agr function Search Results


agr function  (Thermo Fisher)
99
Thermo Fisher agr function
Agr Function, supplied by Thermo Fisher, 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/agr+function/pmc03067101-96-9-38?v=Thermo+Fisher
Average 99 stars, based on 1 article reviews
agr function - by Bioz Stars, 2026-07
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brip1  (Santa Cruz Biotechnology)
93
Santa Cruz Biotechnology brip1
Figure 1. Sequence alterations generated in BRCA1 and their effects on protein-protein interactions and HR. (A) Domain structure of BRCA1 and the binding sites for its interacting partners. NES, nuclear export signal; NLS, nuclear localization signal. (B) Effects of the BRCA1 variants on the binding of BARD1, PALB2, <t>BRIP1</t> and Abraxas. The 3xMyc-tagged BRCA1 proteins were transiently expressed in 293T cells and IPed with an anti-Myc antibody. WCE, whole cell extract. (C) Schematic of the HR reporter assay. The DR-GFP reporter contains two defective copies of the GFP gene, one disrupted by an I-SceI site and the other lacking a promoter. I-SceI cutting of the first copy generates a DSB, and repair by HR with the second copy as a template leads to restoration of a functional GFP gene. (D) HR activities of the variants relative to the wt BRCA1 protein. Data shown are the means from two to seven independent experiments for each variant or mutant. Error bars represent standard deviations (SDs). The grey bars indicate variants that are among the top 20 missense variants but are already present in BRCA1 cDNAs obtained from three independent sources. The calculated cutoff threshold is indicated by horizontal lines. **p<0.01. See Figure 1—source data 1 for details. (E) Levels of BRCA1 protein following knockdown and re- expression. Cells treated with a control siRNA (NSC1) were used as a control for the endogenous protein abundance. DOI: 10.7554/eLife.21350.003 The following source data and figure supplements are available for figure 1:
Brip1, supplied by Santa Cruz Biotechnology, 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/agr+function/10__7554_slash_elife__21350-221-35-33?v=Santa+Cruz+Biotechnology
Average 93 stars, based on 1 article reviews
brip1 - by Bioz Stars, 2026-07
93/100 stars
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Figure 1. Sequence alterations generated in BRCA1 and their effects on protein-protein interactions and HR. (A) Domain structure of BRCA1 and the binding sites for its interacting partners. NES, nuclear export signal; NLS, nuclear localization signal. (B) Effects of the BRCA1 variants on the binding of BARD1, PALB2, BRIP1 and Abraxas. The 3xMyc-tagged BRCA1 proteins were transiently expressed in 293T cells and IPed with an anti-Myc antibody. WCE, whole cell extract. (C) Schematic of the HR reporter assay. The DR-GFP reporter contains two defective copies of the GFP gene, one disrupted by an I-SceI site and the other lacking a promoter. I-SceI cutting of the first copy generates a DSB, and repair by HR with the second copy as a template leads to restoration of a functional GFP gene. (D) HR activities of the variants relative to the wt BRCA1 protein. Data shown are the means from two to seven independent experiments for each variant or mutant. Error bars represent standard deviations (SDs). The grey bars indicate variants that are among the top 20 missense variants but are already present in BRCA1 cDNAs obtained from three independent sources. The calculated cutoff threshold is indicated by horizontal lines. **p<0.01. See Figure 1—source data 1 for details. (E) Levels of BRCA1 protein following knockdown and re- expression. Cells treated with a control siRNA (NSC1) were used as a control for the endogenous protein abundance. DOI: 10.7554/eLife.21350.003 The following source data and figure supplements are available for figure 1:

Journal: eLife

Article Title: Functional and mutational landscapes of BRCA1 for homology-directed repair and therapy resistance

doi: 10.7554/elife.21350

Figure Lengend Snippet: Figure 1. Sequence alterations generated in BRCA1 and their effects on protein-protein interactions and HR. (A) Domain structure of BRCA1 and the binding sites for its interacting partners. NES, nuclear export signal; NLS, nuclear localization signal. (B) Effects of the BRCA1 variants on the binding of BARD1, PALB2, BRIP1 and Abraxas. The 3xMyc-tagged BRCA1 proteins were transiently expressed in 293T cells and IPed with an anti-Myc antibody. WCE, whole cell extract. (C) Schematic of the HR reporter assay. The DR-GFP reporter contains two defective copies of the GFP gene, one disrupted by an I-SceI site and the other lacking a promoter. I-SceI cutting of the first copy generates a DSB, and repair by HR with the second copy as a template leads to restoration of a functional GFP gene. (D) HR activities of the variants relative to the wt BRCA1 protein. Data shown are the means from two to seven independent experiments for each variant or mutant. Error bars represent standard deviations (SDs). The grey bars indicate variants that are among the top 20 missense variants but are already present in BRCA1 cDNAs obtained from three independent sources. The calculated cutoff threshold is indicated by horizontal lines. **p<0.01. See Figure 1—source data 1 for details. (E) Levels of BRCA1 protein following knockdown and re- expression. Cells treated with a control siRNA (NSC1) were used as a control for the endogenous protein abundance. DOI: 10.7554/eLife.21350.003 The following source data and figure supplements are available for figure 1:

Article Snippet: For western blotting analyses, proteins were resolved on 4–12% Tris-Glycine SDS gels, transferred onto nitrocellulose membranes and probed with the following antibodies- Myc (9E10, Covance), PALB2 (M11) (Xia et al., 2006), BARD1 (H300, Santa Cruz), BRIP1 (a gift from Dr. Sharon Cantor, University of Massachusetts Medical School), Abraxas (ab139191, AbCam).

Techniques: Sequencing, Generated, Protein-Protein interactions, Binding Assay, Reporter Assay, Functional Assay, Variant Assay, Mutagenesis, Knockdown, Expressing, Control, Quantitative Proteomics