCR gel image. ( B ). CP1 and CP_2 were vegetatively grown in FTG or induced sporulation in DSSM, and the soluble proteins were isolated by precipitating using ammonium sulfate method. After dissolved in pH 6.8 PBS, the soluble supernatant proteins were subjected to Western Blot analysis with anti-CPE primary Ab. ( C ). WB quantification using ImageJ. The Western Blot image of CPE expression is shown. Different letters mean significant.
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    C. <t>perfringens</t> toxinotype and <t>CPE</t> expressed in CP1 and CP_2. ( A ). CP1 and CP_2 DNA was toxinotyped by PCR. Showed were the PCR gel image. ( B ). CP1 and CP_2 were vegetatively grown in FTG or induced sporulation in DSSM, and the soluble proteins were isolated by precipitating using ammonium sulfate method. After dissolved in pH 6.8 PBS, the soluble supernatant proteins were subjected to Western Blot analysis with anti-CPE primary Ab. ( C ). WB quantification using ImageJ. The Western Blot image of CPE expression is shown. Different letters mean significant.
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    C. <t>perfringens</t> toxinotype and <t>CPE</t> expressed in CP1 and CP_2. ( A ). CP1 and CP_2 DNA was toxinotyped by PCR. Showed were the PCR gel image. ( B ). CP1 and CP_2 were vegetatively grown in FTG or induced sporulation in DSSM, and the soluble proteins were isolated by precipitating using ammonium sulfate method. After dissolved in pH 6.8 PBS, the soluble supernatant proteins were subjected to Western Blot analysis with anti-CPE primary Ab. ( C ). WB quantification using ImageJ. The Western Blot image of CPE expression is shown. Different letters mean significant.
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    C. <t>perfringens</t> toxinotype and <t>CPE</t> expressed in CP1 and CP_2. ( A ). CP1 and CP_2 DNA was toxinotyped by PCR. Showed were the PCR gel image. ( B ). CP1 and CP_2 were vegetatively grown in FTG or induced sporulation in DSSM, and the soluble proteins were isolated by precipitating using ammonium sulfate method. After dissolved in pH 6.8 PBS, the soluble supernatant proteins were subjected to Western Blot analysis with anti-CPE primary Ab. ( C ). WB quantification using ImageJ. The Western Blot image of CPE expression is shown. Different letters mean significant.
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    Image Search Results


    C. perfringens toxinotype and CPE expressed in CP1 and CP_2. ( A ). CP1 and CP_2 DNA was toxinotyped by PCR. Showed were the PCR gel image. ( B ). CP1 and CP_2 were vegetatively grown in FTG or induced sporulation in DSSM, and the soluble proteins were isolated by precipitating using ammonium sulfate method. After dissolved in pH 6.8 PBS, the soluble supernatant proteins were subjected to Western Blot analysis with anti-CPE primary Ab. ( C ). WB quantification using ImageJ. The Western Blot image of CPE expression is shown. Different letters mean significant.

    Journal: Microorganisms

    Article Title: Vaccines Using Clostridium perfringens Sporulation Proteins Reduce Necrotic Enteritis in Chickens

    doi: 10.3390/microorganisms10061110

    Figure Lengend Snippet: C. perfringens toxinotype and CPE expressed in CP1 and CP_2. ( A ). CP1 and CP_2 DNA was toxinotyped by PCR. Showed were the PCR gel image. ( B ). CP1 and CP_2 were vegetatively grown in FTG or induced sporulation in DSSM, and the soluble proteins were isolated by precipitating using ammonium sulfate method. After dissolved in pH 6.8 PBS, the soluble supernatant proteins were subjected to Western Blot analysis with anti-CPE primary Ab. ( C ). WB quantification using ImageJ. The Western Blot image of CPE expression is shown. Different letters mean significant.

    Article Snippet: The membrane was then incubated with 1:1000 dilution of primary rabbit polyclonal anti- C. perfringens enterotoxin (CPE) (cat# 64-052 BioAcademia, Suita, Osaka, Japan), anti-p-MLKL (cat# 37333), anti-cleaved Caspase 3 (cat# 9664), anti-RIP3 (cat# 15828), or anti-Actin (cat# 4970S) antibody (Ab) (the latter four rabbit anti-mouse mAb from Cell Signaling, Danvers, MA, USA) overnight at 4 °C.

    Techniques: Isolation, Western Blot, Expressing

    CP-spor-super vaccines protected birds against NE-induced body weight gain loss. Cohorts of 7–16 birds were fed basal diet and immunized with various CP-spor-super vaccines at d 0 and 10. To induce necrotic enteritis (NE), the birds were infected with 20,000 oocysts/bird E. maxima at 16 days of age and then infected with 10 9 CFU/bird C. perfringens at 20 days of age. The birds were sacrificed at 21 days of age. The daily body weight gain during noninfected phase of d 0–16, E. maxima phase of d 16–20, and NE phase of d 20–21 are shown. All graphs depict mean ± SEM. Different letters of a, b, and c mean p < 0.05. Results are representative of two independent experiments.

    Journal: Microorganisms

    Article Title: Vaccines Using Clostridium perfringens Sporulation Proteins Reduce Necrotic Enteritis in Chickens

    doi: 10.3390/microorganisms10061110

    Figure Lengend Snippet: CP-spor-super vaccines protected birds against NE-induced body weight gain loss. Cohorts of 7–16 birds were fed basal diet and immunized with various CP-spor-super vaccines at d 0 and 10. To induce necrotic enteritis (NE), the birds were infected with 20,000 oocysts/bird E. maxima at 16 days of age and then infected with 10 9 CFU/bird C. perfringens at 20 days of age. The birds were sacrificed at 21 days of age. The daily body weight gain during noninfected phase of d 0–16, E. maxima phase of d 16–20, and NE phase of d 20–21 are shown. All graphs depict mean ± SEM. Different letters of a, b, and c mean p < 0.05. Results are representative of two independent experiments.

    Article Snippet: The membrane was then incubated with 1:1000 dilution of primary rabbit polyclonal anti- C. perfringens enterotoxin (CPE) (cat# 64-052 BioAcademia, Suita, Osaka, Japan), anti-p-MLKL (cat# 37333), anti-cleaved Caspase 3 (cat# 9664), anti-RIP3 (cat# 15828), or anti-Actin (cat# 4970S) antibody (Ab) (the latter four rabbit anti-mouse mAb from Cell Signaling, Danvers, MA, USA) overnight at 4 °C.

    Techniques: Vaccines, Infection

    CP1-2 vaccine reduced C. perfringens colonization and invasion in the small intestine of NE birds. Bird experiment was conducted as in . ( A ) Luminal C. perfringens colonization level in the intestinal content. ( B ) C. perfringens invasion level in the intestinal tissue. All graphs depict mean ± SEM. ***, p < 0.001; **, p < 0.01. Results are representative of two independent experiments.

    Journal: Microorganisms

    Article Title: Vaccines Using Clostridium perfringens Sporulation Proteins Reduce Necrotic Enteritis in Chickens

    doi: 10.3390/microorganisms10061110

    Figure Lengend Snippet: CP1-2 vaccine reduced C. perfringens colonization and invasion in the small intestine of NE birds. Bird experiment was conducted as in . ( A ) Luminal C. perfringens colonization level in the intestinal content. ( B ) C. perfringens invasion level in the intestinal tissue. All graphs depict mean ± SEM. ***, p < 0.001; **, p < 0.01. Results are representative of two independent experiments.

    Article Snippet: The membrane was then incubated with 1:1000 dilution of primary rabbit polyclonal anti- C. perfringens enterotoxin (CPE) (cat# 64-052 BioAcademia, Suita, Osaka, Japan), anti-p-MLKL (cat# 37333), anti-cleaved Caspase 3 (cat# 9664), anti-RIP3 (cat# 15828), or anti-Actin (cat# 4970S) antibody (Ab) (the latter four rabbit anti-mouse mAb from Cell Signaling, Danvers, MA, USA) overnight at 4 °C.

    Techniques: