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DiscoverX corporation treespot compound profile visualization tool
Structural and biochemical characterization of ASN007 (A) Molecular structure of ASN007, MW = 473. (B) Dose-response curves of ERK1/2 inhibitors (ASN007 or SCH772894) in a homogeneous time-resolved fluorescence (HTRF)-based ERK1/2 enzymatic activity assay. (C) Kinome tree dendrogram showing the biochemical kinase profiling assay (KinaseProfiler, Eurofiler), which measures the kinase inhibitory activity of ASN007 in a radiometric enzymatic assay in a panel of 335 purified kinases. Hit kinases reported are marked with a red circle and the size of the circle indicates the relative potency of ASN007 for each kinase. ERK1/2 kinases are illustrated by a blue circle. Green dots indicate kinases against which ASN007 does not have significant activity at 1 μM. The dendrogram was generated using the web tool <t>TREESpot,</t> provided by DiscoverX. (D) IC 50 values (nM) for ASN007 against the top 22 kinases, which showed >75% inhibition at 1 μμM, identified from the primary kinome screening. (E) Dose-dependent effect of ASN007 treatment on phosphorylation of ERK1/2 targets. Representative western blot analysis shows inhibition of RSK1 (Ser380) phosphorylation after 4h of ASN007 treatment in a colorectal adenocarcinoma cell line, HT-29. (F) Dose-response curve of ASN007 inhibition of RSK phosphorylation in the human colon cancer HT-29 BRAF V600E mutant cell line, measured by an ELISA test.
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Article Title: ASN007 is a selective ERK1/2 inhibitor with preferential activity against RAS-and RAF-mutant tumors

Journal: Cell Reports Medicine

doi: 10.1016/j.xcrm.2021.100350

Structural and biochemical characterization of ASN007 (A) Molecular structure of ASN007, MW = 473. (B) Dose-response curves of ERK1/2 inhibitors (ASN007 or SCH772894) in a homogeneous time-resolved fluorescence (HTRF)-based ERK1/2 enzymatic activity assay. (C) Kinome tree dendrogram showing the biochemical kinase profiling assay (KinaseProfiler, Eurofiler), which measures the kinase inhibitory activity of ASN007 in a radiometric enzymatic assay in a panel of 335 purified kinases. Hit kinases reported are marked with a red circle and the size of the circle indicates the relative potency of ASN007 for each kinase. ERK1/2 kinases are illustrated by a blue circle. Green dots indicate kinases against which ASN007 does not have significant activity at 1 μM. The dendrogram was generated using the web tool TREESpot, provided by DiscoverX. (D) IC 50 values (nM) for ASN007 against the top 22 kinases, which showed >75% inhibition at 1 μμM, identified from the primary kinome screening. (E) Dose-dependent effect of ASN007 treatment on phosphorylation of ERK1/2 targets. Representative western blot analysis shows inhibition of RSK1 (Ser380) phosphorylation after 4h of ASN007 treatment in a colorectal adenocarcinoma cell line, HT-29. (F) Dose-response curve of ASN007 inhibition of RSK phosphorylation in the human colon cancer HT-29 BRAF V600E mutant cell line, measured by an ELISA test.
Figure Legend Snippet: Structural and biochemical characterization of ASN007 (A) Molecular structure of ASN007, MW = 473. (B) Dose-response curves of ERK1/2 inhibitors (ASN007 or SCH772894) in a homogeneous time-resolved fluorescence (HTRF)-based ERK1/2 enzymatic activity assay. (C) Kinome tree dendrogram showing the biochemical kinase profiling assay (KinaseProfiler, Eurofiler), which measures the kinase inhibitory activity of ASN007 in a radiometric enzymatic assay in a panel of 335 purified kinases. Hit kinases reported are marked with a red circle and the size of the circle indicates the relative potency of ASN007 for each kinase. ERK1/2 kinases are illustrated by a blue circle. Green dots indicate kinases against which ASN007 does not have significant activity at 1 μM. The dendrogram was generated using the web tool TREESpot, provided by DiscoverX. (D) IC 50 values (nM) for ASN007 against the top 22 kinases, which showed >75% inhibition at 1 μμM, identified from the primary kinome screening. (E) Dose-dependent effect of ASN007 treatment on phosphorylation of ERK1/2 targets. Representative western blot analysis shows inhibition of RSK1 (Ser380) phosphorylation after 4h of ASN007 treatment in a colorectal adenocarcinoma cell line, HT-29. (F) Dose-response curve of ASN007 inhibition of RSK phosphorylation in the human colon cancer HT-29 BRAF V600E mutant cell line, measured by an ELISA test.

Techniques Used: Fluorescence, Enzyme Activity Assay, Activity Assay, Enzymatic Assay, Purification, Generated, Inhibition, Phospho-proteomics, Western Blot, Mutagenesis, Enzyme-linked Immunosorbent Assay


Figure Legend Snippet:

Techniques Used: Plasmid Preparation, Recombinant, Proliferation Assay, Software



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DiscoverX corporation treespot compound profile visualization tool
Structural and biochemical characterization of ASN007 (A) Molecular structure of ASN007, MW = 473. (B) Dose-response curves of ERK1/2 inhibitors (ASN007 or SCH772894) in a homogeneous time-resolved fluorescence (HTRF)-based ERK1/2 enzymatic activity assay. (C) Kinome tree dendrogram showing the biochemical kinase profiling assay (KinaseProfiler, Eurofiler), which measures the kinase inhibitory activity of ASN007 in a radiometric enzymatic assay in a panel of 335 purified kinases. Hit kinases reported are marked with a red circle and the size of the circle indicates the relative potency of ASN007 for each kinase. ERK1/2 kinases are illustrated by a blue circle. Green dots indicate kinases against which ASN007 does not have significant activity at 1 μM. The dendrogram was generated using the web tool <t>TREESpot,</t> provided by DiscoverX. (D) IC 50 values (nM) for ASN007 against the top 22 kinases, which showed >75% inhibition at 1 μμM, identified from the primary kinome screening. (E) Dose-dependent effect of ASN007 treatment on phosphorylation of ERK1/2 targets. Representative western blot analysis shows inhibition of RSK1 (Ser380) phosphorylation after 4h of ASN007 treatment in a colorectal adenocarcinoma cell line, HT-29. (F) Dose-response curve of ASN007 inhibition of RSK phosphorylation in the human colon cancer HT-29 BRAF V600E mutant cell line, measured by an ELISA test.
Treespot Compound Profile Visualization Tool, supplied by DiscoverX 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/treespot+compound+profile+visualization+tool/pmc08324497-152-0-6?v=DiscoverX+corporation
Average 90 stars, based on 1 article reviews
treespot compound profile visualization tool - by Bioz Stars, 2026-07
90/100 stars
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Structural and biochemical characterization of ASN007 (A) Molecular structure of ASN007, MW = 473. (B) Dose-response curves of ERK1/2 inhibitors (ASN007 or SCH772894) in a homogeneous time-resolved fluorescence (HTRF)-based ERK1/2 enzymatic activity assay. (C) Kinome tree dendrogram showing the biochemical kinase profiling assay (KinaseProfiler, Eurofiler), which measures the kinase inhibitory activity of ASN007 in a radiometric enzymatic assay in a panel of 335 purified kinases. Hit kinases reported are marked with a red circle and the size of the circle indicates the relative potency of ASN007 for each kinase. ERK1/2 kinases are illustrated by a blue circle. Green dots indicate kinases against which ASN007 does not have significant activity at 1 μM. The dendrogram was generated using the web tool TREESpot, provided by DiscoverX. (D) IC 50 values (nM) for ASN007 against the top 22 kinases, which showed >75% inhibition at 1 μμM, identified from the primary kinome screening. (E) Dose-dependent effect of ASN007 treatment on phosphorylation of ERK1/2 targets. Representative western blot analysis shows inhibition of RSK1 (Ser380) phosphorylation after 4h of ASN007 treatment in a colorectal adenocarcinoma cell line, HT-29. (F) Dose-response curve of ASN007 inhibition of RSK phosphorylation in the human colon cancer HT-29 BRAF V600E mutant cell line, measured by an ELISA test.

Journal: Cell Reports Medicine

Article Title: ASN007 is a selective ERK1/2 inhibitor with preferential activity against RAS-and RAF-mutant tumors

doi: 10.1016/j.xcrm.2021.100350

Figure Lengend Snippet: Structural and biochemical characterization of ASN007 (A) Molecular structure of ASN007, MW = 473. (B) Dose-response curves of ERK1/2 inhibitors (ASN007 or SCH772894) in a homogeneous time-resolved fluorescence (HTRF)-based ERK1/2 enzymatic activity assay. (C) Kinome tree dendrogram showing the biochemical kinase profiling assay (KinaseProfiler, Eurofiler), which measures the kinase inhibitory activity of ASN007 in a radiometric enzymatic assay in a panel of 335 purified kinases. Hit kinases reported are marked with a red circle and the size of the circle indicates the relative potency of ASN007 for each kinase. ERK1/2 kinases are illustrated by a blue circle. Green dots indicate kinases against which ASN007 does not have significant activity at 1 μM. The dendrogram was generated using the web tool TREESpot, provided by DiscoverX. (D) IC 50 values (nM) for ASN007 against the top 22 kinases, which showed >75% inhibition at 1 μμM, identified from the primary kinome screening. (E) Dose-dependent effect of ASN007 treatment on phosphorylation of ERK1/2 targets. Representative western blot analysis shows inhibition of RSK1 (Ser380) phosphorylation after 4h of ASN007 treatment in a colorectal adenocarcinoma cell line, HT-29. (F) Dose-response curve of ASN007 inhibition of RSK phosphorylation in the human colon cancer HT-29 BRAF V600E mutant cell line, measured by an ELISA test.

Article Snippet: TREEspot Compound Profile Visualization Tool , DiscoverX , N/A.

Techniques: Fluorescence, Enzyme Activity Assay, Activity Assay, Enzymatic Assay, Purification, Generated, Inhibition, Phospho-proteomics, Western Blot, Mutagenesis, Enzyme-linked Immunosorbent Assay

Journal: Cell Reports Medicine

Article Title: ASN007 is a selective ERK1/2 inhibitor with preferential activity against RAS-and RAF-mutant tumors

doi: 10.1016/j.xcrm.2021.100350

Figure Lengend Snippet:

Article Snippet: TREEspot Compound Profile Visualization Tool , DiscoverX , N/A.

Techniques: Plasmid Preparation, Recombinant, Proliferation Assay, Software