reference strain jcm 13569 Search Results


reference bacterial strains  (ATCC)
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ATCC reference bacterial strains
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reference strain jcm 13569  (ATCC)
94
ATCC reference strain jcm 13569
Reference Strain Jcm 13569, 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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mycobacterium abscessus (strain mycobacteroides abscessus subspecies abscessus, jcm 13569)  (BioResource International Inc)
90
BioResource International Inc mycobacterium abscessus (strain mycobacteroides abscessus subspecies abscessus, jcm 13569)
Mycobacterium Abscessus (Strain Mycobacteroides Abscessus Subspecies Abscessus, Jcm 13569), supplied by BioResource International Inc, 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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aphrodite  (Addgene inc)
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Addgene inc aphrodite
Aphrodite, supplied by Addgene inc, 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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recombinant human pitp  (Santa Cruz Biotechnology)
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Santa Cruz Biotechnology recombinant human pitp
Recombinant Human Pitp, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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atp6v1b1/2 (#13569)  (Cell Signaling Technology Inc)
90
Cell Signaling Technology Inc atp6v1b1/2 (#13569)
(A) LAMTOR1 was immunoprecipitated with anti-HA antibodies from HEK293 cell expressing HA-LAMTOR1 and/or Flag-RagB and/or p27 and immunoblotted against Flag (RagB) and HA (LAMTOR1). Expression of the transfected proteins was verified by immunoblot of extracts with anti-Flag, −p27 and −HA antibodies. (B) Quantification of the amount of RagB co-precipitated with LAMTOR1 as in A from 5 experiments. Values were normalized to that in absence of p27. (C) RagB/D were immunoprecipitated with anti-Flag antibodies from HEK293 cell expressing HA-LAMTOR1 and/or Flag-RagB/D and/or Flag-RagB Q99L (RagB GTP)/RagD S77L (RagD GDP) and/or p27 and immunoblotted against Flag (RagB/D) and HA (LAMTOR1). Expression of transfected p27 and HA-LAMTOR1 in corresponding extracts are shown. (D) RagC was immunoprecipitated from p27 +/+ and p27 −/− MEFs in full medium or aa starved for 24 h and the amount of LAMTOR4 co-precipitated was determined. Control IP with rabbit IgG was used as control. Levels of RagC and LAMTOR4 in the corresponding extracts are shown. β-actin was used as loading control. (E) Ratio of LAMTOR4 co-precipitated by that of RagC immunoprecipitated from p27 +/+ and p27 −/− MEFs in full medium or aa starved for 24 h, normalized to full medium condition from 2 experiments as described in E. (F) RagB was immunoprecipitated with anti-Flag antibodies from HEK293 cells expressing Myc-Raptor and/or Flag-RagB and/or p27 and immunoblotted against Myc (Raptor) and Flag (RagB). Expression of the transfected proteins was verified by immunoblot of extracts with anti-Myc, −p27 and −Flag antibodies. (G) Quantification of the amount of Raptor co-precipitated with RagB as described in G from 3 experiments. Values were normalized to that in absence of p27. (H) Raptor was immunoprecipitated with anti-Myc antibodies from HEK293 cells expressing Myc-Raptor and/or Flag-RagB Q99L (RagB GTP)/RagD S77L (RagD GDP) and/or p27 and immunoblotted against Flag (RagB/D) and Myc (Raptor). Expression of transfected p27, Flag RagB/D and Myc-Raptor in corresponding extracts are shown. (I) Schematic summarizing the impact of p27 on Rag and mTORC1 recruitment to Ragulator. (J) TFEB immunostaining in p27 +/+ and p27 −/− MEFs in full medium (0 h) or aa-starved for 48 h. F-actin was stained with phalloïdin and DNA with Hoechst. Scale bars are 50 µm. (K) Percentage of cells with nuclear TFEB signal in cells treated as in K from 3 experiments. At least 87 cells per condition for each genotype were analyzed in each experiment. (L) Fold change of the v-ATPase subunit ATP6V0E1, CTSB (Cathepsin-B) and PUMA mRNA levels in p27 +/+ and p27 −/− MEFs in full medium or aa starved for 1 h or 48 h, determined by RT-qPCR and normalized to GAPDH levels from 8 experiments. All values were normalized to p27 +/+ MEFs in full medium (0 h). (M) Immunoblot for the v-ATPase subunit <t>ATP6V1B1/2,</t> PUMA and p27 in p27 +/+ and p27 −/− MEFs in full medium or aa starved for 24 h. Grb2 was used as loading control. (B, E, G, K, L) Bar graphs show means ± SEM. Statistical significance was evaluated by unpaired t-test with Welch’s correction (B, G) or 2-way ANOVA (K, L); ns: p >0.05; *: p ≤ 0.05; ***: p ≤ 0.001; ****: p ≤ 0.0001.
Atp6v1b1/2 (#13569), supplied by Cell Signaling Technology Inc, 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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rhoa  (Cytoskeleton Inc)
90
Cytoskeleton Inc rhoa
(A) LAMTOR1 was immunoprecipitated with anti-HA antibodies from HEK293 cell expressing HA-LAMTOR1 and/or Flag-RagB and/or p27 and immunoblotted against Flag (RagB) and HA (LAMTOR1). Expression of the transfected proteins was verified by immunoblot of extracts with anti-Flag, −p27 and −HA antibodies. (B) Quantification of the amount of RagB co-precipitated with LAMTOR1 as in A from 5 experiments. Values were normalized to that in absence of p27. (C) RagB/D were immunoprecipitated with anti-Flag antibodies from HEK293 cell expressing HA-LAMTOR1 and/or Flag-RagB/D and/or Flag-RagB Q99L (RagB GTP)/RagD S77L (RagD GDP) and/or p27 and immunoblotted against Flag (RagB/D) and HA (LAMTOR1). Expression of transfected p27 and HA-LAMTOR1 in corresponding extracts are shown. (D) RagC was immunoprecipitated from p27 +/+ and p27 −/− MEFs in full medium or aa starved for 24 h and the amount of LAMTOR4 co-precipitated was determined. Control IP with rabbit IgG was used as control. Levels of RagC and LAMTOR4 in the corresponding extracts are shown. β-actin was used as loading control. (E) Ratio of LAMTOR4 co-precipitated by that of RagC immunoprecipitated from p27 +/+ and p27 −/− MEFs in full medium or aa starved for 24 h, normalized to full medium condition from 2 experiments as described in E. (F) RagB was immunoprecipitated with anti-Flag antibodies from HEK293 cells expressing Myc-Raptor and/or Flag-RagB and/or p27 and immunoblotted against Myc (Raptor) and Flag (RagB). Expression of the transfected proteins was verified by immunoblot of extracts with anti-Myc, −p27 and −Flag antibodies. (G) Quantification of the amount of Raptor co-precipitated with RagB as described in G from 3 experiments. Values were normalized to that in absence of p27. (H) Raptor was immunoprecipitated with anti-Myc antibodies from HEK293 cells expressing Myc-Raptor and/or Flag-RagB Q99L (RagB GTP)/RagD S77L (RagD GDP) and/or p27 and immunoblotted against Flag (RagB/D) and Myc (Raptor). Expression of transfected p27, Flag RagB/D and Myc-Raptor in corresponding extracts are shown. (I) Schematic summarizing the impact of p27 on Rag and mTORC1 recruitment to Ragulator. (J) TFEB immunostaining in p27 +/+ and p27 −/− MEFs in full medium (0 h) or aa-starved for 48 h. F-actin was stained with phalloïdin and DNA with Hoechst. Scale bars are 50 µm. (K) Percentage of cells with nuclear TFEB signal in cells treated as in K from 3 experiments. At least 87 cells per condition for each genotype were analyzed in each experiment. (L) Fold change of the v-ATPase subunit ATP6V0E1, CTSB (Cathepsin-B) and PUMA mRNA levels in p27 +/+ and p27 −/− MEFs in full medium or aa starved for 1 h or 48 h, determined by RT-qPCR and normalized to GAPDH levels from 8 experiments. All values were normalized to p27 +/+ MEFs in full medium (0 h). (M) Immunoblot for the v-ATPase subunit <t>ATP6V1B1/2,</t> PUMA and p27 in p27 +/+ and p27 −/− MEFs in full medium or aa starved for 24 h. Grb2 was used as loading control. (B, E, G, K, L) Bar graphs show means ± SEM. Statistical significance was evaluated by unpaired t-test with Welch’s correction (B, G) or 2-way ANOVA (K, L); ns: p >0.05; *: p ≤ 0.05; ***: p ≤ 0.001; ****: p ≤ 0.0001.
Rhoa, supplied by Cytoskeleton Inc, 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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(A) LAMTOR1 was immunoprecipitated with anti-HA antibodies from HEK293 cell expressing HA-LAMTOR1 and/or Flag-RagB and/or p27 and immunoblotted against Flag (RagB) and HA (LAMTOR1). Expression of the transfected proteins was verified by immunoblot of extracts with anti-Flag, −p27 and −HA antibodies. (B) Quantification of the amount of RagB co-precipitated with LAMTOR1 as in A from 5 experiments. Values were normalized to that in absence of p27. (C) RagB/D were immunoprecipitated with anti-Flag antibodies from HEK293 cell expressing HA-LAMTOR1 and/or Flag-RagB/D and/or Flag-RagB Q99L (RagB GTP)/RagD S77L (RagD GDP) and/or p27 and immunoblotted against Flag (RagB/D) and HA (LAMTOR1). Expression of transfected p27 and HA-LAMTOR1 in corresponding extracts are shown. (D) RagC was immunoprecipitated from p27 +/+ and p27 −/− MEFs in full medium or aa starved for 24 h and the amount of LAMTOR4 co-precipitated was determined. Control IP with rabbit IgG was used as control. Levels of RagC and LAMTOR4 in the corresponding extracts are shown. β-actin was used as loading control. (E) Ratio of LAMTOR4 co-precipitated by that of RagC immunoprecipitated from p27 +/+ and p27 −/− MEFs in full medium or aa starved for 24 h, normalized to full medium condition from 2 experiments as described in E. (F) RagB was immunoprecipitated with anti-Flag antibodies from HEK293 cells expressing Myc-Raptor and/or Flag-RagB and/or p27 and immunoblotted against Myc (Raptor) and Flag (RagB). Expression of the transfected proteins was verified by immunoblot of extracts with anti-Myc, −p27 and −Flag antibodies. (G) Quantification of the amount of Raptor co-precipitated with RagB as described in G from 3 experiments. Values were normalized to that in absence of p27. (H) Raptor was immunoprecipitated with anti-Myc antibodies from HEK293 cells expressing Myc-Raptor and/or Flag-RagB Q99L (RagB GTP)/RagD S77L (RagD GDP) and/or p27 and immunoblotted against Flag (RagB/D) and Myc (Raptor). Expression of transfected p27, Flag RagB/D and Myc-Raptor in corresponding extracts are shown. (I) Schematic summarizing the impact of p27 on Rag and mTORC1 recruitment to Ragulator. (J) TFEB immunostaining in p27 +/+ and p27 −/− MEFs in full medium (0 h) or aa-starved for 48 h. F-actin was stained with phalloïdin and DNA with Hoechst. Scale bars are 50 µm. (K) Percentage of cells with nuclear TFEB signal in cells treated as in K from 3 experiments. At least 87 cells per condition for each genotype were analyzed in each experiment. (L) Fold change of the v-ATPase subunit ATP6V0E1, CTSB (Cathepsin-B) and PUMA mRNA levels in p27 +/+ and p27 −/− MEFs in full medium or aa starved for 1 h or 48 h, determined by RT-qPCR and normalized to GAPDH levels from 8 experiments. All values were normalized to p27 +/+ MEFs in full medium (0 h). (M) Immunoblot for the v-ATPase subunit ATP6V1B1/2, PUMA and p27 in p27 +/+ and p27 −/− MEFs in full medium or aa starved for 24 h. Grb2 was used as loading control. (B, E, G, K, L) Bar graphs show means ± SEM. Statistical significance was evaluated by unpaired t-test with Welch’s correction (B, G) or 2-way ANOVA (K, L); ns: p >0.05; *: p ≤ 0.05; ***: p ≤ 0.001; ****: p ≤ 0.0001.

Journal: bioRxiv

Article Title: p27 regulates the autophagy-lysosomal pathway via the control of Ragulator and mTOR activity in amino acid deprived cells

doi: 10.1101/2020.01.07.896860

Figure Lengend Snippet: (A) LAMTOR1 was immunoprecipitated with anti-HA antibodies from HEK293 cell expressing HA-LAMTOR1 and/or Flag-RagB and/or p27 and immunoblotted against Flag (RagB) and HA (LAMTOR1). Expression of the transfected proteins was verified by immunoblot of extracts with anti-Flag, −p27 and −HA antibodies. (B) Quantification of the amount of RagB co-precipitated with LAMTOR1 as in A from 5 experiments. Values were normalized to that in absence of p27. (C) RagB/D were immunoprecipitated with anti-Flag antibodies from HEK293 cell expressing HA-LAMTOR1 and/or Flag-RagB/D and/or Flag-RagB Q99L (RagB GTP)/RagD S77L (RagD GDP) and/or p27 and immunoblotted against Flag (RagB/D) and HA (LAMTOR1). Expression of transfected p27 and HA-LAMTOR1 in corresponding extracts are shown. (D) RagC was immunoprecipitated from p27 +/+ and p27 −/− MEFs in full medium or aa starved for 24 h and the amount of LAMTOR4 co-precipitated was determined. Control IP with rabbit IgG was used as control. Levels of RagC and LAMTOR4 in the corresponding extracts are shown. β-actin was used as loading control. (E) Ratio of LAMTOR4 co-precipitated by that of RagC immunoprecipitated from p27 +/+ and p27 −/− MEFs in full medium or aa starved for 24 h, normalized to full medium condition from 2 experiments as described in E. (F) RagB was immunoprecipitated with anti-Flag antibodies from HEK293 cells expressing Myc-Raptor and/or Flag-RagB and/or p27 and immunoblotted against Myc (Raptor) and Flag (RagB). Expression of the transfected proteins was verified by immunoblot of extracts with anti-Myc, −p27 and −Flag antibodies. (G) Quantification of the amount of Raptor co-precipitated with RagB as described in G from 3 experiments. Values were normalized to that in absence of p27. (H) Raptor was immunoprecipitated with anti-Myc antibodies from HEK293 cells expressing Myc-Raptor and/or Flag-RagB Q99L (RagB GTP)/RagD S77L (RagD GDP) and/or p27 and immunoblotted against Flag (RagB/D) and Myc (Raptor). Expression of transfected p27, Flag RagB/D and Myc-Raptor in corresponding extracts are shown. (I) Schematic summarizing the impact of p27 on Rag and mTORC1 recruitment to Ragulator. (J) TFEB immunostaining in p27 +/+ and p27 −/− MEFs in full medium (0 h) or aa-starved for 48 h. F-actin was stained with phalloïdin and DNA with Hoechst. Scale bars are 50 µm. (K) Percentage of cells with nuclear TFEB signal in cells treated as in K from 3 experiments. At least 87 cells per condition for each genotype were analyzed in each experiment. (L) Fold change of the v-ATPase subunit ATP6V0E1, CTSB (Cathepsin-B) and PUMA mRNA levels in p27 +/+ and p27 −/− MEFs in full medium or aa starved for 1 h or 48 h, determined by RT-qPCR and normalized to GAPDH levels from 8 experiments. All values were normalized to p27 +/+ MEFs in full medium (0 h). (M) Immunoblot for the v-ATPase subunit ATP6V1B1/2, PUMA and p27 in p27 +/+ and p27 −/− MEFs in full medium or aa starved for 24 h. Grb2 was used as loading control. (B, E, G, K, L) Bar graphs show means ± SEM. Statistical significance was evaluated by unpaired t-test with Welch’s correction (B, G) or 2-way ANOVA (K, L); ns: p >0.05; *: p ≤ 0.05; ***: p ≤ 0.001; ****: p ≤ 0.0001.

Article Snippet: Rabbit anti phospho-p70 S6K1 (Thr389) (#9234), p70 S6K1 (#27087), mTOR (#2983), phospho-mTOR (Ser2448) (#5536), Raptor (#2280), LAMTOR1 (#8975), LAMTOR4 (#13140), LAMTOR5 (#14633), LC3B (#4108), RagA (#4357), RagC (#5466), Cathepsin-B (#D1C7Y), ATP6V1B1/2 (#13569), ULK1 (#8054), phospho-ULK1 (Ser758) (#6888), AMPK (#5832), phospho-AMPK (Thr172) (#2535), p62/SQSTM1 (#39749), phospho-4E-BP1 (Thr37/46) (#2855) and Atg5 (#12994) antibodies were purchased from Cell Signalling Technology.

Techniques: Immunoprecipitation, Expressing, Transfection, Western Blot, Immunostaining, Staining, Quantitative RT-PCR