BPS Bioscience
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Image Search Results

Journal: Journal of Medicinal Chemistry
Article Title: Identification of a Protein Arginine Methyltransferase 7 (PRMT7)/Protein Arginine Methyltransferase 9 (PRMT9) Inhibitor
doi: 10.1021/acs.jmedchem.3c01030
Figure Lengend Snippet: Architecture of PRMT7 and PRMT9 (prepared using Illustrator for Biological Sequences, IBS) and phylogenetic tree of SAM-dependent class I methyltransferases (obtained with the Structural Genomic Consortium ChromoHub and modified with Adobe Illustrator CC 2023). PRMTs are highlighted in the orange area, whereas non-SET domain-containing KMTs are in the gray area.
Article Snippet: In each well, 2 μL of human
Techniques: Modification

Journal: Journal of Medicinal Chemistry
Article Title: Identification of a Protein Arginine Methyltransferase 7 (PRMT7)/Protein Arginine Methyltransferase 9 (PRMT9) Inhibitor
doi: 10.1021/acs.jmedchem.3c01030
Figure Lengend Snippet: Inhibitory activities of selected PRMT modulators (from in-house libraries) against PRMT9.
Article Snippet: In each well, 2 μL of human
Techniques:
![Inhibition of GST-tagged Hs PRMT9 and Hs PRMT7 (panels a and b, respectively) or Ce PRMT7 and Ce PRMT9 (panels c and d, respectively) by compounds 1a – c as detected by a radioisotope-based assay. The experiments were performed as reported in the Experimental procedures section. GST- Hs PRMT9 (a) and GST- Hs PRMT7 (b) were incubated with human GST-SF3B2 (401–550) peptide or recombinant Hs H2B, respectively (1 μg of enzyme, 5 μg of substrate), 0.14 μM [ 3 H]SAM, and the indicated concentrations of tested compounds at the corresponding optimal reaction temperature (37 °C for Hs PRMT9, 15 °C for Hs PRMT7). C. elegans GST-tagged enzymes PRMT9 (c) and PRMT7 (d) were incubated with GST- Ce SFTB-2 (99–248) fragment or recombinant Hs H2B, respectively (1 μg of enzyme, 5 μg of substrate), 0.14 μM [ 3 H]SAM, and the indicated concentrations of tested compounds at the corresponding optimal reaction temperature (25 °C for Ce PRMT9, 15 °C for Ce PRMT7). After SDS-PAGE, the gels were treated as previously described and densitometry analysis was done using ImageJ software, and data was plotted as normalized activity to the no inhibitor controls.](https://pub-med-central-images-cdn.bioz.com/pub_med_central_ids_ending_with_8352/pmc10578352/pmc10578352__jm3c01030_0004.jpg)
Journal: Journal of Medicinal Chemistry
Article Title: Identification of a Protein Arginine Methyltransferase 7 (PRMT7)/Protein Arginine Methyltransferase 9 (PRMT9) Inhibitor
doi: 10.1021/acs.jmedchem.3c01030
Figure Lengend Snippet: Inhibition of GST-tagged Hs PRMT9 and Hs PRMT7 (panels a and b, respectively) or Ce PRMT7 and Ce PRMT9 (panels c and d, respectively) by compounds 1a – c as detected by a radioisotope-based assay. The experiments were performed as reported in the Experimental procedures section. GST- Hs PRMT9 (a) and GST- Hs PRMT7 (b) were incubated with human GST-SF3B2 (401–550) peptide or recombinant Hs H2B, respectively (1 μg of enzyme, 5 μg of substrate), 0.14 μM [ 3 H]SAM, and the indicated concentrations of tested compounds at the corresponding optimal reaction temperature (37 °C for Hs PRMT9, 15 °C for Hs PRMT7). C. elegans GST-tagged enzymes PRMT9 (c) and PRMT7 (d) were incubated with GST- Ce SFTB-2 (99–248) fragment or recombinant Hs H2B, respectively (1 μg of enzyme, 5 μg of substrate), 0.14 μM [ 3 H]SAM, and the indicated concentrations of tested compounds at the corresponding optimal reaction temperature (25 °C for Ce PRMT9, 15 °C for Ce PRMT7). After SDS-PAGE, the gels were treated as previously described and densitometry analysis was done using ImageJ software, and data was plotted as normalized activity to the no inhibitor controls.
Article Snippet: In each well, 2 μL of human
Techniques: Inhibition, Incubation, Recombinant, SDS Page, Software, Activity Assay

Journal: Journal of Medicinal Chemistry
Article Title: Identification of a Protein Arginine Methyltransferase 7 (PRMT7)/Protein Arginine Methyltransferase 9 (PRMT9) Inhibitor
doi: 10.1021/acs.jmedchem.3c01030
Figure Lengend Snippet: Binding mode of 1a in complex with the PRMT9 3D structure (PDB entry 7RBQ ) as predicted by docking calculations (a) and representative frame of the 500 ns long MD simulation (b). The ligand and enzyme are represented as orange and cyan stick and ribbons, respectively. L-RMSD (c) and L-RMSF (d) plots obtained from the analysis of MD simulations.
Article Snippet: In each well, 2 μL of human
Techniques: Binding Assay

Journal: Journal of Medicinal Chemistry
Article Title: Identification of a Protein Arginine Methyltransferase 7 (PRMT7)/Protein Arginine Methyltransferase 9 (PRMT9) Inhibitor
doi: 10.1021/acs.jmedchem.3c01030
Figure Lengend Snippet: Design of compound 1j to strengthen π-stacking interaction with the PRMT9 W152 residue (in blue).
Article Snippet: In each well, 2 μL of human
Techniques: Residue

Journal: Journal of Medicinal Chemistry
Article Title: Identification of a Protein Arginine Methyltransferase 7 (PRMT7)/Protein Arginine Methyltransferase 9 (PRMT9) Inhibitor
doi: 10.1021/acs.jmedchem.3c01030
Figure Lengend Snippet: Sensorgrams obtained from the SPR interaction analysis of compound 1j binding to immobilized PRMT9. The compound was injected at different concentrations (from 25 to 0.05 mM) with an association and a dissociation time of 90 and 180 s, respectively, and with a flow rate of 30 μL/min. The equilibrium dissociation constant ( K D ) was derived from the ratio between kinetic dissociation ( k off ) and association ( k on ) constants.
Article Snippet: In each well, 2 μL of human
Techniques: Binding Assay, Injection, Derivative Assay

Journal: Journal of Medicinal Chemistry
Article Title: Identification of a Protein Arginine Methyltransferase 7 (PRMT7)/Protein Arginine Methyltransferase 9 (PRMT9) Inhibitor
doi: 10.1021/acs.jmedchem.3c01030
Figure Lengend Snippet: Testing the effects of compounds 1a (EML734), 1b (EML736), 1e (EML979), and 1f (EML980) on PRMT9 activity in MCF7 (top) and MDA-MB-436 breast cancer cell lines. MCF7 and MDA-MB-436 cells were treated with 4 candidate inhibitors at indicated concentrations for 72 h. The total cell lysates were harvested in RIPA buffer and the levels of SF3B2 R508me2s, SF3B2, and PRMT9 were detected by using Western blot assays. Anti-Tubulin antibody was used as a loading control.
Article Snippet: In each well, 2 μL of human
Techniques: Activity Assay, Western Blot, Control

Journal: Journal of Medicinal Chemistry
Article Title: Identification of a Protein Arginine Methyltransferase 7 (PRMT7)/Protein Arginine Methyltransferase 9 (PRMT9) Inhibitor
doi: 10.1021/acs.jmedchem.3c01030
Figure Lengend Snippet: Inhibitory Activities of Compounds 1a–h against PRMT9
Article Snippet: In each well, 2 μL of human
Techniques:

Journal: Journal of Medicinal Chemistry
Article Title: Identification of a Protein Arginine Methyltransferase 7 (PRMT7)/Protein Arginine Methyltransferase 9 (PRMT9) Inhibitor
doi: 10.1021/acs.jmedchem.3c01030
Figure Lengend Snippet: Inhibitory Activities of Compound 1i against PRMTs
Article Snippet: In each well, 2 μL of human
Techniques:

Journal: Journal of Medicinal Chemistry
Article Title: Identification of a Protein Arginine Methyltransferase 7 (PRMT7)/Protein Arginine Methyltransferase 9 (PRMT9) Inhibitor
doi: 10.1021/acs.jmedchem.3c01030
Figure Lengend Snippet: Inhibitory Activities of Compound 1j against PRMTs
Article Snippet: In each well, 2 μL of human
Techniques: