amaris custom ablation manager (version 4.6) treatment planning software Search Results


rber chktide peptide proquinase  (SignalChem)
92
SignalChem rber chktide peptide proquinase
Impaired kinase function in SIK3R129C mutant. (A) Alignment of SIK3 orthologs demonstrating evolutionary conservation of p.R129 (conserved residues in grey; R129 in red). (B) 3D homology model of SIK3 kinase domain with indicated ATP binding site (green), substrate binding site (yellow) and activation loop (blue); arrow indicates position of R129. (C) Zoomed in view of the mutant p.R129 (red) surroundings. (D) C-terminally FLAG-tagged wildtype (WT) and R129C SIK3 variants were transfected into HEK293T cells and purified by FLAG immunoprecipitation (IP). The quantities of three independent transfections for each SIK3 variant were determined by western blot (WB). Labeled Empty were cells transfected with empty plasmid. (E-G) Purified SIK3 was used as a kinase in cell-free kinase assays with radioactive ATP and AMARA or <t>CHKtide</t> peptide as substrates. Phosphorylation signal was determined by ATP[32P] autoradiography of kinase reaction spotted on blotting paper (E, F), or by scintillation (G). Recombinant active SIK3 was used as a positive control for kinase activity, while samples with ATP omitted served as negative controls. (F) The ATP[32P] signal shown in (E) was normalized to concentration of immunoprecipitated SIK3 in each reaction and plotted. Data represent compilation of three (AMARA) and four (CHKtide) experiments, with each individual sample measured twice. Statistically significant changes are indicated (Student’s t-test, *** p<0.001). (G) ATP[32P] scintillations expressed as percentages of signal obtained in kinase assays with WT SIK3. The signal obtained in immunocomplexes isolated from cells transfected with empty plasmid instead of SIK3 (E, red lines) represent the background activity. Note the significantly impaired kinase activity of SIK3-R129C, compared to WT SIK3.
Rber Chktide Peptide Proquinase, supplied by SignalChem, 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/amaris+custom+ablation+manager+%28version+4%2E6%29+treatment+planning+software/pmc07529349-371-20-31?v=SignalChem
Average 92 stars, based on 1 article reviews
rber chktide peptide proquinase - by Bioz Stars, 2026-08
92/100 stars
  Buy from Supplier
alamar blue kit  (Aladdin Scientific Corporation)
N/A
Product IntroductionAlamar Blue detection reagent provides a simple, rapid, reliable and safe method for cell proliferation and cytotoxicity detection, which is suitable for high-throughput detection experiments. The main component of the detection reagent is a
   Buy from Supplier
amarocite  (BOC Sciences)
N/A
   Buy from Supplier

Image Search Results


Impaired kinase function in SIK3R129C mutant. (A) Alignment of SIK3 orthologs demonstrating evolutionary conservation of p.R129 (conserved residues in grey; R129 in red). (B) 3D homology model of SIK3 kinase domain with indicated ATP binding site (green), substrate binding site (yellow) and activation loop (blue); arrow indicates position of R129. (C) Zoomed in view of the mutant p.R129 (red) surroundings. (D) C-terminally FLAG-tagged wildtype (WT) and R129C SIK3 variants were transfected into HEK293T cells and purified by FLAG immunoprecipitation (IP). The quantities of three independent transfections for each SIK3 variant were determined by western blot (WB). Labeled Empty were cells transfected with empty plasmid. (E-G) Purified SIK3 was used as a kinase in cell-free kinase assays with radioactive ATP and AMARA or CHKtide peptide as substrates. Phosphorylation signal was determined by ATP[32P] autoradiography of kinase reaction spotted on blotting paper (E, F), or by scintillation (G). Recombinant active SIK3 was used as a positive control for kinase activity, while samples with ATP omitted served as negative controls. (F) The ATP[32P] signal shown in (E) was normalized to concentration of immunoprecipitated SIK3 in each reaction and plotted. Data represent compilation of three (AMARA) and four (CHKtide) experiments, with each individual sample measured twice. Statistically significant changes are indicated (Student’s t-test, *** p<0.001). (G) ATP[32P] scintillations expressed as percentages of signal obtained in kinase assays with WT SIK3. The signal obtained in immunocomplexes isolated from cells transfected with empty plasmid instead of SIK3 (E, red lines) represent the background activity. Note the significantly impaired kinase activity of SIK3-R129C, compared to WT SIK3.

Journal: Science translational medicine

Article Title: PTH/PTHrP-SIK3 mediated pathway affects skeletogenesis through altered mTOR signaling

doi: 10.1126/scitranslmed.aat9356

Figure Lengend Snippet: Impaired kinase function in SIK3R129C mutant. (A) Alignment of SIK3 orthologs demonstrating evolutionary conservation of p.R129 (conserved residues in grey; R129 in red). (B) 3D homology model of SIK3 kinase domain with indicated ATP binding site (green), substrate binding site (yellow) and activation loop (blue); arrow indicates position of R129. (C) Zoomed in view of the mutant p.R129 (red) surroundings. (D) C-terminally FLAG-tagged wildtype (WT) and R129C SIK3 variants were transfected into HEK293T cells and purified by FLAG immunoprecipitation (IP). The quantities of three independent transfections for each SIK3 variant were determined by western blot (WB). Labeled Empty were cells transfected with empty plasmid. (E-G) Purified SIK3 was used as a kinase in cell-free kinase assays with radioactive ATP and AMARA or CHKtide peptide as substrates. Phosphorylation signal was determined by ATP[32P] autoradiography of kinase reaction spotted on blotting paper (E, F), or by scintillation (G). Recombinant active SIK3 was used as a positive control for kinase activity, while samples with ATP omitted served as negative controls. (F) The ATP[32P] signal shown in (E) was normalized to concentration of immunoprecipitated SIK3 in each reaction and plotted. Data represent compilation of three (AMARA) and four (CHKtide) experiments, with each individual sample measured twice. Statistically significant changes are indicated (Student’s t-test, *** p<0.001). (G) ATP[32P] scintillations expressed as percentages of signal obtained in kinase assays with WT SIK3. The signal obtained in immunocomplexes isolated from cells transfected with empty plasmid instead of SIK3 (E, red lines) represent the background activity. Note the significantly impaired kinase activity of SIK3-R129C, compared to WT SIK3.

Article Snippet: Kinase assays were performed using immunopurified SIK3 or 200 ng of recombinant active SIK3 (SignalChem) together with 4.6 μg of RBER-CHKtide peptide (ProQuinase) or 10 μg of AMARA peptide (obtained from SignalChem or Abcam) as a substrate, respectively.

Techniques: Mutagenesis, Binding Assay, Activation Assay, Transfection, Purification, Immunoprecipitation, Variant Assay, Western Blot, Labeling, Plasmid Preparation, Autoradiography, Recombinant, Positive Control, Activity Assay, Concentration Assay, Isolation