38467 Search Results


mbt 384678  (ATCC)
90
ATCC mbt 384678
Mbt 384678, supplied by ATCC, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 90 stars, based on 1 article reviews
mbt 384678 - by Bioz Stars, 2026-03
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ci m6pr  (Novus Biologicals)
91
Novus Biologicals ci m6pr
Functional interaction of UL35 proteins with sorting nexin 5. (A) In a macropinocytosis assay, HeLa cells were transfected with an expression plasmid for FLAG-SNX5 and an expression plasmid for ppUL35 or ppUL35A. At 24 h after transfection, the cells were serum starved for 12 h. Cells were incubated for 3 min with EGF (to increase the basal macropinocytosis rate) and FITC-dextran and subsequently detached and fixed with paraformaldehyde. Uptake of FITC-dextran was measured by quantitation of positive cells by flow cytometry. Results are representative of those from at least 3 independent uptake assays; error bars indicate standard deviations. Significance was calculated employing a two-tailed Student's t test with the Welch correction. (B) To analyze the effects of UL35 proteins on the subcellular localization of <t>CI-M6PR,</t> HeLa cells were transfected with expression plasmids for EYFP-UL35 or EYFP-UL35A or for EYFP-UL82 as a control. At 24 h after transfection, cells were fixed with paraformaldehyde and stained with a specific antibody directed against CI-M6PR. At least 100 cells were scored for compact or dispersed localization. Error bars indicate standard deviations. Similar results were obtained in 3 independent experiments. Significance was calculated employing a two-tailed Student's t test with the Welch correction. *, P ≤ 0.05; **, P ≤ 0.01.
Ci M6pr, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/ci m6pr/product/Novus Biologicals
Average 91 stars, based on 1 article reviews
ci m6pr - by Bioz Stars, 2026-03
91/100 stars
  Buy from Supplier

Image Search Results


Functional interaction of UL35 proteins with sorting nexin 5. (A) In a macropinocytosis assay, HeLa cells were transfected with an expression plasmid for FLAG-SNX5 and an expression plasmid for ppUL35 or ppUL35A. At 24 h after transfection, the cells were serum starved for 12 h. Cells were incubated for 3 min with EGF (to increase the basal macropinocytosis rate) and FITC-dextran and subsequently detached and fixed with paraformaldehyde. Uptake of FITC-dextran was measured by quantitation of positive cells by flow cytometry. Results are representative of those from at least 3 independent uptake assays; error bars indicate standard deviations. Significance was calculated employing a two-tailed Student's t test with the Welch correction. (B) To analyze the effects of UL35 proteins on the subcellular localization of CI-M6PR, HeLa cells were transfected with expression plasmids for EYFP-UL35 or EYFP-UL35A or for EYFP-UL82 as a control. At 24 h after transfection, cells were fixed with paraformaldehyde and stained with a specific antibody directed against CI-M6PR. At least 100 cells were scored for compact or dispersed localization. Error bars indicate standard deviations. Similar results were obtained in 3 independent experiments. Significance was calculated employing a two-tailed Student's t test with the Welch correction. *, P ≤ 0.05; **, P ≤ 0.01.

Journal: Journal of Virology

Article Title: Interaction of Human Cytomegalovirus Tegument Proteins ppUL35 and ppUL35A with Sorting Nexin 5 Regulates Glycoprotein B (gpUL55) Localization

doi: 10.1128/JVI.00013-18

Figure Lengend Snippet: Functional interaction of UL35 proteins with sorting nexin 5. (A) In a macropinocytosis assay, HeLa cells were transfected with an expression plasmid for FLAG-SNX5 and an expression plasmid for ppUL35 or ppUL35A. At 24 h after transfection, the cells were serum starved for 12 h. Cells were incubated for 3 min with EGF (to increase the basal macropinocytosis rate) and FITC-dextran and subsequently detached and fixed with paraformaldehyde. Uptake of FITC-dextran was measured by quantitation of positive cells by flow cytometry. Results are representative of those from at least 3 independent uptake assays; error bars indicate standard deviations. Significance was calculated employing a two-tailed Student's t test with the Welch correction. (B) To analyze the effects of UL35 proteins on the subcellular localization of CI-M6PR, HeLa cells were transfected with expression plasmids for EYFP-UL35 or EYFP-UL35A or for EYFP-UL82 as a control. At 24 h after transfection, cells were fixed with paraformaldehyde and stained with a specific antibody directed against CI-M6PR. At least 100 cells were scored for compact or dispersed localization. Error bars indicate standard deviations. Similar results were obtained in 3 independent experiments. Significance was calculated employing a two-tailed Student's t test with the Welch correction. *, P ≤ 0.05; **, P ≤ 0.01.

Article Snippet: A rabbit monoclonal antibody against β-actin (13E5) was purchased from Cell Signaling Technologies (Frankfurt, Germany), polyclonal rabbit anti-SNX5 antibody (H-40) and polyclonal goat anti-SNX5 were from Santa Cruz (Heidelberg, Germany), and mouse monoclonal antibody directed against CI-M6PR was from Novus Biologicals (Littleton, USA).

Techniques: Functional Assay, Transfection, Expressing, Plasmid Preparation, Incubation, Quantitation Assay, Flow Cytometry, Two Tailed Test, Control, Staining

Characterization of a pentapeptide insertion mutant of ppUL35. (A) 293T cells were transfected with expression plasmids for the ppUL35 pentapeptide insertion mutant Tn71 or Tn72 as well as FLAG-SNX5. After 24 h, cell extracts were precipitated with mouse monoclonal antibody against the FLAG (M2) epitope. Precipitated proteins were separated by polyacrylamide gel electrophoresis, and coprecipitated UL35 proteins were detected with a specific rabbit antiserum. Expression of the respective proteins in the cell extracts (lysate controls) was controlled by immunoblotting (bottom). (B) 293T cells were transfected with expression plasmids for wild-type ppUL35 or the Tn71 mutant as well as ppUL82. After 24 h, cell extracts were precipitated with mouse monoclonal antibodies against the ppUL82 (CMV355) or Myc (9E10) epitope. Precipitated proteins were separated by polyacrylamide gel electrophoresis, and coprecipitated UL35 proteins were detected with a specific rabbit antiserum. (C) U373 cells were transfected in triplicate with the HCMV modulator/enhancer luciferase reporter plasmid pHM287 and effector plasmids expressing the indicated genes. All samples contained the same total amount of DNA. After 24 h, luciferase activity was measured. Results are representative of those from 2 or 3 independent experiments. Significance was calculated employing two-tailed Student's t test. *, P ≤ 0.05; ***, P ≤ 0.001; n.s., not significant. (D) HeLa cells were transfected with empty vector as a control or the expression plasmids for wild-type ppUL35 or the ppUL35-Tn71 mutant. At 24 h after transfection, cells were fixed with paraformaldehyde and stained with a rabbit serum directed against ppUL35 and a mouse monoclonal antibody directed against CI-M6PR to assess the subcellular distribution pattern. Two additional experiments yielded comparable results.

Journal: Journal of Virology

Article Title: Interaction of Human Cytomegalovirus Tegument Proteins ppUL35 and ppUL35A with Sorting Nexin 5 Regulates Glycoprotein B (gpUL55) Localization

doi: 10.1128/JVI.00013-18

Figure Lengend Snippet: Characterization of a pentapeptide insertion mutant of ppUL35. (A) 293T cells were transfected with expression plasmids for the ppUL35 pentapeptide insertion mutant Tn71 or Tn72 as well as FLAG-SNX5. After 24 h, cell extracts were precipitated with mouse monoclonal antibody against the FLAG (M2) epitope. Precipitated proteins were separated by polyacrylamide gel electrophoresis, and coprecipitated UL35 proteins were detected with a specific rabbit antiserum. Expression of the respective proteins in the cell extracts (lysate controls) was controlled by immunoblotting (bottom). (B) 293T cells were transfected with expression plasmids for wild-type ppUL35 or the Tn71 mutant as well as ppUL82. After 24 h, cell extracts were precipitated with mouse monoclonal antibodies against the ppUL82 (CMV355) or Myc (9E10) epitope. Precipitated proteins were separated by polyacrylamide gel electrophoresis, and coprecipitated UL35 proteins were detected with a specific rabbit antiserum. (C) U373 cells were transfected in triplicate with the HCMV modulator/enhancer luciferase reporter plasmid pHM287 and effector plasmids expressing the indicated genes. All samples contained the same total amount of DNA. After 24 h, luciferase activity was measured. Results are representative of those from 2 or 3 independent experiments. Significance was calculated employing two-tailed Student's t test. *, P ≤ 0.05; ***, P ≤ 0.001; n.s., not significant. (D) HeLa cells were transfected with empty vector as a control or the expression plasmids for wild-type ppUL35 or the ppUL35-Tn71 mutant. At 24 h after transfection, cells were fixed with paraformaldehyde and stained with a rabbit serum directed against ppUL35 and a mouse monoclonal antibody directed against CI-M6PR to assess the subcellular distribution pattern. Two additional experiments yielded comparable results.

Article Snippet: A rabbit monoclonal antibody against β-actin (13E5) was purchased from Cell Signaling Technologies (Frankfurt, Germany), polyclonal rabbit anti-SNX5 antibody (H-40) and polyclonal goat anti-SNX5 were from Santa Cruz (Heidelberg, Germany), and mouse monoclonal antibody directed against CI-M6PR was from Novus Biologicals (Littleton, USA).

Techniques: Mutagenesis, Transfection, Expressing, Polyacrylamide Gel Electrophoresis, Western Blot, Bioprocessing, Luciferase, Plasmid Preparation, Activity Assay, Two Tailed Test, Control, Staining