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  • 94
    ATCC atcc 51932 caga caga
    Atcc 51932 Caga Caga, supplied by ATCC, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Santa Cruz Biotechnology phosphorylated caga
    H. pylori hydrogenase enhances <t>CagA</t> translocation into AGS human gastric cells. Western blot analysis using anti-CagA antibody for different H. pylori strains grown in broth alone (A). Lysates of AGS cells after coculture with different H. pylori strains were used for Western blot analysis using anti-CagA antibody (B) or <t>anti-phosphotyrosine</t> (α-PY99) antibody (C).
    Phosphorylated Caga, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 88/100, based on 62 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Austral Biologicals α caga
    Effects of CagL point mutations in the RHS motif on <t>CagA</t> injection and phosphorylation during H. pylori infection of AGS cells . (A) The P12Δ cagL deletion mutant was complemented with CagL WT or various CagL point mutants. AGS cells were infected with the different indicated H. pylori strains (MOI = 100) during a time course of 2 or 4 h, respectively. The resulting protein lysates were subjected to Western blotting using α-phospho-tyrosine (PY-99) and <t>α-CagA</t> antibodies. The α-GAPDH blot served as loading control in each sample. (B) Quantification of CagA phosphorylation. Densitometric measurement of individual band intensities of the α-CagA and α-phospho-tyrosine (PY-99) blots in (A) was performed with the Lumi-Imager F1 (Roche). Quantification revealed the relative amount of phospho-CagA per sample in %. Similar inhibitory activities of all mutants were seen when MOI = 50 was used (not shown).
    α Caga, supplied by Austral Biologicals, used in various techniques. Bioz Stars score: 85/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Austral Biologicals caga antibodies
    PC activation induced by <t>VacA</t> and <t>CagA</t> on THP-1 cells. Both VacA and CagA significantly ( P
    Caga Antibodies, supplied by Austral Biologicals, used in various techniques. Bioz Stars score: 85/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Santa Cruz Biotechnology immunoblotting caga
    PC activation induced by <t>VacA</t> and <t>CagA</t> on THP-1 cells. Both VacA and CagA significantly ( P
    Immunoblotting Caga, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 90/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Santa Cruz Biotechnology caga antibody
    Variation in the <t>CagA</t> amino acid sequence of East Asian-type and Western-type CagA. The target <t>α-EAS</t> sequences “AINRKIDRINKIASAGKG” in EPIYA segment D, based on the sequences of Japanese strains, are shown in frame. A sequence analysis revealed that the typical target sequences in Bhutanese strains was “(T/K)IN(G/R)KID(Q/R)(L/I)N(R/K)(T/I)ASA(G/N)KG,” where (X/Y) means X and Y as the two major amino acids. The sequences of the EPIYA-D segments in Bhutanese strains were highly variable compared to strains deposited in GenBank. In contrast, the East Asian-type and Western-type sequences of EPIYA-C segments in Bhutanese strains were largely identical, similar to the typical sequences of EPIYA-C segments deposited in GenBank. Reference strains used in Fig. 1A (strain name [accession number]) were 103a (AB110966.1), 105a (AB110967.1), 106a (AB110968.1), 108a (AB110969.1), 113b (AB110970.1), 120a (AB110971.1), 122b (AB110972.1), 125b (AB110973.1), 128a (AB110974.1), FJT77 (KF028580.1), 04-518 (AB267252.1), 03-166 (AB267253.1), 04-264 (AB267254.1), THP1477 (AB116744.1), 04-334 (AB267249.1), 03-292 (AB267250.1), 04-366 (AB267251.1), THP1260 (AB116742.1), M3 (AB116740.1), THP463 (AB116735.1), Korea23 (AB057044.1), Korea 12 (AB057043.1), K69 (FJ458129.1), Korea2-3 (AB057040.1), k266 (FJ458163.1), K265 (FJ458162.1), K264 (FJ458161.1), K261 (FJ458158.1), K260 (FJ458157.1), K259 (FJ458156.1). Reference strains used in Fig. 1C (strain name [accession number]) were India41 (AF222807.1), India99 (AF222809.1), OSC40A (EU089774.1), OSC42B (EU089775.1), PCR-156i (EU368669.1), PCR218vi (EU089766.1). RIGLD-OC149 (JX428784.1), SAN53 (EU089771.1), PD682 (EF450167.1), PD636 (EF450165.1), PD308 (EF450162.1), PD488 (EF450161.1), PD537 (EF450160.1), PD501 (EF450159.1), PD351 (EF450158.1), PD348 (EF450157.1), PD6481K (EF450153.1), 216G (GQ899171.1), 1407 (GU143415.1), HPI-14 (FJ849792.1), HPI-13 (FJ849791.1), HPI-11 (FJ849789.1), USA2791 (AB057099.1), Kazak3 (AB057098.1), USA35 (AB057095.1), Italy329 (AB057094.1), Arizona2 (AB057075.1), Arizona1 (AB057074.1).
    Caga Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 85/100, based on 22 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Austral Biologicals caga
    H. pylori stimulates cancer cell motility through the combined <t>CagA-dependent</t> and -independent signaling. CagA is injected into the cell via the α 5 <t>β</t> 1 integrin and associates with known regulators of cell adhesion and motility. CagA-independent
    Caga, supplied by Austral Biologicals, used in various techniques. Bioz Stars score: 89/100, based on 62 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore caga
    H. pylori stimulates cancer cell motility through the combined <t>CagA-dependent</t> and -independent signaling. CagA is injected into the cell via the α 5 <t>β</t> 1 integrin and associates with known regulators of cell adhesion and motility. CagA-independent
    Caga, supplied by Millipore, used in various techniques. Bioz Stars score: 90/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Austral Biologicals polyclonal antiserum against caga
    H. pylori stimulates cancer cell motility through the combined <t>CagA-dependent</t> and -independent signaling. CagA is injected into the cell via the α 5 <t>β</t> 1 integrin and associates with known regulators of cell adhesion and motility. CagA-independent
    Polyclonal Antiserum Against Caga, supplied by Austral Biologicals, used in various techniques. Bioz Stars score: 85/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Abnova pylori caga antibody
    (A) Comparison of the overall protein profiles in crude cell extracts of wild-type H . pylori 26695 (red) and the Hp Δ glyA deletion strain (blue) as determined by capillary electrophoresis (Experion, Bio-Rad) (left) and by migration on SDS-PAGE (right). The absence of a discrete protein band (*) with a molecular mass around 145 kDa is observed in the ΔglyA strain. (B) Immunoblot of crude extracts of H . pylori strains: 26695 ( glyA + , <t>cagA</t> + ), Hp Δ glyA ( glyA - , cagA + ) and X47 ( glyA + , cagA - ). Immunodetection was performed with antibodies directed against CagA and <t>UreB</t> proteins from H . pylori . (C) PCR amplification of a 307 bp internal fragment of cagA performed with the primer pair SA82/SA83 ( Table 1 ). Amplification is observed in the wild-type 26695 and Hp Δ glyA deletion strains, but not in the X47 control strain.
    Pylori Caga Antibody, supplied by Abnova, used in various techniques. Bioz Stars score: 92/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Austral Biologicals pylori caga antibody
    (A) Comparison of the overall protein profiles in crude cell extracts of wild-type H . pylori 26695 (red) and the Hp Δ glyA deletion strain (blue) as determined by capillary electrophoresis (Experion, Bio-Rad) (left) and by migration on SDS-PAGE (right). The absence of a discrete protein band (*) with a molecular mass around 145 kDa is observed in the ΔglyA strain. (B) Immunoblot of crude extracts of H . pylori strains: 26695 ( glyA + , <t>cagA</t> + ), Hp Δ glyA ( glyA - , cagA + ) and X47 ( glyA + , cagA - ). Immunodetection was performed with antibodies directed against CagA and <t>UreB</t> proteins from H . pylori . (C) PCR amplification of a 307 bp internal fragment of cagA performed with the primer pair SA82/SA83 ( Table 1 ). Amplification is observed in the wild-type 26695 and Hp Δ glyA deletion strains, but not in the X47 control strain.
    Pylori Caga Antibody, supplied by Austral Biologicals, used in various techniques. Bioz Stars score: 88/100, based on 31 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Promega luciferase assay smad responsive caga luciferase reporter caga luc
    (A) Comparison of the overall protein profiles in crude cell extracts of wild-type H . pylori 26695 (red) and the Hp Δ glyA deletion strain (blue) as determined by capillary electrophoresis (Experion, Bio-Rad) (left) and by migration on SDS-PAGE (right). The absence of a discrete protein band (*) with a molecular mass around 145 kDa is observed in the ΔglyA strain. (B) Immunoblot of crude extracts of H . pylori strains: 26695 ( glyA + , <t>cagA</t> + ), Hp Δ glyA ( glyA - , cagA + ) and X47 ( glyA + , cagA - ). Immunodetection was performed with antibodies directed against CagA and <t>UreB</t> proteins from H . pylori . (C) PCR amplification of a 307 bp internal fragment of cagA performed with the primer pair SA82/SA83 ( Table 1 ). Amplification is observed in the wild-type 26695 and Hp Δ glyA deletion strains, but not in the X47 control strain.
    Luciferase Assay Smad Responsive Caga Luciferase Reporter Caga Luc, supplied by Promega, used in various techniques. Bioz Stars score: 93/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Abcam caga specific antibody
    (A) Comparison of the overall protein profiles in crude cell extracts of wild-type H . pylori 26695 (red) and the Hp Δ glyA deletion strain (blue) as determined by capillary electrophoresis (Experion, Bio-Rad) (left) and by migration on SDS-PAGE (right). The absence of a discrete protein band (*) with a molecular mass around 145 kDa is observed in the ΔglyA strain. (B) Immunoblot of crude extracts of H . pylori strains: 26695 ( glyA + , <t>cagA</t> + ), Hp Δ glyA ( glyA - , cagA + ) and X47 ( glyA + , cagA - ). Immunodetection was performed with antibodies directed against CagA and <t>UreB</t> proteins from H . pylori . (C) PCR amplification of a 307 bp internal fragment of cagA performed with the primer pair SA82/SA83 ( Table 1 ). Amplification is observed in the wild-type 26695 and Hp Δ glyA deletion strains, but not in the X47 control strain.
    Caga Specific Antibody, supplied by Abcam, used in various techniques. Bioz Stars score: 88/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Abcam pylori caga
    (A) Comparison of the overall protein profiles in crude cell extracts of wild-type H . pylori 26695 (red) and the Hp Δ glyA deletion strain (blue) as determined by capillary electrophoresis (Experion, Bio-Rad) (left) and by migration on SDS-PAGE (right). The absence of a discrete protein band (*) with a molecular mass around 145 kDa is observed in the ΔglyA strain. (B) Immunoblot of crude extracts of H . pylori strains: 26695 ( glyA + , <t>cagA</t> + ), Hp Δ glyA ( glyA - , cagA + ) and X47 ( glyA + , cagA - ). Immunodetection was performed with antibodies directed against CagA and <t>UreB</t> proteins from H . pylori . (C) PCR amplification of a 307 bp internal fragment of cagA performed with the primer pair SA82/SA83 ( Table 1 ). Amplification is observed in the wild-type 26695 and Hp Δ glyA deletion strains, but not in the X47 control strain.
    Pylori Caga, supplied by Abcam, used in various techniques. Bioz Stars score: 88/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology pylori caga
    (A) Comparison of the overall protein profiles in crude cell extracts of wild-type H . pylori 26695 (red) and the Hp Δ glyA deletion strain (blue) as determined by capillary electrophoresis (Experion, Bio-Rad) (left) and by migration on SDS-PAGE (right). The absence of a discrete protein band (*) with a molecular mass around 145 kDa is observed in the ΔglyA strain. (B) Immunoblot of crude extracts of H . pylori strains: 26695 ( glyA + , <t>cagA</t> + ), Hp Δ glyA ( glyA - , cagA + ) and X47 ( glyA + , cagA - ). Immunodetection was performed with antibodies directed against CagA and <t>UreB</t> proteins from H . pylori . (C) PCR amplification of a 307 bp internal fragment of cagA performed with the primer pair SA82/SA83 ( Table 1 ). Amplification is observed in the wild-type 26695 and Hp Δ glyA deletion strains, but not in the X47 control strain.
    Pylori Caga, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 88/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Fisher Scientific caga δcaga
    Human gastric organoids exhibit acute responses to H. pylori infection a, Day 34 hGOs contained a zone of MKI67 + proliferative cells similar to the embryonic (E18.5) and postnatal (P12) mouse antrum. b, Using hGOs to model human-specific disease processes of H. pylori infection. Pathogenic (G27) and attenuated <t>(ΔCagA)</t> bacteria were microinjected into the lumen of hGOs and after 24 hours, bacteria (both G27 and ΔCagA strains) were tightly associated with the apical surface of the hGO epithelium. c, Immunoprecipitation (IP) for the oncogene c-MET demonstrates that H. pylori induced a robust activation (tyrosine phosphorylation) of c-MET, and this is a <t>CagA-dependent</t> process. Further, CagA immunoprecipiated with c-MET, suggesting these proteins interact in hGO epithelial cells. Lysates that were immunoprecipitated are underlined, phospho-c-met and CagA control lysates were not immunoprecipitated but used to confirm molecular weights. The molecular weight markers are indicated (130 and 170kd) and shown in extended figure 9c . d, Within 24 hours, H. pylori infection caused a CagA-dependent two-fold increase in the number of proliferating cells in the hGO epithelium, measured by EdU incorporation. *, p
    Caga δcaga, supplied by Fisher Scientific, used in various techniques. Bioz Stars score: 86/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Becton Dickinson caga positive
    Human gastric organoids exhibit acute responses to H. pylori infection a, Day 34 hGOs contained a zone of MKI67 + proliferative cells similar to the embryonic (E18.5) and postnatal (P12) mouse antrum. b, Using hGOs to model human-specific disease processes of H. pylori infection. Pathogenic (G27) and attenuated <t>(ΔCagA)</t> bacteria were microinjected into the lumen of hGOs and after 24 hours, bacteria (both G27 and ΔCagA strains) were tightly associated with the apical surface of the hGO epithelium. c, Immunoprecipitation (IP) for the oncogene c-MET demonstrates that H. pylori induced a robust activation (tyrosine phosphorylation) of c-MET, and this is a <t>CagA-dependent</t> process. Further, CagA immunoprecipiated with c-MET, suggesting these proteins interact in hGO epithelial cells. Lysates that were immunoprecipitated are underlined, phospho-c-met and CagA control lysates were not immunoprecipitated but used to confirm molecular weights. The molecular weight markers are indicated (130 and 170kd) and shown in extended figure 9c . d, Within 24 hours, H. pylori infection caused a CagA-dependent two-fold increase in the number of proliferating cells in the hGO epithelium, measured by EdU incorporation. *, p
    Caga Positive, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 91/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Austral Biologicals rabbit anti caga
    Human gastric organoids exhibit acute responses to H. pylori infection a, Day 34 hGOs contained a zone of MKI67 + proliferative cells similar to the embryonic (E18.5) and postnatal (P12) mouse antrum. b, Using hGOs to model human-specific disease processes of H. pylori infection. Pathogenic (G27) and attenuated <t>(ΔCagA)</t> bacteria were microinjected into the lumen of hGOs and after 24 hours, bacteria (both G27 and ΔCagA strains) were tightly associated with the apical surface of the hGO epithelium. c, Immunoprecipitation (IP) for the oncogene c-MET demonstrates that H. pylori induced a robust activation (tyrosine phosphorylation) of c-MET, and this is a <t>CagA-dependent</t> process. Further, CagA immunoprecipiated with c-MET, suggesting these proteins interact in hGO epithelial cells. Lysates that were immunoprecipitated are underlined, phospho-c-met and CagA control lysates were not immunoprecipitated but used to confirm molecular weights. The molecular weight markers are indicated (130 and 170kd) and shown in extended figure 9c . d, Within 24 hours, H. pylori infection caused a CagA-dependent two-fold increase in the number of proliferating cells in the hGO epithelium, measured by EdU incorporation. *, p
    Rabbit Anti Caga, supplied by Austral Biologicals, used in various techniques. Bioz Stars score: 91/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Amazon amerindian caga
    Human gastric organoids exhibit acute responses to H. pylori infection a, Day 34 hGOs contained a zone of MKI67 + proliferative cells similar to the embryonic (E18.5) and postnatal (P12) mouse antrum. b, Using hGOs to model human-specific disease processes of H. pylori infection. Pathogenic (G27) and attenuated <t>(ΔCagA)</t> bacteria were microinjected into the lumen of hGOs and after 24 hours, bacteria (both G27 and ΔCagA strains) were tightly associated with the apical surface of the hGO epithelium. c, Immunoprecipitation (IP) for the oncogene c-MET demonstrates that H. pylori induced a robust activation (tyrosine phosphorylation) of c-MET, and this is a <t>CagA-dependent</t> process. Further, CagA immunoprecipiated with c-MET, suggesting these proteins interact in hGO epithelial cells. Lysates that were immunoprecipitated are underlined, phospho-c-met and CagA control lysates were not immunoprecipitated but used to confirm molecular weights. The molecular weight markers are indicated (130 and 170kd) and shown in extended figure 9c . d, Within 24 hours, H. pylori infection caused a CagA-dependent two-fold increase in the number of proliferating cells in the hGO epithelium, measured by EdU incorporation. *, p
    Amerindian Caga, supplied by Amazon, used in various techniques. Bioz Stars score: 86/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Amazon caga variant
    Human gastric organoids exhibit acute responses to H. pylori infection a, Day 34 hGOs contained a zone of MKI67 + proliferative cells similar to the embryonic (E18.5) and postnatal (P12) mouse antrum. b, Using hGOs to model human-specific disease processes of H. pylori infection. Pathogenic (G27) and attenuated <t>(ΔCagA)</t> bacteria were microinjected into the lumen of hGOs and after 24 hours, bacteria (both G27 and ΔCagA strains) were tightly associated with the apical surface of the hGO epithelium. c, Immunoprecipitation (IP) for the oncogene c-MET demonstrates that H. pylori induced a robust activation (tyrosine phosphorylation) of c-MET, and this is a <t>CagA-dependent</t> process. Further, CagA immunoprecipiated with c-MET, suggesting these proteins interact in hGO epithelial cells. Lysates that were immunoprecipitated are underlined, phospho-c-met and CagA control lysates were not immunoprecipitated but used to confirm molecular weights. The molecular weight markers are indicated (130 and 170kd) and shown in extended figure 9c . d, Within 24 hours, H. pylori infection caused a CagA-dependent two-fold increase in the number of proliferating cells in the hGO epithelium, measured by EdU incorporation. *, p
    Caga Variant, supplied by Amazon, used in various techniques. Bioz Stars score: 86/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Amazon pylori caga
    Human gastric organoids exhibit acute responses to H. pylori infection a, Day 34 hGOs contained a zone of MKI67 + proliferative cells similar to the embryonic (E18.5) and postnatal (P12) mouse antrum. b, Using hGOs to model human-specific disease processes of H. pylori infection. Pathogenic (G27) and attenuated <t>(ΔCagA)</t> bacteria were microinjected into the lumen of hGOs and after 24 hours, bacteria (both G27 and ΔCagA strains) were tightly associated with the apical surface of the hGO epithelium. c, Immunoprecipitation (IP) for the oncogene c-MET demonstrates that H. pylori induced a robust activation (tyrosine phosphorylation) of c-MET, and this is a <t>CagA-dependent</t> process. Further, CagA immunoprecipiated with c-MET, suggesting these proteins interact in hGO epithelial cells. Lysates that were immunoprecipitated are underlined, phospho-c-met and CagA control lysates were not immunoprecipitated but used to confirm molecular weights. The molecular weight markers are indicated (130 and 170kd) and shown in extended figure 9c . d, Within 24 hours, H. pylori infection caused a CagA-dependent two-fold increase in the number of proliferating cells in the hGO epithelium, measured by EdU incorporation. *, p
    Pylori Caga, supplied by Amazon, used in various techniques. Bioz Stars score: 91/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Austral Biologicals anti caga serum
    Human gastric organoids exhibit acute responses to H. pylori infection a, Day 34 hGOs contained a zone of MKI67 + proliferative cells similar to the embryonic (E18.5) and postnatal (P12) mouse antrum. b, Using hGOs to model human-specific disease processes of H. pylori infection. Pathogenic (G27) and attenuated <t>(ΔCagA)</t> bacteria were microinjected into the lumen of hGOs and after 24 hours, bacteria (both G27 and ΔCagA strains) were tightly associated with the apical surface of the hGO epithelium. c, Immunoprecipitation (IP) for the oncogene c-MET demonstrates that H. pylori induced a robust activation (tyrosine phosphorylation) of c-MET, and this is a <t>CagA-dependent</t> process. Further, CagA immunoprecipiated with c-MET, suggesting these proteins interact in hGO epithelial cells. Lysates that were immunoprecipitated are underlined, phospho-c-met and CagA control lysates were not immunoprecipitated but used to confirm molecular weights. The molecular weight markers are indicated (130 and 170kd) and shown in extended figure 9c . d, Within 24 hours, H. pylori infection caused a CagA-dependent two-fold increase in the number of proliferating cells in the hGO epithelium, measured by EdU incorporation. *, p
    Anti Caga Serum, supplied by Austral Biologicals, used in various techniques. Bioz Stars score: 85/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    H. pylori hydrogenase enhances CagA translocation into AGS human gastric cells. Western blot analysis using anti-CagA antibody for different H. pylori strains grown in broth alone (A). Lysates of AGS cells after coculture with different H. pylori strains were used for Western blot analysis using anti-CagA antibody (B) or anti-phosphotyrosine (α-PY99) antibody (C).

    Journal: mBio

    Article Title: Hydrogen Metabolism in Helicobacter pylori Plays a Role in Gastric Carcinogenesis through Facilitating CagA Translocation

    doi: 10.1128/mBio.01022-16

    Figure Lengend Snippet: H. pylori hydrogenase enhances CagA translocation into AGS human gastric cells. Western blot analysis using anti-CagA antibody for different H. pylori strains grown in broth alone (A). Lysates of AGS cells after coculture with different H. pylori strains were used for Western blot analysis using anti-CagA antibody (B) or anti-phosphotyrosine (α-PY99) antibody (C).

    Article Snippet: Alternatively, levels of phosphorylated CagA were determined by using an anti-phosphotyrosine antibody (α-PY99 [Santa Cruz]), and actin levels as controls were determined using an antiactin (C-11) antibody (Santa Cruz).

    Techniques: Translocation Assay, Western Blot

    Effects of CagL point mutations in the RHS motif on CagA injection and phosphorylation during H. pylori infection of AGS cells . (A) The P12Δ cagL deletion mutant was complemented with CagL WT or various CagL point mutants. AGS cells were infected with the different indicated H. pylori strains (MOI = 100) during a time course of 2 or 4 h, respectively. The resulting protein lysates were subjected to Western blotting using α-phospho-tyrosine (PY-99) and α-CagA antibodies. The α-GAPDH blot served as loading control in each sample. (B) Quantification of CagA phosphorylation. Densitometric measurement of individual band intensities of the α-CagA and α-phospho-tyrosine (PY-99) blots in (A) was performed with the Lumi-Imager F1 (Roche). Quantification revealed the relative amount of phospho-CagA per sample in %. Similar inhibitory activities of all mutants were seen when MOI = 50 was used (not shown).

    Journal: Frontiers in Cellular and Infection Microbiology

    Article Title: An RGD Helper Sequence in CagL of Helicobacter pylori Assists in Interactions with Integrins and Injection of CagA

    doi: 10.3389/fcimb.2012.00070

    Figure Lengend Snippet: Effects of CagL point mutations in the RHS motif on CagA injection and phosphorylation during H. pylori infection of AGS cells . (A) The P12Δ cagL deletion mutant was complemented with CagL WT or various CagL point mutants. AGS cells were infected with the different indicated H. pylori strains (MOI = 100) during a time course of 2 or 4 h, respectively. The resulting protein lysates were subjected to Western blotting using α-phospho-tyrosine (PY-99) and α-CagA antibodies. The α-GAPDH blot served as loading control in each sample. (B) Quantification of CagA phosphorylation. Densitometric measurement of individual band intensities of the α-CagA and α-phospho-tyrosine (PY-99) blots in (A) was performed with the Lumi-Imager F1 (Roche). Quantification revealed the relative amount of phospho-CagA per sample in %. Similar inhibitory activities of all mutants were seen when MOI = 50 was used (not shown).

    Article Snippet: The pan-α-phospho-tyrosine antibody PY-99 (Santa Cruz) and α-CagA (Austral Biologicals, San Ramon, CA, USA) were used to investigate the phosphorylation of CagA.

    Techniques: Injection, Infection, Mutagenesis, Western Blot

    Effect of CagL deletion or point mutations in the CagL RHS motif on binding of H. pylori to AGS cells . (A) A Δ cagL deletion mutant in strain P12 was generated by replacing the cagL gene with an aphA3 cassette. CagL WT and two CagL mutants carrying either the A84E/E87A or A88E/L91A point mutations were expressed as HA-tag fusion proteins from genes integrated into the ureA locus of the P12Δ cagL strain. The correct expression of each of these CagL variants was verified by Western blotting using an α-HA antibody. The α-CagA Western blot was performed as loading control. (B) AGS cells were infected with each of these strains for 4 h using MOI = 100, followed by determination of the amount of viable bound H. pylori per input strain. The quantification data indicate that each of these strains bound to AGS cells equally well with high efficiency. No significant differences in results were seen when MOI = 50 was used (data not shown).

    Journal: Frontiers in Cellular and Infection Microbiology

    Article Title: An RGD Helper Sequence in CagL of Helicobacter pylori Assists in Interactions with Integrins and Injection of CagA

    doi: 10.3389/fcimb.2012.00070

    Figure Lengend Snippet: Effect of CagL deletion or point mutations in the CagL RHS motif on binding of H. pylori to AGS cells . (A) A Δ cagL deletion mutant in strain P12 was generated by replacing the cagL gene with an aphA3 cassette. CagL WT and two CagL mutants carrying either the A84E/E87A or A88E/L91A point mutations were expressed as HA-tag fusion proteins from genes integrated into the ureA locus of the P12Δ cagL strain. The correct expression of each of these CagL variants was verified by Western blotting using an α-HA antibody. The α-CagA Western blot was performed as loading control. (B) AGS cells were infected with each of these strains for 4 h using MOI = 100, followed by determination of the amount of viable bound H. pylori per input strain. The quantification data indicate that each of these strains bound to AGS cells equally well with high efficiency. No significant differences in results were seen when MOI = 50 was used (data not shown).

    Article Snippet: The pan-α-phospho-tyrosine antibody PY-99 (Santa Cruz) and α-CagA (Austral Biologicals, San Ramon, CA, USA) were used to investigate the phosphorylation of CagA.

    Techniques: Binding Assay, Mutagenesis, Generated, Expressing, Western Blot, Infection

    PC activation induced by VacA and CagA on THP-1 cells. Both VacA and CagA significantly ( P

    Journal: Infection and Immunity

    Article Title: Role of Activated Protein C in Helicobacter pylori-Associated Gastritis

    doi:

    Figure Lengend Snippet: PC activation induced by VacA and CagA on THP-1 cells. Both VacA and CagA significantly ( P

    Article Snippet: Recombinant VacA toxin, recombinant CagA from H. pylori , and polyclonal anti-VacA and anti-CagA antibodies were purchased from Austral Biologicals (San Ramon, Calif.).

    Techniques: Activation Assay

    Variation in the CagA amino acid sequence of East Asian-type and Western-type CagA. The target α-EAS sequences “AINRKIDRINKIASAGKG” in EPIYA segment D, based on the sequences of Japanese strains, are shown in frame. A sequence analysis revealed that the typical target sequences in Bhutanese strains was “(T/K)IN(G/R)KID(Q/R)(L/I)N(R/K)(T/I)ASA(G/N)KG,” where (X/Y) means X and Y as the two major amino acids. The sequences of the EPIYA-D segments in Bhutanese strains were highly variable compared to strains deposited in GenBank. In contrast, the East Asian-type and Western-type sequences of EPIYA-C segments in Bhutanese strains were largely identical, similar to the typical sequences of EPIYA-C segments deposited in GenBank. Reference strains used in Fig. 1A (strain name [accession number]) were 103a (AB110966.1), 105a (AB110967.1), 106a (AB110968.1), 108a (AB110969.1), 113b (AB110970.1), 120a (AB110971.1), 122b (AB110972.1), 125b (AB110973.1), 128a (AB110974.1), FJT77 (KF028580.1), 04-518 (AB267252.1), 03-166 (AB267253.1), 04-264 (AB267254.1), THP1477 (AB116744.1), 04-334 (AB267249.1), 03-292 (AB267250.1), 04-366 (AB267251.1), THP1260 (AB116742.1), M3 (AB116740.1), THP463 (AB116735.1), Korea23 (AB057044.1), Korea 12 (AB057043.1), K69 (FJ458129.1), Korea2-3 (AB057040.1), k266 (FJ458163.1), K265 (FJ458162.1), K264 (FJ458161.1), K261 (FJ458158.1), K260 (FJ458157.1), K259 (FJ458156.1). Reference strains used in Fig. 1C (strain name [accession number]) were India41 (AF222807.1), India99 (AF222809.1), OSC40A (EU089774.1), OSC42B (EU089775.1), PCR-156i (EU368669.1), PCR218vi (EU089766.1). RIGLD-OC149 (JX428784.1), SAN53 (EU089771.1), PD682 (EF450167.1), PD636 (EF450165.1), PD308 (EF450162.1), PD488 (EF450161.1), PD537 (EF450160.1), PD501 (EF450159.1), PD351 (EF450158.1), PD348 (EF450157.1), PD6481K (EF450153.1), 216G (GQ899171.1), 1407 (GU143415.1), HPI-14 (FJ849792.1), HPI-13 (FJ849791.1), HPI-11 (FJ849789.1), USA2791 (AB057099.1), Kazak3 (AB057098.1), USA35 (AB057095.1), Italy329 (AB057094.1), Arizona2 (AB057075.1), Arizona1 (AB057074.1).

    Journal: Scientific Reports

    Article Title: Rare Helicobacter pylori Virulence Genotypes in Bhutan

    doi: 10.1038/srep22584

    Figure Lengend Snippet: Variation in the CagA amino acid sequence of East Asian-type and Western-type CagA. The target α-EAS sequences “AINRKIDRINKIASAGKG” in EPIYA segment D, based on the sequences of Japanese strains, are shown in frame. A sequence analysis revealed that the typical target sequences in Bhutanese strains was “(T/K)IN(G/R)KID(Q/R)(L/I)N(R/K)(T/I)ASA(G/N)KG,” where (X/Y) means X and Y as the two major amino acids. The sequences of the EPIYA-D segments in Bhutanese strains were highly variable compared to strains deposited in GenBank. In contrast, the East Asian-type and Western-type sequences of EPIYA-C segments in Bhutanese strains were largely identical, similar to the typical sequences of EPIYA-C segments deposited in GenBank. Reference strains used in Fig. 1A (strain name [accession number]) were 103a (AB110966.1), 105a (AB110967.1), 106a (AB110968.1), 108a (AB110969.1), 113b (AB110970.1), 120a (AB110971.1), 122b (AB110972.1), 125b (AB110973.1), 128a (AB110974.1), FJT77 (KF028580.1), 04-518 (AB267252.1), 03-166 (AB267253.1), 04-264 (AB267254.1), THP1477 (AB116744.1), 04-334 (AB267249.1), 03-292 (AB267250.1), 04-366 (AB267251.1), THP1260 (AB116742.1), M3 (AB116740.1), THP463 (AB116735.1), Korea23 (AB057044.1), Korea 12 (AB057043.1), K69 (FJ458129.1), Korea2-3 (AB057040.1), k266 (FJ458163.1), K265 (FJ458162.1), K264 (FJ458161.1), K261 (FJ458158.1), K260 (FJ458157.1), K259 (FJ458156.1). Reference strains used in Fig. 1C (strain name [accession number]) were India41 (AF222807.1), India99 (AF222809.1), OSC40A (EU089774.1), OSC42B (EU089775.1), PCR-156i (EU368669.1), PCR218vi (EU089766.1). RIGLD-OC149 (JX428784.1), SAN53 (EU089771.1), PD682 (EF450167.1), PD636 (EF450165.1), PD308 (EF450162.1), PD488 (EF450161.1), PD537 (EF450160.1), PD501 (EF450159.1), PD351 (EF450158.1), PD348 (EF450157.1), PD6481K (EF450153.1), 216G (GQ899171.1), 1407 (GU143415.1), HPI-14 (FJ849792.1), HPI-13 (FJ849791.1), HPI-11 (FJ849789.1), USA2791 (AB057099.1), Kazak3 (AB057098.1), USA35 (AB057095.1), Italy329 (AB057094.1), Arizona2 (AB057075.1), Arizona1 (AB057074.1).

    Article Snippet: Briefly, after antigen retrieval and inactivation of endogenous peroxidase activity, tissue sections were incubated with α-H. pylori antibody (DAKO, Glostrup, Denmark), anti-CagA antibody (b-300; Santa Cruz Biotechnology, Santa Cruz, CA, USA) or α-EAS Ab diluted 1:2,000 with diluting solution (DAKO) overnight at 4 °C.

    Techniques: Sequencing, Western Blot, Polymerase Chain Reaction

    H. pylori stimulates cancer cell motility through the combined CagA-dependent and -independent signaling. CagA is injected into the cell via the α 5 β 1 integrin and associates with known regulators of cell adhesion and motility. CagA-independent

    Journal:

    Article Title: The ?1 Integrin Activates JNK Independent of CagA, and JNK Activation Is Required for Helicobacter pylori CagA+-induced Motility of Gastric Cancer Cells *-induced Motility of Gastric Cancer Cells * S⃞

    doi: 10.1074/jbc.M800289200

    Figure Lengend Snippet: H. pylori stimulates cancer cell motility through the combined CagA-dependent and -independent signaling. CagA is injected into the cell via the α 5 β 1 integrin and associates with known regulators of cell adhesion and motility. CagA-independent

    Article Snippet: Membranes were blocked with 5% milk or 0.1% gelatin in TBST (20 m m Tris, 137 m m NaCl, 0.1% Tween 20, pH 7.5) and incubated overnight with antibodies specific for tubulin (Neo-Markers, Fremont, CA), CagA (Austral Biologicals, San Ramon, CA), β-actin (Sigma), Rac1 (BD Biosciences), phospho-JNK, phospho-AKT, JNK, Cdc42, phospho-MKK4, MKK4, phospho-MKK7, MKK7, phospho-paxillinTyr-118 , and paxillin (Cell Signaling Technology, Beverly, MA) and phospho-paxillinSer-178 (EMD Biosciences, San Diego) in 5% bovine serum albumin or 0.1% gelatin in TBST.

    Techniques: Injection

    (A) Comparison of the overall protein profiles in crude cell extracts of wild-type H . pylori 26695 (red) and the Hp Δ glyA deletion strain (blue) as determined by capillary electrophoresis (Experion, Bio-Rad) (left) and by migration on SDS-PAGE (right). The absence of a discrete protein band (*) with a molecular mass around 145 kDa is observed in the ΔglyA strain. (B) Immunoblot of crude extracts of H . pylori strains: 26695 ( glyA + , cagA + ), Hp Δ glyA ( glyA - , cagA + ) and X47 ( glyA + , cagA - ). Immunodetection was performed with antibodies directed against CagA and UreB proteins from H . pylori . (C) PCR amplification of a 307 bp internal fragment of cagA performed with the primer pair SA82/SA83 ( Table 1 ). Amplification is observed in the wild-type 26695 and Hp Δ glyA deletion strains, but not in the X47 control strain.

    Journal: PLoS ONE

    Article Title: Structural and functional insight into serine hydroxymethyltransferase from Helicobacter pylori

    doi: 10.1371/journal.pone.0208850

    Figure Lengend Snippet: (A) Comparison of the overall protein profiles in crude cell extracts of wild-type H . pylori 26695 (red) and the Hp Δ glyA deletion strain (blue) as determined by capillary electrophoresis (Experion, Bio-Rad) (left) and by migration on SDS-PAGE (right). The absence of a discrete protein band (*) with a molecular mass around 145 kDa is observed in the ΔglyA strain. (B) Immunoblot of crude extracts of H . pylori strains: 26695 ( glyA + , cagA + ), Hp Δ glyA ( glyA - , cagA + ) and X47 ( glyA + , cagA - ). Immunodetection was performed with antibodies directed against CagA and UreB proteins from H . pylori . (C) PCR amplification of a 307 bp internal fragment of cagA performed with the primer pair SA82/SA83 ( Table 1 ). Amplification is observed in the wild-type 26695 and Hp Δ glyA deletion strains, but not in the X47 control strain.

    Article Snippet: Mouse monoclonal anti-polyhistidine antibody (Sigma-Aldrich), rabbit polyclonal anti-UreB antibody (Abcam), and mouse monoclonal anti-H . pylori CagA antibody (Abnova) were used as primary antibodies.

    Techniques: Electrophoresis, Migration, SDS Page, Immunodetection, Polymerase Chain Reaction, Amplification

    Human gastric organoids exhibit acute responses to H. pylori infection a, Day 34 hGOs contained a zone of MKI67 + proliferative cells similar to the embryonic (E18.5) and postnatal (P12) mouse antrum. b, Using hGOs to model human-specific disease processes of H. pylori infection. Pathogenic (G27) and attenuated (ΔCagA) bacteria were microinjected into the lumen of hGOs and after 24 hours, bacteria (both G27 and ΔCagA strains) were tightly associated with the apical surface of the hGO epithelium. c, Immunoprecipitation (IP) for the oncogene c-MET demonstrates that H. pylori induced a robust activation (tyrosine phosphorylation) of c-MET, and this is a CagA-dependent process. Further, CagA immunoprecipiated with c-MET, suggesting these proteins interact in hGO epithelial cells. Lysates that were immunoprecipitated are underlined, phospho-c-met and CagA control lysates were not immunoprecipitated but used to confirm molecular weights. The molecular weight markers are indicated (130 and 170kd) and shown in extended figure 9c . d, Within 24 hours, H. pylori infection caused a CagA-dependent two-fold increase in the number of proliferating cells in the hGO epithelium, measured by EdU incorporation. *, p

    Journal: Nature

    Article Title: Modeling human development and disease in pluripotent stem cell-derived gastric organoids

    doi: 10.1038/nature13863

    Figure Lengend Snippet: Human gastric organoids exhibit acute responses to H. pylori infection a, Day 34 hGOs contained a zone of MKI67 + proliferative cells similar to the embryonic (E18.5) and postnatal (P12) mouse antrum. b, Using hGOs to model human-specific disease processes of H. pylori infection. Pathogenic (G27) and attenuated (ΔCagA) bacteria were microinjected into the lumen of hGOs and after 24 hours, bacteria (both G27 and ΔCagA strains) were tightly associated with the apical surface of the hGO epithelium. c, Immunoprecipitation (IP) for the oncogene c-MET demonstrates that H. pylori induced a robust activation (tyrosine phosphorylation) of c-MET, and this is a CagA-dependent process. Further, CagA immunoprecipiated with c-MET, suggesting these proteins interact in hGO epithelial cells. Lysates that were immunoprecipitated are underlined, phospho-c-met and CagA control lysates were not immunoprecipitated but used to confirm molecular weights. The molecular weight markers are indicated (130 and 170kd) and shown in extended figure 9c . d, Within 24 hours, H. pylori infection caused a CagA-dependent two-fold increase in the number of proliferating cells in the hGO epithelium, measured by EdU incorporation. *, p

    Article Snippet: H. pylori infection H. pylori strain G27 and a mutant G27 strain lacking CagA (ΔCagA) were grown on blood agar plates consisting of Columbia Agar Base (Fisher Scientific), 5% horse blood (Colorado Serum Company), 5 μg ml−1 , vancomycin and 10 μg ml−1 trimethoprim as described previously .

    Techniques: Infection, Immunoprecipitation, Activation Assay, Molecular Weight