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Santa Cruz Biotechnology rabbit igg anti caga polyclonal antibody b 300
Expression, delivery, and phosphorylation of <t>CagA.</t> (A) Western blot analysis of bacterial lysates from the six indicated Korean strains was conducted using a monoclonal anti-CagA antibody (top) or the <t>polyclonal</t> anti-CagA antibody b-300 (bottom). (B)
Rabbit Igg Anti Caga Polyclonal Antibody B 300, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 85/100, based on 666 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1) Product Images from "Polymorphism in the CagA EPIYA Motif Impacts Development of Gastric Cancer ▿Polymorphism in the CagA EPIYA Motif Impacts Development of Gastric Cancer ▿ §"

Article Title: Polymorphism in the CagA EPIYA Motif Impacts Development of Gastric Cancer ▿Polymorphism in the CagA EPIYA Motif Impacts Development of Gastric Cancer ▿ §

Journal: Journal of Clinical Microbiology

doi: 10.1128/JCM.02330-08

Expression, delivery, and phosphorylation of CagA. (A) Western blot analysis of bacterial lysates from the six indicated Korean strains was conducted using a monoclonal anti-CagA antibody (top) or the polyclonal anti-CagA antibody b-300 (bottom). (B)
Figure Legend Snippet: Expression, delivery, and phosphorylation of CagA. (A) Western blot analysis of bacterial lysates from the six indicated Korean strains was conducted using a monoclonal anti-CagA antibody (top) or the polyclonal anti-CagA antibody b-300 (bottom). (B)

Techniques Used: Expressing, Western Blot

2) Product Images from "Functional Analysis of the cag Pathogenicity Island in Helicobacter pylori Isolates from Patients with Gastritis, Peptic Ulcer, and Gastric Cancer "

Article Title: Functional Analysis of the cag Pathogenicity Island in Helicobacter pylori Isolates from Patients with Gastritis, Peptic Ulcer, and Gastric Cancer

Journal: Infection and Immunity

doi: 10.1128/IAI.72.2.1043-1056.2004

Phosphorylation of the CagA protein and induction of IL-8 during infection of AGS cells with 15 representative H. pylori isolates. (A) CagA tyrosine phosphorylation was analyzed in Western blots with a phosphotyrosine-specific antibody, PY-99 (arrows). The asterisk indicates the position of an unknown 125-kDa host cell protein that is phosphorylated in the PBS control. This protein changed its phosphorylation status during infection. (B) Stripping and reprobing of the blot with an anti-CagA antibody (Ab-1) indicated the positions of the different CagA protein species on the gel (arrows). UH4, Ka223, Ka125, and Ka148/2 are cag PAI − strains and did not express CagA. CagA of strain Ca130 was expressed but not phosphorylated. Infection was for 4 h at an MOI of 100. (C) In a parallel experiment, AGS cells were infected under the same conditions for 24 h and IL-8 release into the culture supernatant was measured by ELISA. The results shown are representative of three independent experiments. The error bars indicate standard deviations.
Figure Legend Snippet: Phosphorylation of the CagA protein and induction of IL-8 during infection of AGS cells with 15 representative H. pylori isolates. (A) CagA tyrosine phosphorylation was analyzed in Western blots with a phosphotyrosine-specific antibody, PY-99 (arrows). The asterisk indicates the position of an unknown 125-kDa host cell protein that is phosphorylated in the PBS control. This protein changed its phosphorylation status during infection. (B) Stripping and reprobing of the blot with an anti-CagA antibody (Ab-1) indicated the positions of the different CagA protein species on the gel (arrows). UH4, Ka223, Ka125, and Ka148/2 are cag PAI − strains and did not express CagA. CagA of strain Ca130 was expressed but not phosphorylated. Infection was for 4 h at an MOI of 100. (C) In a parallel experiment, AGS cells were infected under the same conditions for 24 h and IL-8 release into the culture supernatant was measured by ELISA. The results shown are representative of three independent experiments. The error bars indicate standard deviations.

Techniques Used: Infection, Western Blot, Stripping Membranes, Enzyme-linked Immunosorbent Assay

Detection of unique and multiple CagA protein species. (A) Anti-phosphotyrosine patterns of AGS infected with different H. pylori ) were also observed but ran out of the gels shown. Full-length CagA is indicated by the arrowhead. The red dots indicate phosphorylated proteins corresponding in size to CagA protein species, the green dots indicate phosphorylated proteins not corresponding in size to CagA protein species, and the blue dots label CagA protein species with no detectable phosphorylated form during infection. H. pylori strain P1 served as a control because the fragmentation of 135-kDa wild-type CagA into an amino-terminal p100 CagA fragment and a carboxy-terminal p35 CagA ). +, present; −, absent. (B) H. pylori strains P284 and OM1011 are unique and showed a double band of full-length CagA. This double band had nearly identical intensities in the anti-CagA blot (black arrows) but showed a different phosphorylation pattern during infection (red arrows).
Figure Legend Snippet: Detection of unique and multiple CagA protein species. (A) Anti-phosphotyrosine patterns of AGS infected with different H. pylori ) were also observed but ran out of the gels shown. Full-length CagA is indicated by the arrowhead. The red dots indicate phosphorylated proteins corresponding in size to CagA protein species, the green dots indicate phosphorylated proteins not corresponding in size to CagA protein species, and the blue dots label CagA protein species with no detectable phosphorylated form during infection. H. pylori strain P1 served as a control because the fragmentation of 135-kDa wild-type CagA into an amino-terminal p100 CagA fragment and a carboxy-terminal p35 CagA ). +, present; −, absent. (B) H. pylori strains P284 and OM1011 are unique and showed a double band of full-length CagA. This double band had nearly identical intensities in the anti-CagA blot (black arrows) but showed a different phosphorylation pattern during infection (red arrows).

Techniques Used: Infection

Induction of c-Src inactivation and cortactin dephosphorylation. (A) CagA P-Tyr -specific inactivation of c-Src. Western blotting with a phosphospecific anti-c-Sr c antibody revealed that some, but not all, H. pylori strains induce c-Src inactivation by dephosphorylation of residue Y-418 (top) in the catalytic kinase domain. Densitometric measurements of band intensities revealed the Src activity in comparison to uninfected AGS cells in the PBS control (middle). Stripping and reprobing of the blot with a monoclonal anti-Src antibody revealed that equal amounts of Src are present in all lanes (bottom). (B) Cortactin is a major phosphorylated protein in uninfected AGS cells and is specifically dephosphorylated during infection with some H. pylori ). The phosphotyrosine pattern of cell lysates at 80 kDa shows dephosphorylation of cortactin in infections with those H. pylori isolates that induce CagA phosphorylation and Src inactivation (middle). Stripping and reprobing of the blot with a monoclonal anti-cortactin antibody revealed that similar amounts of cortactin were present in all lanes (bottom).
Figure Legend Snippet: Induction of c-Src inactivation and cortactin dephosphorylation. (A) CagA P-Tyr -specific inactivation of c-Src. Western blotting with a phosphospecific anti-c-Sr c antibody revealed that some, but not all, H. pylori strains induce c-Src inactivation by dephosphorylation of residue Y-418 (top) in the catalytic kinase domain. Densitometric measurements of band intensities revealed the Src activity in comparison to uninfected AGS cells in the PBS control (middle). Stripping and reprobing of the blot with a monoclonal anti-Src antibody revealed that equal amounts of Src are present in all lanes (bottom). (B) Cortactin is a major phosphorylated protein in uninfected AGS cells and is specifically dephosphorylated during infection with some H. pylori ). The phosphotyrosine pattern of cell lysates at 80 kDa shows dephosphorylation of cortactin in infections with those H. pylori isolates that induce CagA phosphorylation and Src inactivation (middle). Stripping and reprobing of the blot with a monoclonal anti-cortactin antibody revealed that similar amounts of cortactin were present in all lanes (bottom).

Techniques Used: De-Phosphorylation Assay, Western Blot, Activity Assay, Stripping Membranes, Infection

3) Product Images from "Inhibitory Effects of Anthocyanins on Secretion of Helicobacter pylori CagA and VacA Toxins"

Article Title: Inhibitory Effects of Anthocyanins on Secretion of Helicobacter pylori CagA and VacA Toxins

Journal: International Journal of Medical Sciences

doi: 10.7150/ijms.5094

Effect of anthocyanins on secretion of H. pylori CagA and VacA. H. pylori was cultured with 100 μM of anthocyanin in Mueller-Hinton broth/10% FBS for 3 days and proteins assessed by Western blot. (A), secreted CagA and VacA in culture media. (B), secreted H. pylori proteins reacting with rabbit anti- H. pylori polyclonal antibody. (C) , intracellular CagA and VacA. (D) , intracellular H. pylori proteins reacting with rabbit anti- H. pylori polyclonal antibody. Representative image from five independent experiments.
Figure Legend Snippet: Effect of anthocyanins on secretion of H. pylori CagA and VacA. H. pylori was cultured with 100 μM of anthocyanin in Mueller-Hinton broth/10% FBS for 3 days and proteins assessed by Western blot. (A), secreted CagA and VacA in culture media. (B), secreted H. pylori proteins reacting with rabbit anti- H. pylori polyclonal antibody. (C) , intracellular CagA and VacA. (D) , intracellular H. pylori proteins reacting with rabbit anti- H. pylori polyclonal antibody. Representative image from five independent experiments.

Techniques Used: Cell Culture, Western Blot

4) Product Images from "Helicobacter pylori Counteracts the Apoptotic Action of Its VacA Toxin by Injecting the CagA Protein into Gastric Epithelial Cells"

Article Title: Helicobacter pylori Counteracts the Apoptotic Action of Its VacA Toxin by Injecting the CagA Protein into Gastric Epithelial Cells

Journal: PLoS Pathogens

doi: 10.1371/journal.ppat.1000603

Transfection of gastric epithelial cells with GFP-Bcl2 inhibits VacA-induced apoptosis while not blocking pinocytosis or intracellular trafficking of the toxin. (A) Apoptosis (shown as fold increase over the respective non-transfected control cells) induced by either VacA or etoposide in AGS or MKN 28 cells transfected with GFP-Bcl2, GFP-Bcl-xL, GFP-Mcl1, or the GFP vector. Cells were treated with VacA or etoposide as in Figure 3A . Non-treated cells served as controls. Mean±SEM of 3 independent experiments. *: P
Figure Legend Snippet: Transfection of gastric epithelial cells with GFP-Bcl2 inhibits VacA-induced apoptosis while not blocking pinocytosis or intracellular trafficking of the toxin. (A) Apoptosis (shown as fold increase over the respective non-transfected control cells) induced by either VacA or etoposide in AGS or MKN 28 cells transfected with GFP-Bcl2, GFP-Bcl-xL, GFP-Mcl1, or the GFP vector. Cells were treated with VacA or etoposide as in Figure 3A . Non-treated cells served as controls. Mean±SEM of 3 independent experiments. *: P

Techniques Used: Transfection, Blocking Assay, Plasmid Preparation

5) Product Images from "Proteomics-Based Identification and Analysis of Proteins Associated with Helicobacter pylori in Gastric Cancer"

Article Title: Proteomics-Based Identification and Analysis of Proteins Associated with Helicobacter pylori in Gastric Cancer

Journal: PLoS ONE

doi: 10.1371/journal.pone.0146521

Introduction of CagA into gastric cancer cells. (A and B) Western blot analysis of CagA and phosphorylated CagA in H . pylori -infected SGC-7901(A) and AGS (B) cells. The cells infected with the indicated ratio of cells to H . pylori for the indicated time were collected and lysed, and the proteins were separated by SDS-PAGE. Cells infected with H . pylori boiled for 15 min at a MOI of 1:1000 were used as a control. (C and D) Detection of CagA mRNA and protein in cagA -overexpressing SGC-7901 cells by RT-PCR (C) and western blot (D). GAPDH served as the loading control. The data are representative of three independent experiments. Hp , H . pylori ; P-CagA, phosphorylated CagA; GAPDH, Glyceraldehyde-3-phosphate- dehydrogenase.
Figure Legend Snippet: Introduction of CagA into gastric cancer cells. (A and B) Western blot analysis of CagA and phosphorylated CagA in H . pylori -infected SGC-7901(A) and AGS (B) cells. The cells infected with the indicated ratio of cells to H . pylori for the indicated time were collected and lysed, and the proteins were separated by SDS-PAGE. Cells infected with H . pylori boiled for 15 min at a MOI of 1:1000 were used as a control. (C and D) Detection of CagA mRNA and protein in cagA -overexpressing SGC-7901 cells by RT-PCR (C) and western blot (D). GAPDH served as the loading control. The data are representative of three independent experiments. Hp , H . pylori ; P-CagA, phosphorylated CagA; GAPDH, Glyceraldehyde-3-phosphate- dehydrogenase.

Techniques Used: Western Blot, Infection, SDS Page, Reverse Transcription Polymerase Chain Reaction

6) Product Images from "Inhibitory Effects of Anthocyanins on Secretion of Helicobacter pylori CagA and VacA Toxins"

Article Title: Inhibitory Effects of Anthocyanins on Secretion of Helicobacter pylori CagA and VacA Toxins

Journal: International Journal of Medical Sciences

doi: 10.7150/ijms.5094

Effect of anthocyanins on secretion of H. pylori CagA and VacA. H. pylori was cultured with 100 μM of anthocyanin in Mueller-Hinton broth/10% FBS for 3 days and proteins assessed by Western blot. (A), secreted CagA and VacA in culture media. (B), secreted H. pylori proteins reacting with rabbit anti- H. pylori polyclonal antibody. (C) , intracellular CagA and VacA. (D) , intracellular H. pylori proteins reacting with rabbit anti- H. pylori polyclonal antibody. Representative image from five independent experiments.
Figure Legend Snippet: Effect of anthocyanins on secretion of H. pylori CagA and VacA. H. pylori was cultured with 100 μM of anthocyanin in Mueller-Hinton broth/10% FBS for 3 days and proteins assessed by Western blot. (A), secreted CagA and VacA in culture media. (B), secreted H. pylori proteins reacting with rabbit anti- H. pylori polyclonal antibody. (C) , intracellular CagA and VacA. (D) , intracellular H. pylori proteins reacting with rabbit anti- H. pylori polyclonal antibody. Representative image from five independent experiments.

Techniques Used: Cell Culture, Western Blot

7) Product Images from "Comparative Transcriptomics of H. pylori Strains AM5, SS1 and Their hpyAVIBM Deletion Mutants: Possible Roles of Cytosine Methylation"

Article Title: Comparative Transcriptomics of H. pylori Strains AM5, SS1 and Their hpyAVIBM Deletion Mutants: Possible Roles of Cytosine Methylation

Journal: PLoS ONE

doi: 10.1371/journal.pone.0042303

Western blotting for CagA and VacA protein levels in H. pylori strainsAM5 and AM5Δ hpyAVIBM .
Figure Legend Snippet: Western blotting for CagA and VacA protein levels in H. pylori strainsAM5 and AM5Δ hpyAVIBM .

Techniques Used: Western Blot

8) Product Images from "Helicobacter pylori Counteracts the Apoptotic Action of Its VacA Toxin by Injecting the CagA Protein into Gastric Epithelial Cells"

Article Title: Helicobacter pylori Counteracts the Apoptotic Action of Its VacA Toxin by Injecting the CagA Protein into Gastric Epithelial Cells

Journal: PLoS Pathogens

doi: 10.1371/journal.ppat.1000603

Transfection of gastric epithelial cells with GFP-Bcl2 inhibits VacA-induced apoptosis while not blocking pinocytosis or intracellular trafficking of the toxin. (A) Apoptosis (shown as fold increase over the respective non-transfected control cells) induced by either VacA or etoposide in AGS or MKN 28 cells transfected with GFP-Bcl2, GFP-Bcl-xL, GFP-Mcl1, or the GFP vector. Cells were treated with VacA or etoposide as in Figure 3A . Non-treated cells served as controls. Mean±SEM of 3 independent experiments. *: P
Figure Legend Snippet: Transfection of gastric epithelial cells with GFP-Bcl2 inhibits VacA-induced apoptosis while not blocking pinocytosis or intracellular trafficking of the toxin. (A) Apoptosis (shown as fold increase over the respective non-transfected control cells) induced by either VacA or etoposide in AGS or MKN 28 cells transfected with GFP-Bcl2, GFP-Bcl-xL, GFP-Mcl1, or the GFP vector. Cells were treated with VacA or etoposide as in Figure 3A . Non-treated cells served as controls. Mean±SEM of 3 independent experiments. *: P

Techniques Used: Transfection, Blocking Assay, Plasmid Preparation

9) Product Images from "Comparative Transcriptomics of H. pylori Strains AM5, SS1 and Their hpyAVIBM Deletion Mutants: Possible Roles of Cytosine Methylation"

Article Title: Comparative Transcriptomics of H. pylori Strains AM5, SS1 and Their hpyAVIBM Deletion Mutants: Possible Roles of Cytosine Methylation

Journal: PLoS ONE

doi: 10.1371/journal.pone.0042303

Western blotting for CagA and VacA protein levels in H. pylori strainsAM5 and AM5Δ hpyAVIBM .
Figure Legend Snippet: Western blotting for CagA and VacA protein levels in H. pylori strainsAM5 and AM5Δ hpyAVIBM .

Techniques Used: Western Blot

10) Product Images from "Functional Analysis of the cag Pathogenicity Island in Helicobacter pylori Isolates from Patients with Gastritis, Peptic Ulcer, and Gastric Cancer "

Article Title: Functional Analysis of the cag Pathogenicity Island in Helicobacter pylori Isolates from Patients with Gastritis, Peptic Ulcer, and Gastric Cancer

Journal: Infection and Immunity

doi: 10.1128/IAI.72.2.1043-1056.2004

In vitro phosphorylation of CagA. (A) We observed nine nonphosphorylated CagA protein species during infection of AGS cells with the following H. pylori strains: M15, M27, M33, and M64 (gastritis group); Ka61 (peptic ulcer group); and MPI47, Ca115, Ca130, and Ca204 (gastric cancer group). These CagA proteins could be phosphorylated in an in vitro phosphorylation assay. The results are shown for three strains. Incubation of the H. pylori lysate with lysate of AGS cells or recombinant human c-Src (data not shown) resulted in specific CagA phosphorylation (arrowhead). The lysates of the TIGR H. pylori strain 26695 and a phosphorylation-deficient deletion mutant (ΔP-Tyr) were used as positive and negative controls, respectively. CagA phosphorylation was not detected either in the lysate of wild-type H. pylori incubated without c-Src or in the lysate of the CagAΔP-Tyr mutant incubated with c-Src. (B) An anti-CagA blot with antibody Ab-1 was performed as a control. +, present; −, absent.
Figure Legend Snippet: In vitro phosphorylation of CagA. (A) We observed nine nonphosphorylated CagA protein species during infection of AGS cells with the following H. pylori strains: M15, M27, M33, and M64 (gastritis group); Ka61 (peptic ulcer group); and MPI47, Ca115, Ca130, and Ca204 (gastric cancer group). These CagA proteins could be phosphorylated in an in vitro phosphorylation assay. The results are shown for three strains. Incubation of the H. pylori lysate with lysate of AGS cells or recombinant human c-Src (data not shown) resulted in specific CagA phosphorylation (arrowhead). The lysates of the TIGR H. pylori strain 26695 and a phosphorylation-deficient deletion mutant (ΔP-Tyr) were used as positive and negative controls, respectively. CagA phosphorylation was not detected either in the lysate of wild-type H. pylori incubated without c-Src or in the lysate of the CagAΔP-Tyr mutant incubated with c-Src. (B) An anti-CagA blot with antibody Ab-1 was performed as a control. +, present; −, absent.

Techniques Used: In Vitro, Infection, Phosphorylation Assay, Incubation, Recombinant, Mutagenesis

11) Product Images from "KCTD5 and Ubiquitin Proteasome Signaling Are Required for Helicobacter pylori Adherence"

Article Title: KCTD5 and Ubiquitin Proteasome Signaling Are Required for Helicobacter pylori Adherence

Journal: Frontiers in Cellular and Infection Microbiology

doi: 10.3389/fcimb.2017.00450

Ubiquitination of total proteins and proteasome activity in AGS cells co-cultured with H. pylori . (A) Representative immunoblot of total ubiquitinated protein from AGS cells infected with H. pylori (MOI = 300) for 8 h, in presence or absence of 2.5 μM Lactacystin. Tubulin is shown as loading control and CagA as infection control. (B) Quantification of proteasome activity in AGS cells infected with H. pylori wild type and its isogenic mutants cagA, vacA and, in presence of 2.5 μM Lactacystin for 8 h. Asterisk represents significant difference ( p
Figure Legend Snippet: Ubiquitination of total proteins and proteasome activity in AGS cells co-cultured with H. pylori . (A) Representative immunoblot of total ubiquitinated protein from AGS cells infected with H. pylori (MOI = 300) for 8 h, in presence or absence of 2.5 μM Lactacystin. Tubulin is shown as loading control and CagA as infection control. (B) Quantification of proteasome activity in AGS cells infected with H. pylori wild type and its isogenic mutants cagA, vacA and, in presence of 2.5 μM Lactacystin for 8 h. Asterisk represents significant difference ( p

Techniques Used: Activity Assay, Cell Culture, Infection

12) Product Images from "Dynamic Expansion and Contraction of cagA Copy Number in Helicobacter pylori Impact Development of Gastric Disease"

Article Title: Dynamic Expansion and Contraction of cagA Copy Number in Helicobacter pylori Impact Development of Gastric Disease

Journal: mBio

doi: 10.1128/mBio.01779-16

Relative levels of CagA protein and CagA phosphorylation. (A) The protein levels of CagA and UreA in lysates of H. pylori strains PMSS1, S F -1, S L -2, M F -3, and M L -1 were measured by Western blotting (upper panel). For each lysate, 0.5, 1, 1.5, and 2 μg of total protein were used to determine standard curves for CagA and UreA. The immunoblot images were analyzed using ImageJ software, and the values were plotted on a graph (lower panel). (B) Ratios of CagA to UreA were calculated, and each value was normalized to the value calculated for cagA -S F -1 to determine relative CagA protein levels. The bar graphs indicate average levels of CagA expression of each strain, and error bars represent standard deviations, derived from results of 2 independent experiments. (C) Lysates of AGS cells that were infected with H. pylori strains PMSS1, Δ cagA FL -2, S F -1, S L -2, M F -3, and M L -1 were immunoblotted for phosphorylated CagA (p-CagA), glyceraldehyde-3-phosphate dehydrogenase (GAPDH), CagA, and UreA. GAPDH and UreA were used as controls.
Figure Legend Snippet: Relative levels of CagA protein and CagA phosphorylation. (A) The protein levels of CagA and UreA in lysates of H. pylori strains PMSS1, S F -1, S L -2, M F -3, and M L -1 were measured by Western blotting (upper panel). For each lysate, 0.5, 1, 1.5, and 2 μg of total protein were used to determine standard curves for CagA and UreA. The immunoblot images were analyzed using ImageJ software, and the values were plotted on a graph (lower panel). (B) Ratios of CagA to UreA were calculated, and each value was normalized to the value calculated for cagA -S F -1 to determine relative CagA protein levels. The bar graphs indicate average levels of CagA expression of each strain, and error bars represent standard deviations, derived from results of 2 independent experiments. (C) Lysates of AGS cells that were infected with H. pylori strains PMSS1, Δ cagA FL -2, S F -1, S L -2, M F -3, and M L -1 were immunoblotted for phosphorylated CagA (p-CagA), glyceraldehyde-3-phosphate dehydrogenase (GAPDH), CagA, and UreA. GAPDH and UreA were used as controls.

Techniques Used: Western Blot, Software, Expressing, Derivative Assay, Infection

13) Product Images from "Proteasome Particle-Rich Structures Are Widely Present in Human Epithelial Neoplasms: Correlative Light, Confocal and Electron Microscopy Study"

Article Title: Proteasome Particle-Rich Structures Are Widely Present in Human Epithelial Neoplasms: Correlative Light, Confocal and Electron Microscopy Study

Journal: PLoS ONE

doi: 10.1371/journal.pone.0021317

Lung large cell carcinoma, hepatocarcinoma and colon adenocarcinoma. ( A – C ) Juxtanuclear PaCS in a lung large cell carcinoma ( A , 10,000x), boxed area enlarged in B (50,000x) whose boxed area is enlarged in C (75,000x) to show its particulate structure and proteasome immunogold reactivity. ( D and E ) Hepatocellular carcinoma showing both hyaline bodies (hb), reactive for p62 protein in D (30,000x) and unreactive for 19S proteasome in E (25,000x), and PaCS (asterisks) unreactive for p62 and reactive for 19S proteasome. r, ribosomes. Inset to D (450x): hyaline and Mallory bodies react for p62 protein immunoperoxidase in formalin-fixed paraffin sections. ( F – H ) Colon adenocarcinoma ( F , 10,000x) with partly intracellular and partly interstitial bacteria, a cytoplasmic vacuole (v) and a PaCS (boxed) bordering the cell plasma membrane, enlarged in G (40,000x) and H (75,000x). Note partial lysis of proteasome particles, though retaining 19S proteasome reactivity, development of irregular dense bodies and an encircling peripheral membrane, suggesting transition from a PaCS to an autophagic vacuole, also enclosing ribosome-like particles (r) and a bacterium (top right in G and H ) with capsulated wall typical of Gram-positive organisms.
Figure Legend Snippet: Lung large cell carcinoma, hepatocarcinoma and colon adenocarcinoma. ( A – C ) Juxtanuclear PaCS in a lung large cell carcinoma ( A , 10,000x), boxed area enlarged in B (50,000x) whose boxed area is enlarged in C (75,000x) to show its particulate structure and proteasome immunogold reactivity. ( D and E ) Hepatocellular carcinoma showing both hyaline bodies (hb), reactive for p62 protein in D (30,000x) and unreactive for 19S proteasome in E (25,000x), and PaCS (asterisks) unreactive for p62 and reactive for 19S proteasome. r, ribosomes. Inset to D (450x): hyaline and Mallory bodies react for p62 protein immunoperoxidase in formalin-fixed paraffin sections. ( F – H ) Colon adenocarcinoma ( F , 10,000x) with partly intracellular and partly interstitial bacteria, a cytoplasmic vacuole (v) and a PaCS (boxed) bordering the cell plasma membrane, enlarged in G (40,000x) and H (75,000x). Note partial lysis of proteasome particles, though retaining 19S proteasome reactivity, development of irregular dense bodies and an encircling peripheral membrane, suggesting transition from a PaCS to an autophagic vacuole, also enclosing ribosome-like particles (r) and a bacterium (top right in G and H ) with capsulated wall typical of Gram-positive organisms.

Techniques Used: Lysis

14) Product Images from "Complex Cellular Responses of Helicobacter pylori-Colonized Gastric Adenocarcinoma Cells ▿"

Article Title: Complex Cellular Responses of Helicobacter pylori-Colonized Gastric Adenocarcinoma Cells ▿

Journal: Infection and Immunity

doi: 10.1128/IAI.01350-10

Kinetics of CagA phosphorylation. Cells were either left untreated (−) or infected with H. pylori at an MOI of 50 for the indicated time periods. CagA tyrosine phosphorylation was analyzed by immunoblotting using an anti-phosphotyrosine (p-CagA)
Figure Legend Snippet: Kinetics of CagA phosphorylation. Cells were either left untreated (−) or infected with H. pylori at an MOI of 50 for the indicated time periods. CagA tyrosine phosphorylation was analyzed by immunoblotting using an anti-phosphotyrosine (p-CagA)

Techniques Used: Infection

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Transfection:

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Isolation:

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Real-time Polymerase Chain Reaction:

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Incubation:

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    Santa Cruz Biotechnology rabbit igg anti caga polyclonal antibody b 300
    Expression, delivery, and phosphorylation of <t>CagA.</t> (A) Western blot analysis of bacterial lysates from the six indicated Korean strains was conducted using a monoclonal anti-CagA antibody (top) or the <t>polyclonal</t> anti-CagA antibody b-300 (bottom). (B)
    Rabbit Igg Anti Caga Polyclonal Antibody B 300, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 85/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit igg anti caga polyclonal antibody b 300/product/Santa Cruz Biotechnology
    Average 85 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    rabbit igg anti caga polyclonal antibody b 300 - by Bioz Stars, 2020-09
    85/100 stars
      Buy from Supplier

    85
    Santa Cruz Biotechnology rabbit polyclonal anti caga
    Expression, delivery, and phosphorylation of <t>CagA.</t> (A) Western blot analysis of bacterial lysates from the six indicated Korean strains was conducted using a monoclonal anti-CagA antibody (top) or the <t>polyclonal</t> anti-CagA antibody b-300 (bottom). (B)
    Rabbit Polyclonal Anti Caga, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 85/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit polyclonal anti caga/product/Santa Cruz Biotechnology
    Average 85 stars, based on 3 article reviews
    Price from $9.99 to $1999.99
    rabbit polyclonal anti caga - by Bioz Stars, 2020-09
    85/100 stars
      Buy from Supplier

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    Expression, delivery, and phosphorylation of CagA. (A) Western blot analysis of bacterial lysates from the six indicated Korean strains was conducted using a monoclonal anti-CagA antibody (top) or the polyclonal anti-CagA antibody b-300 (bottom). (B)

    Journal: Journal of Clinical Microbiology

    Article Title: Polymorphism in the CagA EPIYA Motif Impacts Development of Gastric Cancer ▿Polymorphism in the CagA EPIYA Motif Impacts Development of Gastric Cancer ▿ §

    doi: 10.1128/JCM.02330-08

    Figure Lengend Snippet: Expression, delivery, and phosphorylation of CagA. (A) Western blot analysis of bacterial lysates from the six indicated Korean strains was conducted using a monoclonal anti-CagA antibody (top) or the polyclonal anti-CagA antibody b-300 (bottom). (B)

    Article Snippet: Alternatively, membranes were probed with a 1:5,000 dilution of rabbit IgG anti-CagA polyclonal antibody b-300 (Santa Cruz Biotechnology), followed by a 1:20,000 dilution of HRP-conjugated bovine anti-rabbit IgG secondary antibody (Santa Cruz Biotechnology).

    Techniques: Expressing, Western Blot