braf f 7 Search Results


braf f 7  (Santa Cruz Biotechnology)
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Figure 3. Structure-based model predictions: ARAF isoform upregulation results in the increase in the range of paradoxical activation. (A) Schematic overview of the processes described in the model. (B–D) Dependence of ERK signaling on the ARAF abundance for cells expressing mutant RAS ([RAS–GTP] = 250 nM). ARAF abundance was set to 50 nM (black) and 200 nM (sky blue). For both conditions, <t>BRAF</t> and CRAF abundances were set to 50 nM. Dashed horizontal lines indicate basal ppERK levels for each condition. Vertical dashed lines denote inhibitor concentrations at which dose response curves drop below their basal levels. The model predicts stationary responses of ERK signaling to the Type II RAF inhibitor (B), Type I RAF inhibitor (C), and Type I 1
Braf F 7, supplied by Santa Cruz Biotechnology, 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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Figure 3. Structure-based model predictions: ARAF isoform upregulation results in the increase in the range of paradoxical activation. (A) Schematic overview of the processes described in the model. (B–D) Dependence of ERK signaling on the ARAF abundance for cells expressing mutant RAS ([RAS–GTP] = 250 nM). ARAF abundance was set to 50 nM (black) and 200 nM (sky blue). For both conditions, BRAF and CRAF abundances were set to 50 nM. Dashed horizontal lines indicate basal ppERK levels for each condition. Vertical dashed lines denote inhibitor concentrations at which dose response curves drop below their basal levels. The model predicts stationary responses of ERK signaling to the Type II RAF inhibitor (B), Type I RAF inhibitor (C), and Type I 1

Journal: Biomolecules

Article Title: A Combination of Conformation-Specific RAF Inhibitors Overcome Drug Resistance Brought about by RAF Overexpression.

doi: 10.3390/biom13081212

Figure Lengend Snippet: Figure 3. Structure-based model predictions: ARAF isoform upregulation results in the increase in the range of paradoxical activation. (A) Schematic overview of the processes described in the model. (B–D) Dependence of ERK signaling on the ARAF abundance for cells expressing mutant RAS ([RAS–GTP] = 250 nM). ARAF abundance was set to 50 nM (black) and 200 nM (sky blue). For both conditions, BRAF and CRAF abundances were set to 50 nM. Dashed horizontal lines indicate basal ppERK levels for each condition. Vertical dashed lines denote inhibitor concentrations at which dose response curves drop below their basal levels. The model predicts stationary responses of ERK signaling to the Type II RAF inhibitor (B), Type I RAF inhibitor (C), and Type I 1

Article Snippet: Protein visualization was performed by the iBrightTM CL750 Imaging System (InvitrogenTM, Thermo Fisher Scientific, Waltham, MA, USA), using horseradish peroxidase-conjugated secondary antibodies (#7074 resp. #7076, from Cell Signaling Technologies, Danvers, MA, USA), and the enhanced chemiluminescence system (GE Healthcare, Piscataway, NJ, USA) for the following antibodies: ARAF (D2P9P) (#75804); GAPDH (14C10) (#2118), both from Cell Signaling Technologies, Danvers, MA, USA; BRAF (F-7) (# sc-5284); CRAF/RAF1 (C-12) (# sc-133), both from Santa Cruz Biotechnology, Inc., Dallas, TX, USA, 75220; and polyclonal rabbit anti-human mitogen-activated protein (MAP) kinase [extra-cellular signalregulated kinase (ERK) 1 & 2] antibody (#M5670), monoclonal mouse anti-human MAP kinase, activated (diphosphorylated ERK-1 & 2) antibody (#8159), both from Sigma-Aldrich, Burlington, MA, USA.

Techniques: Activation Assay, Expressing, Mutagenesis