cox regression stata 9.2 Search Results


q5 site  (New England Biolabs)
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1 methyl2 pyrrolidinone  (Chem Impex International)
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19101xr  (New England Biolabs)
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version 11 1  (STATA Corporation)
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STATA Corporation version 11 1
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version 12 1  (STATA Corporation)
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STATA Corporation version 12 1
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line 1 amplicons  (New England Biolabs)
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New England Biolabs line 1 amplicons
Line 1 Amplicons, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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senp2  (Biosynth Carbosynth)
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Biosynth Carbosynth senp2
Tpr is required for SAC proteostasis throughout the cell cycle. (A and B) Normalized expression of tpr , mad1 , mad2 , mps1 , cdc20 , and p31 in control and Tpr-depleted asynchronous or mitotic cells. Error bars represent standard deviations from three independent experiments. (C) WB analysis of asynchronous, G2, and mitotic enriched HeLa cell extracts from control (+) and Tpr-depleted (−) cells with (+) or without (−) MG132 with the indicated antibodies. The percentage of protein levels relative to controls is indicated. (D) c-Mad2 IP from asynchronous and mitotic HeLa cells with (+) or without (−) Tpr, in the presence (+) or absence (−) of MG132. (E and F) Cells with or without Tpr were treated with cycloheximide (CHX) for various time points as indicated. Total protein extracts of asynchronous HeLa cells were analyzed by WB to detect Tpr, Mps1, Mad1, and t-Mad2 in control and Tpr-depleted cells. α-Tubulin was used as a loading control. *, P < 0.05; **, P < 0.01; ***, P < 0.001. The error bars indicate standard deviations from two independent experiments. (G) Immunodetection of Mad1 (red), SENP1, and <t>SENP2</t> (green) in Tpr-depleted cells (−). A nondepleted cell (+) was used as internal control. DNA was counterstained with DAPI (blue). (H) WB analysis of asynchronous cell extracts in control and after SENP1 or SENP2 RNAi. The percentage of protein levels relative to controls is indicated. α-Tubulin was used as a loading control. Bar, 10 µm.
Senp2, supplied by Biosynth Carbosynth, 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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version 10  (STATA Corporation)
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STATA Corporation version 10
Tpr is required for SAC proteostasis throughout the cell cycle. (A and B) Normalized expression of tpr , mad1 , mad2 , mps1 , cdc20 , and p31 in control and Tpr-depleted asynchronous or mitotic cells. Error bars represent standard deviations from three independent experiments. (C) WB analysis of asynchronous, G2, and mitotic enriched HeLa cell extracts from control (+) and Tpr-depleted (−) cells with (+) or without (−) MG132 with the indicated antibodies. The percentage of protein levels relative to controls is indicated. (D) c-Mad2 IP from asynchronous and mitotic HeLa cells with (+) or without (−) Tpr, in the presence (+) or absence (−) of MG132. (E and F) Cells with or without Tpr were treated with cycloheximide (CHX) for various time points as indicated. Total protein extracts of asynchronous HeLa cells were analyzed by WB to detect Tpr, Mps1, Mad1, and t-Mad2 in control and Tpr-depleted cells. α-Tubulin was used as a loading control. *, P < 0.05; **, P < 0.01; ***, P < 0.001. The error bars indicate standard deviations from two independent experiments. (G) Immunodetection of Mad1 (red), SENP1, and <t>SENP2</t> (green) in Tpr-depleted cells (−). A nondepleted cell (+) was used as internal control. DNA was counterstained with DAPI (blue). (H) WB analysis of asynchronous cell extracts in control and after SENP1 or SENP2 RNAi. The percentage of protein levels relative to controls is indicated. α-Tubulin was used as a loading control. Bar, 10 µm.
Version 10, supplied by STATA Corporation, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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dna polymerase  (New England Biolabs)
96
New England Biolabs dna polymerase
Tpr is required for SAC proteostasis throughout the cell cycle. (A and B) Normalized expression of tpr , mad1 , mad2 , mps1 , cdc20 , and p31 in control and Tpr-depleted asynchronous or mitotic cells. Error bars represent standard deviations from three independent experiments. (C) WB analysis of asynchronous, G2, and mitotic enriched HeLa cell extracts from control (+) and Tpr-depleted (−) cells with (+) or without (−) MG132 with the indicated antibodies. The percentage of protein levels relative to controls is indicated. (D) c-Mad2 IP from asynchronous and mitotic HeLa cells with (+) or without (−) Tpr, in the presence (+) or absence (−) of MG132. (E and F) Cells with or without Tpr were treated with cycloheximide (CHX) for various time points as indicated. Total protein extracts of asynchronous HeLa cells were analyzed by WB to detect Tpr, Mps1, Mad1, and t-Mad2 in control and Tpr-depleted cells. α-Tubulin was used as a loading control. *, P < 0.05; **, P < 0.01; ***, P < 0.001. The error bars indicate standard deviations from two independent experiments. (G) Immunodetection of Mad1 (red), SENP1, and <t>SENP2</t> (green) in Tpr-depleted cells (−). A nondepleted cell (+) was used as internal control. DNA was counterstained with DAPI (blue). (H) WB analysis of asynchronous cell extracts in control and after SENP1 or SENP2 RNAi. The percentage of protein levels relative to controls is indicated. α-Tubulin was used as a loading control. Bar, 10 µm.
Dna Polymerase, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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chs 92 lamp primer mix  (New England Biolabs)
95
New England Biolabs chs 92 lamp primer mix
Tpr is required for SAC proteostasis throughout the cell cycle. (A and B) Normalized expression of tpr , mad1 , mad2 , mps1 , cdc20 , and p31 in control and Tpr-depleted asynchronous or mitotic cells. Error bars represent standard deviations from three independent experiments. (C) WB analysis of asynchronous, G2, and mitotic enriched HeLa cell extracts from control (+) and Tpr-depleted (−) cells with (+) or without (−) MG132 with the indicated antibodies. The percentage of protein levels relative to controls is indicated. (D) c-Mad2 IP from asynchronous and mitotic HeLa cells with (+) or without (−) Tpr, in the presence (+) or absence (−) of MG132. (E and F) Cells with or without Tpr were treated with cycloheximide (CHX) for various time points as indicated. Total protein extracts of asynchronous HeLa cells were analyzed by WB to detect Tpr, Mps1, Mad1, and t-Mad2 in control and Tpr-depleted cells. α-Tubulin was used as a loading control. *, P < 0.05; **, P < 0.01; ***, P < 0.001. The error bars indicate standard deviations from two independent experiments. (G) Immunodetection of Mad1 (red), SENP1, and <t>SENP2</t> (green) in Tpr-depleted cells (−). A nondepleted cell (+) was used as internal control. DNA was counterstained with DAPI (blue). (H) WB analysis of asynchronous cell extracts in control and after SENP1 or SENP2 RNAi. The percentage of protein levels relative to controls is indicated. α-Tubulin was used as a loading control. Bar, 10 µm.
Chs 92 Lamp Primer Mix, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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stata v.9.2  (STATA Corporation)
90
STATA Corporation stata v.9.2
Tpr is required for SAC proteostasis throughout the cell cycle. (A and B) Normalized expression of tpr , mad1 , mad2 , mps1 , cdc20 , and p31 in control and Tpr-depleted asynchronous or mitotic cells. Error bars represent standard deviations from three independent experiments. (C) WB analysis of asynchronous, G2, and mitotic enriched HeLa cell extracts from control (+) and Tpr-depleted (−) cells with (+) or without (−) MG132 with the indicated antibodies. The percentage of protein levels relative to controls is indicated. (D) c-Mad2 IP from asynchronous and mitotic HeLa cells with (+) or without (−) Tpr, in the presence (+) or absence (−) of MG132. (E and F) Cells with or without Tpr were treated with cycloheximide (CHX) for various time points as indicated. Total protein extracts of asynchronous HeLa cells were analyzed by WB to detect Tpr, Mps1, Mad1, and t-Mad2 in control and Tpr-depleted cells. α-Tubulin was used as a loading control. *, P < 0.05; **, P < 0.01; ***, P < 0.001. The error bars indicate standard deviations from two independent experiments. (G) Immunodetection of Mad1 (red), SENP1, and <t>SENP2</t> (green) in Tpr-depleted cells (−). A nondepleted cell (+) was used as internal control. DNA was counterstained with DAPI (blue). (H) WB analysis of asynchronous cell extracts in control and after SENP1 or SENP2 RNAi. The percentage of protein levels relative to controls is indicated. α-Tubulin was used as a loading control. Bar, 10 µm.
Stata V.9.2, supplied by STATA Corporation, 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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grade 92 steel specimens  (BGH Edelstahl Siegen GmbH)
90
BGH Edelstahl Siegen GmbH grade 92 steel specimens
Tpr is required for SAC proteostasis throughout the cell cycle. (A and B) Normalized expression of tpr , mad1 , mad2 , mps1 , cdc20 , and p31 in control and Tpr-depleted asynchronous or mitotic cells. Error bars represent standard deviations from three independent experiments. (C) WB analysis of asynchronous, G2, and mitotic enriched HeLa cell extracts from control (+) and Tpr-depleted (−) cells with (+) or without (−) MG132 with the indicated antibodies. The percentage of protein levels relative to controls is indicated. (D) c-Mad2 IP from asynchronous and mitotic HeLa cells with (+) or without (−) Tpr, in the presence (+) or absence (−) of MG132. (E and F) Cells with or without Tpr were treated with cycloheximide (CHX) for various time points as indicated. Total protein extracts of asynchronous HeLa cells were analyzed by WB to detect Tpr, Mps1, Mad1, and t-Mad2 in control and Tpr-depleted cells. α-Tubulin was used as a loading control. *, P < 0.05; **, P < 0.01; ***, P < 0.001. The error bars indicate standard deviations from two independent experiments. (G) Immunodetection of Mad1 (red), SENP1, and <t>SENP2</t> (green) in Tpr-depleted cells (−). A nondepleted cell (+) was used as internal control. DNA was counterstained with DAPI (blue). (H) WB analysis of asynchronous cell extracts in control and after SENP1 or SENP2 RNAi. The percentage of protein levels relative to controls is indicated. α-Tubulin was used as a loading control. Bar, 10 µm.
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Image Search Results


Tpr is required for SAC proteostasis throughout the cell cycle. (A and B) Normalized expression of tpr , mad1 , mad2 , mps1 , cdc20 , and p31 in control and Tpr-depleted asynchronous or mitotic cells. Error bars represent standard deviations from three independent experiments. (C) WB analysis of asynchronous, G2, and mitotic enriched HeLa cell extracts from control (+) and Tpr-depleted (−) cells with (+) or without (−) MG132 with the indicated antibodies. The percentage of protein levels relative to controls is indicated. (D) c-Mad2 IP from asynchronous and mitotic HeLa cells with (+) or without (−) Tpr, in the presence (+) or absence (−) of MG132. (E and F) Cells with or without Tpr were treated with cycloheximide (CHX) for various time points as indicated. Total protein extracts of asynchronous HeLa cells were analyzed by WB to detect Tpr, Mps1, Mad1, and t-Mad2 in control and Tpr-depleted cells. α-Tubulin was used as a loading control. *, P < 0.05; **, P < 0.01; ***, P < 0.001. The error bars indicate standard deviations from two independent experiments. (G) Immunodetection of Mad1 (red), SENP1, and SENP2 (green) in Tpr-depleted cells (−). A nondepleted cell (+) was used as internal control. DNA was counterstained with DAPI (blue). (H) WB analysis of asynchronous cell extracts in control and after SENP1 or SENP2 RNAi. The percentage of protein levels relative to controls is indicated. α-Tubulin was used as a loading control. Bar, 10 µm.

Journal: The Journal of Cell Biology

Article Title: Spindle assembly checkpoint robustness requires Tpr-mediated regulation of Mad1/Mad2 proteostasis

doi: 10.1083/jcb.201309076

Figure Lengend Snippet: Tpr is required for SAC proteostasis throughout the cell cycle. (A and B) Normalized expression of tpr , mad1 , mad2 , mps1 , cdc20 , and p31 in control and Tpr-depleted asynchronous or mitotic cells. Error bars represent standard deviations from three independent experiments. (C) WB analysis of asynchronous, G2, and mitotic enriched HeLa cell extracts from control (+) and Tpr-depleted (−) cells with (+) or without (−) MG132 with the indicated antibodies. The percentage of protein levels relative to controls is indicated. (D) c-Mad2 IP from asynchronous and mitotic HeLa cells with (+) or without (−) Tpr, in the presence (+) or absence (−) of MG132. (E and F) Cells with or without Tpr were treated with cycloheximide (CHX) for various time points as indicated. Total protein extracts of asynchronous HeLa cells were analyzed by WB to detect Tpr, Mps1, Mad1, and t-Mad2 in control and Tpr-depleted cells. α-Tubulin was used as a loading control. *, P < 0.05; **, P < 0.01; ***, P < 0.001. The error bars indicate standard deviations from two independent experiments. (G) Immunodetection of Mad1 (red), SENP1, and SENP2 (green) in Tpr-depleted cells (−). A nondepleted cell (+) was used as internal control. DNA was counterstained with DAPI (blue). (H) WB analysis of asynchronous cell extracts in control and after SENP1 or SENP2 RNAi. The percentage of protein levels relative to controls is indicated. α-Tubulin was used as a loading control. Bar, 10 µm.

Article Snippet: Mouse anti-Mad1 (generated against full-length Mad1, 1:500; provided by A. Santamaria and E. Nigg, Biozentrum, Basel, Switzerland), rabbit anti-Mad1 (generated against full-length Mad1, 1:1,000; provided by P. Meraldi, University of Geneva, Switzerland), mouse anti–c-Mad2 (generated against full-length Mad2, 1:500; provided by A. Santamaria), rabbit anti–t-Mad2 (1:300; Bethyl Laboratories, Inc.), sheep anti–o-Mad2 (generated against full-length Mad2, 1:200; provided by S. Taylor, University of Manchester, UK), rabbit anti-Cdc20 (1:100; Santa Cruz Biotechnology, Inc.), mouse anti-Mps1 (1:100; Merck Millipore), rabbit anti-Tpr (1:500; Novus Biologicals), sheep anti-BubR1 (generated against aa 2–422, 1:300; provided by S. Taylor), rabbit anti-SENP1 or -SENP2 (generated against aa 273–449 and aa 1–92, respectively; 1:1,000; provided by M. Dasso, National Institutes of Health, Bethesda, MD), and human anticentromere antibodies (ACAs; 1:5,000, provided by B. Earnshaw; or 1:2,000, Fitzgerald Industries International) were used as primary antibodies, and Alexa Fluor 488, 568, and 647 (Invitrogen) were used as secondary antibodies (1:1,000).

Techniques: Expressing, Control, Immunodetection