mouse anti cora Search Results


mouse monoclonal anti-rat iga (mara-2  (Accurate Chemical & Scientific Corporation)
90
Accurate Chemical & Scientific Corporation mouse monoclonal anti-rat iga (mara-2
Mouse Monoclonal Anti Rat Iga (Mara 2, supplied by Accurate Chemical & Scientific Corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/mouse+anti+cora/pmc02493197-101-39-45?v=Accurate+Chemical+%26+Scientific+Corporation
Average 90 stars, based on 1 article reviews
mouse monoclonal anti-rat iga (mara-2 - by Bioz Stars, 2026-08
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lin54  (Bethyl)
93
Bethyl lin54
(A) A diagram showing in which organ a particular component of the DREAM complex was identified as a cyclin E1-interacting protein by our mass spectrometric analyses. The number of organs in which a given protein was found to associate with cyclin E1 is depicted by the color. (B) Association of cyclin E1 with components of the DREAM complex in the spleens of tagged knock-in mice (KI) was verified by immunoprecipitating (IP) cyclin E1 with anti-Flag antibody followed by immunoblotting with the indicated antibodies. (C) IP followed by re-IP-immunoblotting to demonstrate that cyclin E1, Cdk2 and the DREAM complex components are present within the same multi-protein complex. Cyclin E1 was immunoprecipitated from spleens of KI mice using anti-Flag antibody, protein complexes were eluted with Flag peptides, re-immunoprecipitated with IgG (control) or with anti-p130 antibody, and then immunoblotted with the indicated antibodies. (D) T98G cells were serum starved for 72 hrs (0% FBS). Subsequently, cells were stimulated to re-enter the cell cycle by addition of 20% FBS supplemented with either 0.2% DMSO (control, left two panels) or 20 μM CVT-313 (right two panels), and harvested at the indicated time-points. Cell extracts (whole) as well as anti-Lin37 immunoprecipitates were resolved on 4–15% gradient SDS-PAGE gels and probed with indicated antibodies. Gapdh serves as a loading control. (E) Cyclin E1-Cdk2 kinase can phosphorylate purified recombinant Lin proteins in vitro. Lin9, Lin52 and <t>Lin54</t> were expressed as GST-fusion proteins in E . Coli , purified and subjected to in vitro kinase reactions with the recombinant cyclin E1-Cdk2 in the presence of [γ 32 P]ATP. Recombinant histone H1 was used as a positive control and GST as a negative control. (F) A diagram illustrating amino acid residues in human Lin proteins that were phosphorylated by cyclin E-Cdk2. (G) Wild-type Cdk2 (K2WT) or analog-sensitive Cdk2 (K2AS) were transfected into 293T cells together with cyclin E1 and Flag-tagged Lin37 or vector control. After supplementing cells with 6-Fu-ATPγS, labeling of Lin37 was evaluated by immunoprecipitating Lin37 with an anti-Flag antibody followed by immunoblotting with anti-thiophosphate ester antibody. A blue arrowhead indicates 6-Fu-ATPγS-labeled Lin37.
Lin54, supplied by Bethyl, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/mouse+anti+cora/pmc05102403-260-58-61?v=Bethyl
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lin54 - by Bioz Stars, 2026-08
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rabbit h2ax  (Bethyl)
93
Bethyl rabbit h2ax
Figure 4. BLM and EXO1 promote DNA DSB resection and associated events in human cells. (A) BLM and EXO1 deficiency impairs Camp- tothecin-induced RPA focus formation. U2OS cells were transfected with siRNAs directed against Luciferase (siCNTL), CtIP, BLM, EXO1, or a combination of BLM and EXO1, then 72 h later were mock-treated or treated with 1 µM Camptothecin for 1 h. Cells were next detergent- extracted and fixed, then foci for phosphorylated histone <t>H2AX</t> (H2AX) and RPA2 were visualized by indirect immunofluorescence. More than 100 cells were counted for each sample and the percentages of cells exhibiting both H2AX and RPA foci was determined. Data represent the mean ± SEM from three independent experiments. All counting was done blind. (B) BLM and EXO1 promote DSB signaling. Extracts of mock-treated or Camptothecin-treated cells depleted for the indicated factors were analyzed by Western blotting with the indicated antibodies. Endogenous EXO1 levels were too low to allow detection with anti-EXO1 antisera and so verification of EXO1 siRNA depletion was done with cells stably expressing a GFP-Exo1 construct (see Supplemental Fig. S4). (C) RPA Ser-4 and Ser-8 phosphorylation (RPApS4/S8) is compromised by BLM and EXO1 depletion. CtIP, BLM, or EXO1 were depleted and cells were treated as in A, followed by analysis by indirect immunoflu- orescence with the indicated antibodies. More than 100 cells were counted for each sample, and data represent the mean ± SEM from three independent experiments. Counting was done blind. (D) Codepletion or BLM and EXO1 yields Camptothecin hypersensitivity. Seventy-two hours following transfection with the indicated siRNAs, U2OS cells were treated with Camptothecin for 1 h, and cell survival was determined by colony formation. Data represent the mean ± SEM from three independent experiments.
Rabbit H2ax, supplied by Bethyl, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/mouse+anti+cora/pm18923075-126-30-29?v=Bethyl
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rabbit h2ax - by Bioz Stars, 2026-08
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rat anti-mouse syndecan-4 igg  (Becton Dickinson)
90
Becton Dickinson rat anti-mouse syndecan-4 igg
Figure 4. BLM and EXO1 promote DNA DSB resection and associated events in human cells. (A) BLM and EXO1 deficiency impairs Camp- tothecin-induced RPA focus formation. U2OS cells were transfected with siRNAs directed against Luciferase (siCNTL), CtIP, BLM, EXO1, or a combination of BLM and EXO1, then 72 h later were mock-treated or treated with 1 µM Camptothecin for 1 h. Cells were next detergent- extracted and fixed, then foci for phosphorylated histone <t>H2AX</t> (H2AX) and RPA2 were visualized by indirect immunofluorescence. More than 100 cells were counted for each sample and the percentages of cells exhibiting both H2AX and RPA foci was determined. Data represent the mean ± SEM from three independent experiments. All counting was done blind. (B) BLM and EXO1 promote DSB signaling. Extracts of mock-treated or Camptothecin-treated cells depleted for the indicated factors were analyzed by Western blotting with the indicated antibodies. Endogenous EXO1 levels were too low to allow detection with anti-EXO1 antisera and so verification of EXO1 siRNA depletion was done with cells stably expressing a GFP-Exo1 construct (see Supplemental Fig. S4). (C) RPA Ser-4 and Ser-8 phosphorylation (RPApS4/S8) is compromised by BLM and EXO1 depletion. CtIP, BLM, or EXO1 were depleted and cells were treated as in A, followed by analysis by indirect immunoflu- orescence with the indicated antibodies. More than 100 cells were counted for each sample, and data represent the mean ± SEM from three independent experiments. Counting was done blind. (D) Codepletion or BLM and EXO1 yields Camptothecin hypersensitivity. Seventy-two hours following transfection with the indicated siRNAs, U2OS cells were treated with Camptothecin for 1 h, and cell survival was determined by colony formation. Data represent the mean ± SEM from three independent experiments.
Rat Anti Mouse Syndecan 4 Igg, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/mouse+anti+cora/pmc02656657-167-34-38?v=Becton+Dickinson
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rat anti-mouse syndecan-4 igg - by Bioz Stars, 2026-08
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mouse anti his antibody  (Aviva Systems)
92
Aviva Systems mouse anti his antibody
Figure 4. BLM and EXO1 promote DNA DSB resection and associated events in human cells. (A) BLM and EXO1 deficiency impairs Camp- tothecin-induced RPA focus formation. U2OS cells were transfected with siRNAs directed against Luciferase (siCNTL), CtIP, BLM, EXO1, or a combination of BLM and EXO1, then 72 h later were mock-treated or treated with 1 µM Camptothecin for 1 h. Cells were next detergent- extracted and fixed, then foci for phosphorylated histone <t>H2AX</t> (H2AX) and RPA2 were visualized by indirect immunofluorescence. More than 100 cells were counted for each sample and the percentages of cells exhibiting both H2AX and RPA foci was determined. Data represent the mean ± SEM from three independent experiments. All counting was done blind. (B) BLM and EXO1 promote DSB signaling. Extracts of mock-treated or Camptothecin-treated cells depleted for the indicated factors were analyzed by Western blotting with the indicated antibodies. Endogenous EXO1 levels were too low to allow detection with anti-EXO1 antisera and so verification of EXO1 siRNA depletion was done with cells stably expressing a GFP-Exo1 construct (see Supplemental Fig. S4). (C) RPA Ser-4 and Ser-8 phosphorylation (RPApS4/S8) is compromised by BLM and EXO1 depletion. CtIP, BLM, or EXO1 were depleted and cells were treated as in A, followed by analysis by indirect immunoflu- orescence with the indicated antibodies. More than 100 cells were counted for each sample, and data represent the mean ± SEM from three independent experiments. Counting was done blind. (D) Codepletion or BLM and EXO1 yields Camptothecin hypersensitivity. Seventy-two hours following transfection with the indicated siRNAs, U2OS cells were treated with Camptothecin for 1 h, and cell survival was determined by colony formation. Data represent the mean ± SEM from three independent experiments.
Mouse Anti His Antibody, supplied by Aviva Systems, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/mouse+anti+cora/pmc08211017-185-7-10?v=Aviva+Systems
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mouse anti his antibody - by Bioz Stars, 2026-08
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rabbit anti fgl2  (Aviva Systems)
86
Aviva Systems rabbit anti fgl2
Figure 4. BLM and EXO1 promote DNA DSB resection and associated events in human cells. (A) BLM and EXO1 deficiency impairs Camp- tothecin-induced RPA focus formation. U2OS cells were transfected with siRNAs directed against Luciferase (siCNTL), CtIP, BLM, EXO1, or a combination of BLM and EXO1, then 72 h later were mock-treated or treated with 1 µM Camptothecin for 1 h. Cells were next detergent- extracted and fixed, then foci for phosphorylated histone <t>H2AX</t> (H2AX) and RPA2 were visualized by indirect immunofluorescence. More than 100 cells were counted for each sample and the percentages of cells exhibiting both H2AX and RPA foci was determined. Data represent the mean ± SEM from three independent experiments. All counting was done blind. (B) BLM and EXO1 promote DSB signaling. Extracts of mock-treated or Camptothecin-treated cells depleted for the indicated factors were analyzed by Western blotting with the indicated antibodies. Endogenous EXO1 levels were too low to allow detection with anti-EXO1 antisera and so verification of EXO1 siRNA depletion was done with cells stably expressing a GFP-Exo1 construct (see Supplemental Fig. S4). (C) RPA Ser-4 and Ser-8 phosphorylation (RPApS4/S8) is compromised by BLM and EXO1 depletion. CtIP, BLM, or EXO1 were depleted and cells were treated as in A, followed by analysis by indirect immunoflu- orescence with the indicated antibodies. More than 100 cells were counted for each sample, and data represent the mean ± SEM from three independent experiments. Counting was done blind. (D) Codepletion or BLM and EXO1 yields Camptothecin hypersensitivity. Seventy-two hours following transfection with the indicated siRNAs, U2OS cells were treated with Camptothecin for 1 h, and cell survival was determined by colony formation. Data represent the mean ± SEM from three independent experiments.
Rabbit Anti Fgl2, supplied by Aviva Systems, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/mouse+anti+cora/pmc05336537-56-9-11?v=Aviva+Systems
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rabbit anti fgl2 - by Bioz Stars, 2026-08
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gfap  (Boster Bio)
94
Boster Bio gfap
Figure 4. BLM and EXO1 promote DNA DSB resection and associated events in human cells. (A) BLM and EXO1 deficiency impairs Camp- tothecin-induced RPA focus formation. U2OS cells were transfected with siRNAs directed against Luciferase (siCNTL), CtIP, BLM, EXO1, or a combination of BLM and EXO1, then 72 h later were mock-treated or treated with 1 µM Camptothecin for 1 h. Cells were next detergent- extracted and fixed, then foci for phosphorylated histone <t>H2AX</t> (H2AX) and RPA2 were visualized by indirect immunofluorescence. More than 100 cells were counted for each sample and the percentages of cells exhibiting both H2AX and RPA foci was determined. Data represent the mean ± SEM from three independent experiments. All counting was done blind. (B) BLM and EXO1 promote DSB signaling. Extracts of mock-treated or Camptothecin-treated cells depleted for the indicated factors were analyzed by Western blotting with the indicated antibodies. Endogenous EXO1 levels were too low to allow detection with anti-EXO1 antisera and so verification of EXO1 siRNA depletion was done with cells stably expressing a GFP-Exo1 construct (see Supplemental Fig. S4). (C) RPA Ser-4 and Ser-8 phosphorylation (RPApS4/S8) is compromised by BLM and EXO1 depletion. CtIP, BLM, or EXO1 were depleted and cells were treated as in A, followed by analysis by indirect immunoflu- orescence with the indicated antibodies. More than 100 cells were counted for each sample, and data represent the mean ± SEM from three independent experiments. Counting was done blind. (D) Codepletion or BLM and EXO1 yields Camptothecin hypersensitivity. Seventy-two hours following transfection with the indicated siRNAs, U2OS cells were treated with Camptothecin for 1 h, and cell survival was determined by colony formation. Data represent the mean ± SEM from three independent experiments.
Gfap, supplied by Boster Bio, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/mouse+anti+cora/pmc04528219-52-9-12?v=Boster+Bio
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gfap - by Bioz Stars, 2026-08
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mouse monoclonal antibody against hcv core protein  (Danaher Inc)
99
Danaher Inc mouse monoclonal antibody against hcv core protein
Figure 4. BLM and EXO1 promote DNA DSB resection and associated events in human cells. (A) BLM and EXO1 deficiency impairs Camp- tothecin-induced RPA focus formation. U2OS cells were transfected with siRNAs directed against Luciferase (siCNTL), CtIP, BLM, EXO1, or a combination of BLM and EXO1, then 72 h later were mock-treated or treated with 1 µM Camptothecin for 1 h. Cells were next detergent- extracted and fixed, then foci for phosphorylated histone <t>H2AX</t> (H2AX) and RPA2 were visualized by indirect immunofluorescence. More than 100 cells were counted for each sample and the percentages of cells exhibiting both H2AX and RPA foci was determined. Data represent the mean ± SEM from three independent experiments. All counting was done blind. (B) BLM and EXO1 promote DSB signaling. Extracts of mock-treated or Camptothecin-treated cells depleted for the indicated factors were analyzed by Western blotting with the indicated antibodies. Endogenous EXO1 levels were too low to allow detection with anti-EXO1 antisera and so verification of EXO1 siRNA depletion was done with cells stably expressing a GFP-Exo1 construct (see Supplemental Fig. S4). (C) RPA Ser-4 and Ser-8 phosphorylation (RPApS4/S8) is compromised by BLM and EXO1 depletion. CtIP, BLM, or EXO1 were depleted and cells were treated as in A, followed by analysis by indirect immunoflu- orescence with the indicated antibodies. More than 100 cells were counted for each sample, and data represent the mean ± SEM from three independent experiments. Counting was done blind. (D) Codepletion or BLM and EXO1 yields Camptothecin hypersensitivity. Seventy-two hours following transfection with the indicated siRNAs, U2OS cells were treated with Camptothecin for 1 h, and cell survival was determined by colony formation. Data represent the mean ± SEM from three independent experiments.
Mouse Monoclonal Antibody Against Hcv Core Protein, supplied by Danaher Inc, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/mouse+anti+cora/pmc02573220-166-9-17?v=Danaher+Inc
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mouse monoclonal antibody against hcv core protein - by Bioz Stars, 2026-08
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mab mouse macrophages (moma-2  (Accurate Chemical & Scientific Corporation)
90
Accurate Chemical & Scientific Corporation mab mouse macrophages (moma-2
Figure 4. BLM and EXO1 promote DNA DSB resection and associated events in human cells. (A) BLM and EXO1 deficiency impairs Camp- tothecin-induced RPA focus formation. U2OS cells were transfected with siRNAs directed against Luciferase (siCNTL), CtIP, BLM, EXO1, or a combination of BLM and EXO1, then 72 h later were mock-treated or treated with 1 µM Camptothecin for 1 h. Cells were next detergent- extracted and fixed, then foci for phosphorylated histone <t>H2AX</t> (H2AX) and RPA2 were visualized by indirect immunofluorescence. More than 100 cells were counted for each sample and the percentages of cells exhibiting both H2AX and RPA foci was determined. Data represent the mean ± SEM from three independent experiments. All counting was done blind. (B) BLM and EXO1 promote DSB signaling. Extracts of mock-treated or Camptothecin-treated cells depleted for the indicated factors were analyzed by Western blotting with the indicated antibodies. Endogenous EXO1 levels were too low to allow detection with anti-EXO1 antisera and so verification of EXO1 siRNA depletion was done with cells stably expressing a GFP-Exo1 construct (see Supplemental Fig. S4). (C) RPA Ser-4 and Ser-8 phosphorylation (RPApS4/S8) is compromised by BLM and EXO1 depletion. CtIP, BLM, or EXO1 were depleted and cells were treated as in A, followed by analysis by indirect immunoflu- orescence with the indicated antibodies. More than 100 cells were counted for each sample, and data represent the mean ± SEM from three independent experiments. Counting was done blind. (D) Codepletion or BLM and EXO1 yields Camptothecin hypersensitivity. Seventy-two hours following transfection with the indicated siRNAs, U2OS cells were treated with Camptothecin for 1 h, and cell survival was determined by colony formation. Data represent the mean ± SEM from three independent experiments.
Mab Mouse Macrophages (Moma 2, supplied by Accurate Chemical & Scientific Corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/mouse+anti+cora/pm12208806-60-44-47?v=Accurate+Chemical+%26+Scientific+Corporation
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mab mouse macrophages (moma-2 - by Bioz Stars, 2026-08
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foxp3 mouse monoclonal abcam  (Danaher Inc)
99
Danaher Inc foxp3 mouse monoclonal abcam
Figure 4. BLM and EXO1 promote DNA DSB resection and associated events in human cells. (A) BLM and EXO1 deficiency impairs Camp- tothecin-induced RPA focus formation. U2OS cells were transfected with siRNAs directed against Luciferase (siCNTL), CtIP, BLM, EXO1, or a combination of BLM and EXO1, then 72 h later were mock-treated or treated with 1 µM Camptothecin for 1 h. Cells were next detergent- extracted and fixed, then foci for phosphorylated histone <t>H2AX</t> (H2AX) and RPA2 were visualized by indirect immunofluorescence. More than 100 cells were counted for each sample and the percentages of cells exhibiting both H2AX and RPA foci was determined. Data represent the mean ± SEM from three independent experiments. All counting was done blind. (B) BLM and EXO1 promote DSB signaling. Extracts of mock-treated or Camptothecin-treated cells depleted for the indicated factors were analyzed by Western blotting with the indicated antibodies. Endogenous EXO1 levels were too low to allow detection with anti-EXO1 antisera and so verification of EXO1 siRNA depletion was done with cells stably expressing a GFP-Exo1 construct (see Supplemental Fig. S4). (C) RPA Ser-4 and Ser-8 phosphorylation (RPApS4/S8) is compromised by BLM and EXO1 depletion. CtIP, BLM, or EXO1 were depleted and cells were treated as in A, followed by analysis by indirect immunoflu- orescence with the indicated antibodies. More than 100 cells were counted for each sample, and data represent the mean ± SEM from three independent experiments. Counting was done blind. (D) Codepletion or BLM and EXO1 yields Camptothecin hypersensitivity. Seventy-two hours following transfection with the indicated siRNAs, U2OS cells were treated with Camptothecin for 1 h, and cell survival was determined by colony formation. Data represent the mean ± SEM from three independent experiments.
Foxp3 Mouse Monoclonal Abcam, supplied by Danaher Inc, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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foxp3 mouse monoclonal abcam - by Bioz Stars, 2026-08
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anti-human apo a-i mouse igg  (Abnova)
90
Abnova anti-human apo a-i mouse igg
Figure 4. BLM and EXO1 promote DNA DSB resection and associated events in human cells. (A) BLM and EXO1 deficiency impairs Camp- tothecin-induced RPA focus formation. U2OS cells were transfected with siRNAs directed against Luciferase (siCNTL), CtIP, BLM, EXO1, or a combination of BLM and EXO1, then 72 h later were mock-treated or treated with 1 µM Camptothecin for 1 h. Cells were next detergent- extracted and fixed, then foci for phosphorylated histone <t>H2AX</t> (H2AX) and RPA2 were visualized by indirect immunofluorescence. More than 100 cells were counted for each sample and the percentages of cells exhibiting both H2AX and RPA foci was determined. Data represent the mean ± SEM from three independent experiments. All counting was done blind. (B) BLM and EXO1 promote DSB signaling. Extracts of mock-treated or Camptothecin-treated cells depleted for the indicated factors were analyzed by Western blotting with the indicated antibodies. Endogenous EXO1 levels were too low to allow detection with anti-EXO1 antisera and so verification of EXO1 siRNA depletion was done with cells stably expressing a GFP-Exo1 construct (see Supplemental Fig. S4). (C) RPA Ser-4 and Ser-8 phosphorylation (RPApS4/S8) is compromised by BLM and EXO1 depletion. CtIP, BLM, or EXO1 were depleted and cells were treated as in A, followed by analysis by indirect immunoflu- orescence with the indicated antibodies. More than 100 cells were counted for each sample, and data represent the mean ± SEM from three independent experiments. Counting was done blind. (D) Codepletion or BLM and EXO1 yields Camptothecin hypersensitivity. Seventy-two hours following transfection with the indicated siRNAs, U2OS cells were treated with Camptothecin for 1 h, and cell survival was determined by colony formation. Data represent the mean ± SEM from three independent experiments.
Anti Human Apo A I Mouse Igg, supplied by Abnova, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/mouse+anti+cora/pmc08265427-68-15-20?v=Abnova
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anti-human apo a-i mouse igg - by Bioz Stars, 2026-08
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mouse anti-human serglycin monoclonal antibody  (Abnova)
90
Abnova mouse anti-human serglycin monoclonal antibody
Figure 4. BLM and EXO1 promote DNA DSB resection and associated events in human cells. (A) BLM and EXO1 deficiency impairs Camp- tothecin-induced RPA focus formation. U2OS cells were transfected with siRNAs directed against Luciferase (siCNTL), CtIP, BLM, EXO1, or a combination of BLM and EXO1, then 72 h later were mock-treated or treated with 1 µM Camptothecin for 1 h. Cells were next detergent- extracted and fixed, then foci for phosphorylated histone <t>H2AX</t> (H2AX) and RPA2 were visualized by indirect immunofluorescence. More than 100 cells were counted for each sample and the percentages of cells exhibiting both H2AX and RPA foci was determined. Data represent the mean ± SEM from three independent experiments. All counting was done blind. (B) BLM and EXO1 promote DSB signaling. Extracts of mock-treated or Camptothecin-treated cells depleted for the indicated factors were analyzed by Western blotting with the indicated antibodies. Endogenous EXO1 levels were too low to allow detection with anti-EXO1 antisera and so verification of EXO1 siRNA depletion was done with cells stably expressing a GFP-Exo1 construct (see Supplemental Fig. S4). (C) RPA Ser-4 and Ser-8 phosphorylation (RPApS4/S8) is compromised by BLM and EXO1 depletion. CtIP, BLM, or EXO1 were depleted and cells were treated as in A, followed by analysis by indirect immunoflu- orescence with the indicated antibodies. More than 100 cells were counted for each sample, and data represent the mean ± SEM from three independent experiments. Counting was done blind. (D) Codepletion or BLM and EXO1 yields Camptothecin hypersensitivity. Seventy-two hours following transfection with the indicated siRNAs, U2OS cells were treated with Camptothecin for 1 h, and cell survival was determined by colony formation. Data represent the mean ± SEM from three independent experiments.
Mouse Anti Human Serglycin Monoclonal Antibody, supplied by Abnova, 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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mouse anti-human serglycin monoclonal antibody - by Bioz Stars, 2026-08
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Image Search Results


(A) A diagram showing in which organ a particular component of the DREAM complex was identified as a cyclin E1-interacting protein by our mass spectrometric analyses. The number of organs in which a given protein was found to associate with cyclin E1 is depicted by the color. (B) Association of cyclin E1 with components of the DREAM complex in the spleens of tagged knock-in mice (KI) was verified by immunoprecipitating (IP) cyclin E1 with anti-Flag antibody followed by immunoblotting with the indicated antibodies. (C) IP followed by re-IP-immunoblotting to demonstrate that cyclin E1, Cdk2 and the DREAM complex components are present within the same multi-protein complex. Cyclin E1 was immunoprecipitated from spleens of KI mice using anti-Flag antibody, protein complexes were eluted with Flag peptides, re-immunoprecipitated with IgG (control) or with anti-p130 antibody, and then immunoblotted with the indicated antibodies. (D) T98G cells were serum starved for 72 hrs (0% FBS). Subsequently, cells were stimulated to re-enter the cell cycle by addition of 20% FBS supplemented with either 0.2% DMSO (control, left two panels) or 20 μM CVT-313 (right two panels), and harvested at the indicated time-points. Cell extracts (whole) as well as anti-Lin37 immunoprecipitates were resolved on 4–15% gradient SDS-PAGE gels and probed with indicated antibodies. Gapdh serves as a loading control. (E) Cyclin E1-Cdk2 kinase can phosphorylate purified recombinant Lin proteins in vitro. Lin9, Lin52 and Lin54 were expressed as GST-fusion proteins in E . Coli , purified and subjected to in vitro kinase reactions with the recombinant cyclin E1-Cdk2 in the presence of [γ 32 P]ATP. Recombinant histone H1 was used as a positive control and GST as a negative control. (F) A diagram illustrating amino acid residues in human Lin proteins that were phosphorylated by cyclin E-Cdk2. (G) Wild-type Cdk2 (K2WT) or analog-sensitive Cdk2 (K2AS) were transfected into 293T cells together with cyclin E1 and Flag-tagged Lin37 or vector control. After supplementing cells with 6-Fu-ATPγS, labeling of Lin37 was evaluated by immunoprecipitating Lin37 with an anti-Flag antibody followed by immunoblotting with anti-thiophosphate ester antibody. A blue arrowhead indicates 6-Fu-ATPγS-labeled Lin37.

Journal: PLoS Genetics

Article Title: Proteomic Landscape of Tissue-Specific Cyclin E Functions in Vivo

doi: 10.1371/journal.pgen.1006429

Figure Lengend Snippet: (A) A diagram showing in which organ a particular component of the DREAM complex was identified as a cyclin E1-interacting protein by our mass spectrometric analyses. The number of organs in which a given protein was found to associate with cyclin E1 is depicted by the color. (B) Association of cyclin E1 with components of the DREAM complex in the spleens of tagged knock-in mice (KI) was verified by immunoprecipitating (IP) cyclin E1 with anti-Flag antibody followed by immunoblotting with the indicated antibodies. (C) IP followed by re-IP-immunoblotting to demonstrate that cyclin E1, Cdk2 and the DREAM complex components are present within the same multi-protein complex. Cyclin E1 was immunoprecipitated from spleens of KI mice using anti-Flag antibody, protein complexes were eluted with Flag peptides, re-immunoprecipitated with IgG (control) or with anti-p130 antibody, and then immunoblotted with the indicated antibodies. (D) T98G cells were serum starved for 72 hrs (0% FBS). Subsequently, cells were stimulated to re-enter the cell cycle by addition of 20% FBS supplemented with either 0.2% DMSO (control, left two panels) or 20 μM CVT-313 (right two panels), and harvested at the indicated time-points. Cell extracts (whole) as well as anti-Lin37 immunoprecipitates were resolved on 4–15% gradient SDS-PAGE gels and probed with indicated antibodies. Gapdh serves as a loading control. (E) Cyclin E1-Cdk2 kinase can phosphorylate purified recombinant Lin proteins in vitro. Lin9, Lin52 and Lin54 were expressed as GST-fusion proteins in E . Coli , purified and subjected to in vitro kinase reactions with the recombinant cyclin E1-Cdk2 in the presence of [γ 32 P]ATP. Recombinant histone H1 was used as a positive control and GST as a negative control. (F) A diagram illustrating amino acid residues in human Lin proteins that were phosphorylated by cyclin E-Cdk2. (G) Wild-type Cdk2 (K2WT) or analog-sensitive Cdk2 (K2AS) were transfected into 293T cells together with cyclin E1 and Flag-tagged Lin37 or vector control. After supplementing cells with 6-Fu-ATPγS, labeling of Lin37 was evaluated by immunoprecipitating Lin37 with an anti-Flag antibody followed by immunoblotting with anti-thiophosphate ester antibody. A blue arrowhead indicates 6-Fu-ATPγS-labeled Lin37.

Article Snippet: For immunoblotting, immunoprecipitation and immunostaining, we used antibodies against cyclin E1 (Santa Cruz, BioLegend or Millipore), cyclin D1, cyclin D3, cyclin B1, Cdk1, Cdk2, Cdk4, Cdk5, p107, Pcna, B-Myb, , Rbbp9 (Santa Cruz), p130 (Santa Cruz or BD Transduction Labs or Bethyl Laboratories), HA (Covance), actin, Flag, Mybl1, cyclin A2 (Sigma), Gapdh (Invitrogen or Millipore), Lin9, Lin37, Lin52, Lin54, Rbbp4, Rbbp7 (Bethyl Laboratories), E2f4, Dp1, Cdc7 (Lab Vision), thiophosphate ester, Dmrtc2 (Abcam or Sigma), Mapk15 (Abcam), RalA, mTOR/Frap1, cyclin B3, phosphor-Rb, Tubulin and Miwi (Cell Signaling).

Techniques: Knock-In, Western Blot, Immunoprecipitation, Control, SDS Page, Purification, Recombinant, In Vitro, Positive Control, Negative Control, Transfection, Plasmid Preparation, Labeling

Figure 4. BLM and EXO1 promote DNA DSB resection and associated events in human cells. (A) BLM and EXO1 deficiency impairs Camp- tothecin-induced RPA focus formation. U2OS cells were transfected with siRNAs directed against Luciferase (siCNTL), CtIP, BLM, EXO1, or a combination of BLM and EXO1, then 72 h later were mock-treated or treated with 1 µM Camptothecin for 1 h. Cells were next detergent- extracted and fixed, then foci for phosphorylated histone H2AX (H2AX) and RPA2 were visualized by indirect immunofluorescence. More than 100 cells were counted for each sample and the percentages of cells exhibiting both H2AX and RPA foci was determined. Data represent the mean ± SEM from three independent experiments. All counting was done blind. (B) BLM and EXO1 promote DSB signaling. Extracts of mock-treated or Camptothecin-treated cells depleted for the indicated factors were analyzed by Western blotting with the indicated antibodies. Endogenous EXO1 levels were too low to allow detection with anti-EXO1 antisera and so verification of EXO1 siRNA depletion was done with cells stably expressing a GFP-Exo1 construct (see Supplemental Fig. S4). (C) RPA Ser-4 and Ser-8 phosphorylation (RPApS4/S8) is compromised by BLM and EXO1 depletion. CtIP, BLM, or EXO1 were depleted and cells were treated as in A, followed by analysis by indirect immunoflu- orescence with the indicated antibodies. More than 100 cells were counted for each sample, and data represent the mean ± SEM from three independent experiments. Counting was done blind. (D) Codepletion or BLM and EXO1 yields Camptothecin hypersensitivity. Seventy-two hours following transfection with the indicated siRNAs, U2OS cells were treated with Camptothecin for 1 h, and cell survival was determined by colony formation. Data represent the mean ± SEM from three independent experiments.

Journal: Genes & development

Article Title: DNA helicases Sgs1 and BLM promote DNA double-strand break resection.

doi: 10.1101/gad.503108

Figure Lengend Snippet: Figure 4. BLM and EXO1 promote DNA DSB resection and associated events in human cells. (A) BLM and EXO1 deficiency impairs Camp- tothecin-induced RPA focus formation. U2OS cells were transfected with siRNAs directed against Luciferase (siCNTL), CtIP, BLM, EXO1, or a combination of BLM and EXO1, then 72 h later were mock-treated or treated with 1 µM Camptothecin for 1 h. Cells were next detergent- extracted and fixed, then foci for phosphorylated histone H2AX (H2AX) and RPA2 were visualized by indirect immunofluorescence. More than 100 cells were counted for each sample and the percentages of cells exhibiting both H2AX and RPA foci was determined. Data represent the mean ± SEM from three independent experiments. All counting was done blind. (B) BLM and EXO1 promote DSB signaling. Extracts of mock-treated or Camptothecin-treated cells depleted for the indicated factors were analyzed by Western blotting with the indicated antibodies. Endogenous EXO1 levels were too low to allow detection with anti-EXO1 antisera and so verification of EXO1 siRNA depletion was done with cells stably expressing a GFP-Exo1 construct (see Supplemental Fig. S4). (C) RPA Ser-4 and Ser-8 phosphorylation (RPApS4/S8) is compromised by BLM and EXO1 depletion. CtIP, BLM, or EXO1 were depleted and cells were treated as in A, followed by analysis by indirect immunoflu- orescence with the indicated antibodies. More than 100 cells were counted for each sample, and data represent the mean ± SEM from three independent experiments. Counting was done blind. (D) Codepletion or BLM and EXO1 yields Camptothecin hypersensitivity. Seventy-two hours following transfection with the indicated siRNAs, U2OS cells were treated with Camptothecin for 1 h, and cell survival was determined by colony formation. Data represent the mean ± SEM from three independent experiments.

Article Snippet: The antibodies used in this study were rabbit -Rad53 (a gift from Noel Lowndes), goat -BLM (C18, Santa Cruz Biotechnologies), mouse -RPA2 (Ab1, 9HD, Lab Vision), rabbit -RPA pS4/S8 (Bethyl), rabbit - H2AX (Cell Signaling), rabbit -Chk2 pT68 (Cell Signaling), rabbit -Chk2 (Abcam), rabbit -Chk1 pS345 mAb (133D3, Cell Signaling), mouse -Chk1 (G4, Santa Cruz Biotechnologies), and a mouse monoclonal antibody to CtIP (provided by R. Baer) (Yu and Baer 2000).

Techniques: Transfection, Luciferase, Immunofluorescence, Western Blot, Stable Transfection, Expressing, Construct, Phospho-proteomics