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Austral Biologicals mouse monoclonal anti caga
Mouse Monoclonal Anti Caga, supplied by Austral Biologicals, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/mouse monoclonal anti caga/product/Austral Biologicals
Average 90 stars, based on 1 article reviews
Price from $9.99 to $1999.99
mouse monoclonal anti caga - by Bioz Stars, 2020-09
90/100 stars

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Article Title: Metabolic labelling of cholesteryl glucosides in Helicobacter pylori reveals how the uptake of human lipids enhances bacterial virulence reveals how the uptake of human lipids enhances bacterial virulence †Electronic supplementary information (ESI) available: General reagents and instruments of chemical synthesis, supp
Article Snippet: .. The membranes were blocked with 5% (w/v) skimmed milk in TBS buffer containing 0.01% Tween 20 at room temperature for 1 h and incubated overnight with mouse monoclonal anti-CagA (Austral Biologicals; 1 : 2000), mouse monoclonal anti-phosphotyrosine (4G10, Millipore; 1 : 2000) or mouse monoclonal anti-GAPDH (ab9482, Abcam, UK; 1 : 5000) at 4 °C. .. The blots were washed and incubated with HRP-conjugated secondary antibodies (Santa Cruz Biotechnology, USA) at a 1 : 5000 dilution, and the proteins of interest were visualised using an enhanced chemiluminescence assay (WBKLS0500, Millipore).

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    Austral Biologicals mouse monoclonal α caga antibody
    Role of EPIYA motifs in <t>CagA</t> phosphorylation during H. pylori infection was investigated with seven different α-phosphotyrosine antibodies. AGS cells were infected for 6-expressing H. pylori strains as indicated. The samples in Figure 4 were harvested after photographing. Phosphorylation of CagA was examined using the indicated α–phosphotyrosine antibodies. Loading of equal amounts of CagA from each sample was confirmed by probing with a monoclonal <t>α-CagA</t> antibody. A larger section of the ∼120−180 kDa range is shown and contains the phospho-CagA bands of different sizes (arrows) as well as a set of tyrosine-phosphorylated host cell proteins (red asterisks). The blue asterisk indicates a putative N-terminal fragment of CagA which sometimes appears on SDS-PAGE gels [23] .
    Mouse Monoclonal α Caga Antibody, supplied by Austral Biologicals, used in various techniques. Bioz Stars score: 86/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mouse monoclonal α caga antibody/product/Austral Biologicals
    Average 86 stars, based on 13 article reviews
    Price from $9.99 to $1999.99
    mouse monoclonal α caga antibody - by Bioz Stars, 2020-09
    86/100 stars
      Buy from Supplier

    85
    Austral Biologicals mouse immunoglobulin g1 igg1 anti caga monoclonal antibody
    Role of EPIYA motifs in <t>CagA</t> phosphorylation during H. pylori infection was investigated with seven different α-phosphotyrosine antibodies. AGS cells were infected for 6-expressing H. pylori strains as indicated. The samples in Figure 4 were harvested after photographing. Phosphorylation of CagA was examined using the indicated α–phosphotyrosine antibodies. Loading of equal amounts of CagA from each sample was confirmed by probing with a monoclonal <t>α-CagA</t> antibody. A larger section of the ∼120−180 kDa range is shown and contains the phospho-CagA bands of different sizes (arrows) as well as a set of tyrosine-phosphorylated host cell proteins (red asterisks). The blue asterisk indicates a putative N-terminal fragment of CagA which sometimes appears on SDS-PAGE gels [23] .
    Mouse Immunoglobulin G1 Igg1 Anti Caga Monoclonal Antibody, supplied by Austral Biologicals, 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/mouse immunoglobulin g1 igg1 anti caga monoclonal antibody/product/Austral Biologicals
    Average 85 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    mouse immunoglobulin g1 igg1 anti caga monoclonal antibody - by Bioz Stars, 2020-09
    85/100 stars
      Buy from Supplier

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    Role of EPIYA motifs in CagA phosphorylation during H. pylori infection was investigated with seven different α-phosphotyrosine antibodies. AGS cells were infected for 6-expressing H. pylori strains as indicated. The samples in Figure 4 were harvested after photographing. Phosphorylation of CagA was examined using the indicated α–phosphotyrosine antibodies. Loading of equal amounts of CagA from each sample was confirmed by probing with a monoclonal α-CagA antibody. A larger section of the ∼120−180 kDa range is shown and contains the phospho-CagA bands of different sizes (arrows) as well as a set of tyrosine-phosphorylated host cell proteins (red asterisks). The blue asterisk indicates a putative N-terminal fragment of CagA which sometimes appears on SDS-PAGE gels [23] .

    Journal: PLoS ONE

    Article Title: Systematic Analysis of Phosphotyrosine Antibodies Recognizing Single Phosphorylated EPIYA-Motifs in CagA of Western-Type Helicobacter pylori Strains

    doi: 10.1371/journal.pone.0096488

    Figure Lengend Snippet: Role of EPIYA motifs in CagA phosphorylation during H. pylori infection was investigated with seven different α-phosphotyrosine antibodies. AGS cells were infected for 6-expressing H. pylori strains as indicated. The samples in Figure 4 were harvested after photographing. Phosphorylation of CagA was examined using the indicated α–phosphotyrosine antibodies. Loading of equal amounts of CagA from each sample was confirmed by probing with a monoclonal α-CagA antibody. A larger section of the ∼120−180 kDa range is shown and contains the phospho-CagA bands of different sizes (arrows) as well as a set of tyrosine-phosphorylated host cell proteins (red asterisks). The blue asterisk indicates a putative N-terminal fragment of CagA which sometimes appears on SDS-PAGE gels [23] .

    Article Snippet: Membranes were incubated with the seven α-phosphotyrosine antibodies ( ) or mouse monoclonal α-CagA antibody (Austral Biologicals, San Ramon, CA, USA) according to the instructions of the manufacturer.

    Techniques: Infection, Expressing, SDS Page

    Sequence comparison of the three TPM sites in CagA proteins from different clinical H. pylori strains and specific detection of phosphorylated EPIYT-motif during co-culture. Panel A : CagA proteins of H. pylori vary in their carboxy-terminal TPM sites. These EPIYA-repeats serve as tyrosine phosphorylation sites of CagA and can be targeted by c-Abl and c-Src kinases. Three EPIYA- or EPIYT-segments at position A, B and C are shaded with yellow. One striking feature of B-TPM is the presence of a threonine residue in the +1 position (shaded with blue) relative to the phosphorylated tyrosine residue, which is highly conserved in most but not all H. pylori strains and may affect the capabilities of binding the p85 subunit of PI3-kinase, as discussed in the text. The CagA protein sequences were obtained from databases and sequence alignment was done using the ClustalW2 program ( http://www.ebi.ac.uk/Tools/msa/clustalw2/ ). Panel B : To investigate whether the EPIYT-motif can be phosphorylated during co-culture, AGS cells were co-incubated with the indicated CagA-expressing H. pylori strains for 6 h. Phosphorylation of CagA was examined using the phospho-specific α-pCagA-EPIYT-918 antibody. Loading of equal amounts of protein in each sample was confirmed by probing with monoclonal α-CagA and α-GAPDH antibodies.

    Journal: PLoS Pathogens

    Article Title: A Specific A/T Polymorphism in Western Tyrosine Phosphorylation B-Motifs Regulates Helicobacter pylori CagA Epithelial Cell Interactions

    doi: 10.1371/journal.ppat.1004621

    Figure Lengend Snippet: Sequence comparison of the three TPM sites in CagA proteins from different clinical H. pylori strains and specific detection of phosphorylated EPIYT-motif during co-culture. Panel A : CagA proteins of H. pylori vary in their carboxy-terminal TPM sites. These EPIYA-repeats serve as tyrosine phosphorylation sites of CagA and can be targeted by c-Abl and c-Src kinases. Three EPIYA- or EPIYT-segments at position A, B and C are shaded with yellow. One striking feature of B-TPM is the presence of a threonine residue in the +1 position (shaded with blue) relative to the phosphorylated tyrosine residue, which is highly conserved in most but not all H. pylori strains and may affect the capabilities of binding the p85 subunit of PI3-kinase, as discussed in the text. The CagA protein sequences were obtained from databases and sequence alignment was done using the ClustalW2 program ( http://www.ebi.ac.uk/Tools/msa/clustalw2/ ). Panel B : To investigate whether the EPIYT-motif can be phosphorylated during co-culture, AGS cells were co-incubated with the indicated CagA-expressing H. pylori strains for 6 h. Phosphorylation of CagA was examined using the phospho-specific α-pCagA-EPIYT-918 antibody. Loading of equal amounts of protein in each sample was confirmed by probing with monoclonal α-CagA and α-GAPDH antibodies.

    Article Snippet: Rabbit polyclonal and mouse monoclonal α-CagA antibodies were from Austral Biologicals, or from Emd Millipore Corporation (Billerica MA).

    Techniques: Sequencing, Co-Culture Assay, Binding Assay, Incubation, Expressing

    The EPIYT site at B-TPM of CagA is phosphorylated and necessary for interaction with PI3-kinase. Panel A : Site-directed mutagenesis of CagA TPM-motifs A, B and C was performed to generate the indicated phospho-resistant variants. Tyrosine residues in adjacent TPM-motifs were replaced by phenylalanines. The resulting single and double mutants are indicated and complemented into the H. pylori Δ cagA mutant. Panel B : AGS cells were co-cultured with the various CagA-expressing H. pylori strains for 6 h as indicated. Cell extracts were harvested and subjected to immunoprecipitation (IP) using α-CagA antibodies. CagA phosphorylation in the IPs was examined using α-pY-99 and α-CagA antibodies (arrows). All strains expressed similar amounts of CagA, and H. pylori expressing CagA wild-type (wt), EPIYT-AC Y > F , and EPIYT-B Y > F all showed phosphorylation signal. Western blotting using α-PI3-kinase antibody revealed that only CagA wt and EPIYT-AC Y > F can bind to PI3-kinase, but not the EPIYT-B Y > F mutant, suggesting that EPIYT-B is phosphorylated and necessary for the interaction.

    Journal: PLoS Pathogens

    Article Title: A Specific A/T Polymorphism in Western Tyrosine Phosphorylation B-Motifs Regulates Helicobacter pylori CagA Epithelial Cell Interactions

    doi: 10.1371/journal.ppat.1004621

    Figure Lengend Snippet: The EPIYT site at B-TPM of CagA is phosphorylated and necessary for interaction with PI3-kinase. Panel A : Site-directed mutagenesis of CagA TPM-motifs A, B and C was performed to generate the indicated phospho-resistant variants. Tyrosine residues in adjacent TPM-motifs were replaced by phenylalanines. The resulting single and double mutants are indicated and complemented into the H. pylori Δ cagA mutant. Panel B : AGS cells were co-cultured with the various CagA-expressing H. pylori strains for 6 h as indicated. Cell extracts were harvested and subjected to immunoprecipitation (IP) using α-CagA antibodies. CagA phosphorylation in the IPs was examined using α-pY-99 and α-CagA antibodies (arrows). All strains expressed similar amounts of CagA, and H. pylori expressing CagA wild-type (wt), EPIYT-AC Y > F , and EPIYT-B Y > F all showed phosphorylation signal. Western blotting using α-PI3-kinase antibody revealed that only CagA wt and EPIYT-AC Y > F can bind to PI3-kinase, but not the EPIYT-B Y > F mutant, suggesting that EPIYT-B is phosphorylated and necessary for the interaction.

    Article Snippet: Rabbit polyclonal and mouse monoclonal α-CagA antibodies were from Austral Biologicals, or from Emd Millipore Corporation (Billerica MA).

    Techniques: Mutagenesis, Cell Culture, Expressing, Immunoprecipitation, Western Blot

    PI3-kinase can interact with B-TPM of CagA during co-culture. Panel A : Site-directed mutagenesis of CagA TPM-motifs A, B and C was performed to generate the indicated phospho-resistant variants. Tyrosine residues in adjacent TPM-motifs were replaced by phenylalanines. The resulting single and triple mutants were named as indicated and complemented into the H. pylori Δ cagA mutant. Panel B : AGS cells were co-cultured with the various CagA-expressing H. pylori strains for 6 h as indicated. Cell extracts were harvested and subjected to reverse immunoprecipitation (IP) using α-PI3-kinase antibodies. All samples contained similar amounts of PI3-kinase in the input control. CagA presence and phosphorylation at the EPIYT-site in the IPs was examined using phospho-specific α-pCagA-EPIYT-918 and α-CagA antibodies (arrows). Only the lane with H. pylori expressing CagA wt revealed a signal for CagA and phosphorylation at EPIYT-918 in the IP, indicating that phosphorylated EPIYT-B is necessary for the interaction with PI3-kinase. Panel C : After 24 h co-culture of AGS cells with the isogenic H. pylori strains containing the engineered CagA molecules, whole cell lysates were subjected to immunoprecipitation with an anti-CagA antibody. The anti-CagA immunoprecipitates (IP) were separated on SDS-PAGE, followed by western blot with anti-PI3-kinase (p85), which indicated that the engineered CagA B-EPIYA and CagA B-EPIYT molecules have different affinity to the PI3-kinase protein in AGS cells.

    Journal: PLoS Pathogens

    Article Title: A Specific A/T Polymorphism in Western Tyrosine Phosphorylation B-Motifs Regulates Helicobacter pylori CagA Epithelial Cell Interactions

    doi: 10.1371/journal.ppat.1004621

    Figure Lengend Snippet: PI3-kinase can interact with B-TPM of CagA during co-culture. Panel A : Site-directed mutagenesis of CagA TPM-motifs A, B and C was performed to generate the indicated phospho-resistant variants. Tyrosine residues in adjacent TPM-motifs were replaced by phenylalanines. The resulting single and triple mutants were named as indicated and complemented into the H. pylori Δ cagA mutant. Panel B : AGS cells were co-cultured with the various CagA-expressing H. pylori strains for 6 h as indicated. Cell extracts were harvested and subjected to reverse immunoprecipitation (IP) using α-PI3-kinase antibodies. All samples contained similar amounts of PI3-kinase in the input control. CagA presence and phosphorylation at the EPIYT-site in the IPs was examined using phospho-specific α-pCagA-EPIYT-918 and α-CagA antibodies (arrows). Only the lane with H. pylori expressing CagA wt revealed a signal for CagA and phosphorylation at EPIYT-918 in the IP, indicating that phosphorylated EPIYT-B is necessary for the interaction with PI3-kinase. Panel C : After 24 h co-culture of AGS cells with the isogenic H. pylori strains containing the engineered CagA molecules, whole cell lysates were subjected to immunoprecipitation with an anti-CagA antibody. The anti-CagA immunoprecipitates (IP) were separated on SDS-PAGE, followed by western blot with anti-PI3-kinase (p85), which indicated that the engineered CagA B-EPIYA and CagA B-EPIYT molecules have different affinity to the PI3-kinase protein in AGS cells.

    Article Snippet: Rabbit polyclonal and mouse monoclonal α-CagA antibodies were from Austral Biologicals, or from Emd Millipore Corporation (Billerica MA).

    Techniques: Co-Culture Assay, Mutagenesis, Cell Culture, Expressing, Immunoprecipitation, SDS Page, Western Blot