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Austral Biologicals rabbit anti caga
Rabbit Anti Caga, supplied by Austral Biologicals, used in various techniques. Bioz Stars score: 91/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/rabbit anti caga/product/Austral Biologicals
Average 91 stars, based on 2 article reviews
Price from $9.99 to $1999.99
rabbit anti caga - by Bioz Stars, 2020-09
91/100 stars

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Article Title: Nod1 imprints inflammatory and carcinogenic responses toward the gastric pathogen Helicobacter pylori
Article Snippet: .. Incubation with primary antibodies (mouse anti-PY99 (Santa Cruz Biotechnology), rabbit anti-CagA (Austral Biologicals), and mouse anti-GAPDH (Millipore) was performed for 1 hour followed by addition of respective HRP-conjugated secondary antibodies (anti-mouse-HRP or anti-rabbit-HRP; Promega). .. The reaction was developed using ECL (Thermo Scientific).

other:

Article Title: Fallacy of the Unique Genome: Sequence Diversity within Single Helicobacter pylori Strains
Article Snippet: Enhanced chemiluminescence (ECL) reagents were utilized for visualization of bound antibody (Thermo Scientific).

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    Austral Biologicals rabbit polyclonal α caga antibody
    <t>CagA</t> injection by H. pylori cannot be achieved in infected HEK293 cell lines but in AGS gastric epithelial cells. Western blot analysis of (A) AGS, (B) HEK293-TLR2, (C) HEK293 and (D) HEK293-TLR5 cells infected with H. pylori wild-type strains P1, P12, P310 or 26695 for 6 hours. Phosphorylation of injected CagA was monitored using phosphotyrosine α-PY-99 and <t>α-CagA</t> antibodies. Red arrows indicate the position of phosphorylated CagA on the blot. Western blots for the house keeping gene GAPDH served as loading control.
    Rabbit Polyclonal α Caga Antibody, supplied by Austral Biologicals, used in various techniques. Bioz Stars score: 88/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit polyclonal α caga antibody/product/Austral Biologicals
    Average 88 stars, based on 6 article reviews
    Price from $9.99 to $1999.99
    rabbit polyclonal α caga antibody - by Bioz Stars, 2020-09
    88/100 stars
      Buy from Supplier

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    CagA injection by H. pylori cannot be achieved in infected HEK293 cell lines but in AGS gastric epithelial cells. Western blot analysis of (A) AGS, (B) HEK293-TLR2, (C) HEK293 and (D) HEK293-TLR5 cells infected with H. pylori wild-type strains P1, P12, P310 or 26695 for 6 hours. Phosphorylation of injected CagA was monitored using phosphotyrosine α-PY-99 and α-CagA antibodies. Red arrows indicate the position of phosphorylated CagA on the blot. Western blots for the house keeping gene GAPDH served as loading control.

    Journal: PLoS ONE

    Article Title: Induction of TLR-2 and TLR-5 Expression by Helicobacter pylori Switches cagPAI-Dependent Signalling Leading to the Secretion of IL-8 and TNF-?

    doi: 10.1371/journal.pone.0019614

    Figure Lengend Snippet: CagA injection by H. pylori cannot be achieved in infected HEK293 cell lines but in AGS gastric epithelial cells. Western blot analysis of (A) AGS, (B) HEK293-TLR2, (C) HEK293 and (D) HEK293-TLR5 cells infected with H. pylori wild-type strains P1, P12, P310 or 26695 for 6 hours. Phosphorylation of injected CagA was monitored using phosphotyrosine α-PY-99 and α-CagA antibodies. Red arrows indicate the position of phosphorylated CagA on the blot. Western blots for the house keeping gene GAPDH served as loading control.

    Article Snippet: Phosphorylated and non-phosphorylated CagA proteins were detected by incubation of the membranes with a mouse monoclonal α-phosphotyrosine antibody PY99 (Santa Cruz, USA) and a rabbit polyclonal α-CagA antibody (Austral Biologicals, USA).

    Techniques: Injection, Infection, Western Blot

    Elevated E-cadherin cleavage and CagA translocation in host cells by overexpression of HtrA. Polarized MKN-28 cells were infected with IPTG-induced or control Hp wt or Hp htrA 26695 for 24 h. a Cell pellets and supernatants were prepared and subjected to α-E-cadherin Western blotting. The full-length E-cadherin signals (130 kDa) in the cell pellets and cleaved-off NTF-domain (90 kDa) in the culture supernatants are marked with arrows . b Translocation and phosphorylation of CagA ( arrow ) were analyzed using α-PY-99 and α-CagA antibodies, respectively. The asterisk marks a phosphorylated 125 kDa host cell protein migrating below CagA. c The band intensities of cleaved E-cadherin NTF-fragments and phospho-CagA signals were quantified densitometrically. The relative amounts of NTF-fragment and phosphorylated CagA are given in “fold change”. All experiments were done in triplicates

    Journal: Gut Pathogens

    Article Title: Overexpression of serine protease HtrA enhances disruption of adherens junctions, paracellular transmigration and type IV secretion of CagA by Helicobacter pylori

    doi: 10.1186/s13099-017-0189-6

    Figure Lengend Snippet: Elevated E-cadherin cleavage and CagA translocation in host cells by overexpression of HtrA. Polarized MKN-28 cells were infected with IPTG-induced or control Hp wt or Hp htrA 26695 for 24 h. a Cell pellets and supernatants were prepared and subjected to α-E-cadherin Western blotting. The full-length E-cadherin signals (130 kDa) in the cell pellets and cleaved-off NTF-domain (90 kDa) in the culture supernatants are marked with arrows . b Translocation and phosphorylation of CagA ( arrow ) were analyzed using α-PY-99 and α-CagA antibodies, respectively. The asterisk marks a phosphorylated 125 kDa host cell protein migrating below CagA. c The band intensities of cleaved E-cadherin NTF-fragments and phospho-CagA signals were quantified densitometrically. The relative amounts of NTF-fragment and phosphorylated CagA are given in “fold change”. All experiments were done in triplicates

    Article Snippet: Antibodies The following antibodies were purchased: rabbit polyclonal α-CagA antibody (Austral Biologicals, San Ramon, CA/USA), monoclonal pan-phosphotyrosine α-PY99 (Santa Cruz, Santa Cruz, CA/USA), rabbit α-GAPDH (Santa Cruz), rabbit α-H. pylori (Dako, Glostrup/Denmark) and two monoclonal antibodies directed against the extracellular domain of E-cadherin, H-108 (Santa Cruz) and CD324 (BD Biosciences, San Jose, CA/USA).

    Techniques: Translocation Assay, Over Expression, Infection, Western Blot

    Chromosomal introduction of a second, inducible htrA gene copy in H. pylori. a Schematic presentation of the IPTG-inducible htrA 26695 expression construct with the chloramphenicol acetyl-transferase (CAT) cassette ( top ), which was cloned into the plasticity region of H. pylori between genes HP0999 and HP1000 ( bottom ). b This construct was transformed into H. pylori wild-type ( Hp wt) strains 26695 and P12, and the expression of HtrA was investigated after 24 h growth in BHI medium in the presence or absence of 1 or 2 mM IPTG, respectively. The results for strain 26695 are shown. Western blotting using α-FlaA and α-CagA antibodies served as controls, indicating that equal amounts of proteins are present in the samples. c The band intensities of HtrA proteins were quantified densitometrically. The relative protein expression is given in “fold change”

    Journal: Gut Pathogens

    Article Title: Overexpression of serine protease HtrA enhances disruption of adherens junctions, paracellular transmigration and type IV secretion of CagA by Helicobacter pylori

    doi: 10.1186/s13099-017-0189-6

    Figure Lengend Snippet: Chromosomal introduction of a second, inducible htrA gene copy in H. pylori. a Schematic presentation of the IPTG-inducible htrA 26695 expression construct with the chloramphenicol acetyl-transferase (CAT) cassette ( top ), which was cloned into the plasticity region of H. pylori between genes HP0999 and HP1000 ( bottom ). b This construct was transformed into H. pylori wild-type ( Hp wt) strains 26695 and P12, and the expression of HtrA was investigated after 24 h growth in BHI medium in the presence or absence of 1 or 2 mM IPTG, respectively. The results for strain 26695 are shown. Western blotting using α-FlaA and α-CagA antibodies served as controls, indicating that equal amounts of proteins are present in the samples. c The band intensities of HtrA proteins were quantified densitometrically. The relative protein expression is given in “fold change”

    Article Snippet: Antibodies The following antibodies were purchased: rabbit polyclonal α-CagA antibody (Austral Biologicals, San Ramon, CA/USA), monoclonal pan-phosphotyrosine α-PY99 (Santa Cruz, Santa Cruz, CA/USA), rabbit α-GAPDH (Santa Cruz), rabbit α-H. pylori (Dako, Glostrup/Denmark) and two monoclonal antibodies directed against the extracellular domain of E-cadherin, H-108 (Santa Cruz) and CD324 (BD Biosciences, San Jose, CA/USA).

    Techniques: Expressing, Construct, Chloramphenicol Acetyltransferase Assay, Clone Assay, Transformation Assay, Western Blot

    Elevated HtrA secretion levels in H. pylori does not affect the extracellular delivery of VacA and GGT. a H. pylori wild-type strain 26695 ( Hp wt) and 26695 transformed with htrA 26695 were grown for 24 h in BHI broth medium with 1% β-cyclodextrin in the presence or absence of 1 or 2 mM IPTG, respectively. Bacteria-free supernatants were prepared and subjected to Western blotting using α-HtrA, α-VacA and α-GGT antibodies. The blots against α-CagA served as control. The band intensities of secreted HtrA ( b ) as well as VacA and GGT ( c ) were quantified densitometrically. The relative protein expression is given in “fold change”. All secretion assays were done in triplicates

    Journal: Gut Pathogens

    Article Title: Overexpression of serine protease HtrA enhances disruption of adherens junctions, paracellular transmigration and type IV secretion of CagA by Helicobacter pylori

    doi: 10.1186/s13099-017-0189-6

    Figure Lengend Snippet: Elevated HtrA secretion levels in H. pylori does not affect the extracellular delivery of VacA and GGT. a H. pylori wild-type strain 26695 ( Hp wt) and 26695 transformed with htrA 26695 were grown for 24 h in BHI broth medium with 1% β-cyclodextrin in the presence or absence of 1 or 2 mM IPTG, respectively. Bacteria-free supernatants were prepared and subjected to Western blotting using α-HtrA, α-VacA and α-GGT antibodies. The blots against α-CagA served as control. The band intensities of secreted HtrA ( b ) as well as VacA and GGT ( c ) were quantified densitometrically. The relative protein expression is given in “fold change”. All secretion assays were done in triplicates

    Article Snippet: Antibodies The following antibodies were purchased: rabbit polyclonal α-CagA antibody (Austral Biologicals, San Ramon, CA/USA), monoclonal pan-phosphotyrosine α-PY99 (Santa Cruz, Santa Cruz, CA/USA), rabbit α-GAPDH (Santa Cruz), rabbit α-H. pylori (Dako, Glostrup/Denmark) and two monoclonal antibodies directed against the extracellular domain of E-cadherin, H-108 (Santa Cruz) and CD324 (BD Biosciences, San Jose, CA/USA).

    Techniques: Transformation Assay, Western Blot, Expressing

    CagA phosphorylation at EPIYA-motifs during H. pylori infection of AGS cells was investigated using seven different α-phosphotyrosine antibodies. Seven different CagA-expressing East Asian-type H. pylori strains as well as the T4SS-inactive negative control (Shi470 ΔcagL ) were used for infection studies on AGS cells. The infection was monitored over 6 h and the samples shown in Fig. 5 were harvested after photographing. Tyrosine phosphorylation of EPIYA-motifs in CagA of the seven different strains was analyzed with the indicated α-phosphotyrosine antibodies as previously described [ 48 ]. Presence of equal amounts of CagA from each sample was approved using a monoclonal α-CagA antibody. The ~120-170 kDa section of the gels is shown. Arrows indicate the phospho-CagA bands, while red asterisks mark bands of various tyrosine-phosphorylated host cell proteins

    Journal: BMC Microbiology

    Article Title: Systematic analysis of phosphotyrosine antibodies recognizing single phosphorylated EPIYA-motifs in CagA of East Asian-type Helicobacter pylori strains

    doi: 10.1186/s12866-016-0820-6

    Figure Lengend Snippet: CagA phosphorylation at EPIYA-motifs during H. pylori infection of AGS cells was investigated using seven different α-phosphotyrosine antibodies. Seven different CagA-expressing East Asian-type H. pylori strains as well as the T4SS-inactive negative control (Shi470 ΔcagL ) were used for infection studies on AGS cells. The infection was monitored over 6 h and the samples shown in Fig. 5 were harvested after photographing. Tyrosine phosphorylation of EPIYA-motifs in CagA of the seven different strains was analyzed with the indicated α-phosphotyrosine antibodies as previously described [ 48 ]. Presence of equal amounts of CagA from each sample was approved using a monoclonal α-CagA antibody. The ~120-170 kDa section of the gels is shown. Arrows indicate the phospho-CagA bands, while red asterisks mark bands of various tyrosine-phosphorylated host cell proteins

    Article Snippet: After blocking the membranes in TBST buffer with 5 % skim milk or with 3 % bovine serum albumin (BSA) for 1 hour at room temperature, they were incubated with rabbit polyclonal α-CagA antibody (Austral Biologicals, San Ramon, CA/USA) or with the seven commercial α-phosphotyrosine antibodies (Table ).

    Techniques: Infection, Expressing, Negative Control

    H tr A protein expression, oligomer formation and secretion in a large set of strains. A. Casein zymography of the indicated H . pylori strains reveals proteolytically active H tr A protein species of 55 kDa , 165 kDa and 220 kDa as labelled with arrows. Purified recombinant H tr A of 26695 is loaded in lane 9 and produced the same pattern of active HtrA forms. B. H . pylori isolates were grown in liquid BHI medium for 12 h and then fractionated in bacterial cell pellets (top) and supernatants (bottom). Immunoblotting using α‐ H tr A antibodies show that all H . pylori strains exhibit strong H tr A signals in the supernatant fraction but varied substantially in their band intensities. As control, the bacterial pellets and supernatants were probed with α‐ CagA and α‐ UreB antibodies, excluding artificially lysed bacteria.

    Journal: Molecular Microbiology

    Article Title: Characterisation of worldwide Helicobacter pylori strains reveals genetic conservation and essentiality of serine protease HtrA

    doi: 10.1111/mmi.13276

    Figure Lengend Snippet: H tr A protein expression, oligomer formation and secretion in a large set of strains. A. Casein zymography of the indicated H . pylori strains reveals proteolytically active H tr A protein species of 55 kDa , 165 kDa and 220 kDa as labelled with arrows. Purified recombinant H tr A of 26695 is loaded in lane 9 and produced the same pattern of active HtrA forms. B. H . pylori isolates were grown in liquid BHI medium for 12 h and then fractionated in bacterial cell pellets (top) and supernatants (bottom). Immunoblotting using α‐ H tr A antibodies show that all H . pylori strains exhibit strong H tr A signals in the supernatant fraction but varied substantially in their band intensities. As control, the bacterial pellets and supernatants were probed with α‐ CagA and α‐ UreB antibodies, excluding artificially lysed bacteria.

    Article Snippet: CagA proteins were detected by incubation of the membranes with a rabbit polyclonal α‐CagA antibody (Austral Biologicals, USA).

    Techniques: Expressing, Zymography, Purification, Recombinant, Produced