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p akt  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc p akt
    P Akt, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 17213 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/p+akt+ser473/Phospho-Akt+(Ser473)+XP+Rabbit+mAb/pmc13018931-113-24-27
    Average 99 stars, based on 17213 article reviews
    p akt - by Bioz Stars, 2026-10
    99/100 stars

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    Related Articles

    other:

    Article Title: Effects of branched-chain amino acids on iron deficiency-induced muscle atrophy
    Article Snippet: p-Akt (Ser473) , Rabbit , 4060 , 1:2000 , Cell Signaling Technology.

    Article Title: Dietary energy levels regulate feed intake of broilers through the brain-gut axis
    Article Snippet: p-Akt (Ser473) , Cell signaling technology , Cat #9271.

    Western Blot:

    Article Title: Attempt to control head and neck cancer through medium-molecular weight drug discovery
    Article Snippet: Background: Head and neck squamous cell carcinoma (HNSCC) arises from the squamous epithelium of the head and neck region, comprising heterogeneous lesions with distinct risk factors and diverse genetic and epigenetic alteration patterns.. HNSCC is often difficult to control when lymph node metastasis has occurred, and treatment outcomes remain unsatisfactory.. Elucidating the genetic and epigenetic profiles of cancer-associated genes is essential for improving clinical outcomes, yet to date the key molecules driving HNSCC progression remain

    Article Title: Discovery of triazolyl azabicyclo[3.1.0]hexane derivative as an autotaxin inhibitors for the treatment of pulmonary fibrosis.
    Article Snippet: Autotaxin (ATX), the enzyme responsible for generating lysophosphatidic acid (LPA), is a validated target for fibrosis and cancer immunotherapy.. Current ATX inhibitors face challenges related to insufficient efficacy or safety concerns, reflecting trade-offs between zinc engagement and selectivity.. Here, we report a rigid triazolylazabicyclo[3.1.0]hexanyl–oxadiazolyl-pyrimidine scaffold developed through structure-based design, designed to potentially enhance ATX selectivity by promoting defined binding geometry.

    Cell-Signaling:

    Article Title: Discovery of triazolyl azabicyclo[3.1.0]hexane derivative as an autotaxin inhibitors for the treatment of pulmonary fibrosis.
    Article Snippet: Autotaxin (ATX), the enzyme responsible for generating lysophosphatidic acid (LPA), is a validated target for fibrosis and cancer immunotherapy.. Current ATX inhibitors face challenges related to insufficient efficacy or safety concerns, reflecting trade-offs between zinc engagement and selectivity.. Here, we report a rigid triazolylazabicyclo[3.1.0]hexanyl–oxadiazolyl-pyrimidine scaffold developed through structure-based design, designed to potentially enhance ATX selectivity by promoting defined binding geometry.

    Article Title: Novel Silver(I) and Gold(I) N‐Heterocyclic Carbene Complexes Induce ROS ‐Dependent Autophagic Cell Death in Human Hepatoma Cell Line HepG2
    Article Snippet: .. Primary antibodies specific for anti‐PARP (#9542), LC3A/B (#12741), β‐actin (#3700), AKT (#4691), p‐AKT (Ser473) (#4060), were purchased from Cell Signaling Technology (CST, Danvers, MA, USA). .. Primary antibodies specific for Beclin‐1 (#849701), was purchased from Biolegend (San Diego, CA, USA).

    Immunohistochemistry:

    Article Title: Discovery of triazolyl azabicyclo[3.1.0]hexane derivative as an autotaxin inhibitors for the treatment of pulmonary fibrosis.
    Article Snippet: Autotaxin (ATX), the enzyme responsible for generating lysophosphatidic acid (LPA), is a validated target for fibrosis and cancer immunotherapy.. Current ATX inhibitors face challenges related to insufficient efficacy or safety concerns, reflecting trade-offs between zinc engagement and selectivity.. Here, we report a rigid triazolylazabicyclo[3.1.0]hexanyl–oxadiazolyl-pyrimidine scaffold developed through structure-based design, designed to potentially enhance ATX selectivity by promoting defined binding geometry.

    Purification:

    Article Title: Discovery of triazolyl azabicyclo[3.1.0]hexane derivative as an autotaxin inhibitors for the treatment of pulmonary fibrosis.
    Article Snippet: Autotaxin (ATX), the enzyme responsible for generating lysophosphatidic acid (LPA), is a validated target for fibrosis and cancer immunotherapy.. Current ATX inhibitors face challenges related to insufficient efficacy or safety concerns, reflecting trade-offs between zinc engagement and selectivity.. Here, we report a rigid triazolylazabicyclo[3.1.0]hexanyl–oxadiazolyl-pyrimidine scaffold developed through structure-based design, designed to potentially enhance ATX selectivity by promoting defined binding geometry.

    Incubation:

    Article Title: Mutant ribosomal protein RPS15 drives B cell malignancy through oxidative stress and genomic instability.
    Article Snippet: Protein concentration was determined using the Pierce bicinchoninic acid assay (Life Technologies #23225) and 40 μg of protein were loaded per lane on a 4-12% Bis-Tris or 3-8% Tris-Acetate gel (Life Technologies #NP0323 and #EA03785). .. Proteins were transferred onto polyvinylidene fluoride membranes (Life Technologies IB24002) using an iBlot 2 at 20V for 6-12 minutes and subsequently incubated in 5% BSA, 1X TBST AR TI CL E IN P RE SS (Teknova #T9511) prior to probing with one of the following primary antibodies: RPS15 (1:1000 dilution; #PIPA562977, Thermo Fisher Scientific), RPL5 (1:1000; #14568S, Cell Signaling Technology), ATM (1:1000; #2873, clone D2E2, Cell Signaling Technology), p-ATM Ser1981 (1:250; #AF1655, R&D), SMC1 (1:1000; #4802, Cell Signaling Technology), p-SMC1 Ser957 (1:1000; #4805, clone 5D11G5, Cell Signaling Technology), Chk2 (1:1000; #sc-5278, clone A12, Santa Cruz), p-Chk2 Thr68 (1:500; #2661, Cell Signaling Technology), Chk1 (1:1000; #sc8408, clone G-4, Santa Cruz), p-Chk1 Ser345 (1:500; #2341, Cell Signaling Technology), γH2AX Ser139 (1:1000; #05-636, clone JBW301, Millipore; and 1:1000; #2577, Cell Signaling Technology), p53 (1:1000; #9282 and #2524 [clone 1C12], Cell Signaling Technology), p21 (1:500; #64016, Cell Signaling Technology), cyclin A (1:200, #sc-239, clone BF683, Santa Cruz), AKT (1:1000, #4298, clone 40D4, Cell Signaling Technology), p-AKT Ser473 (1:1000, #4060, clone D9E, Cell Signaling Technology), ERK1/2 (1:1000, #4695, clone 137F5, Cell Signaling Technology), p-ERK1/2 Tyr202/204 (1:1000, #4370, clone D13.4.4E, Cell Signaling Technology), p-SYK Tyr525/526 (1:1000, #2711, Cell Signaling Technology), SYK (1:1000, #13198, clone D3Z1E, Cell Signaling Technology), p-PLCγ1 Tyr783 (1:1000, #2821, Cell Signaling Technology), PLCγ1 (1:1000, #5690, clone D9H10, Cell Signaling Technology), GPX1 (1:200; #AF3798, R&D), EIF1AD (1:500, #20528-1, Proteintech), OTUD4 (1:500; #25070-1, Proteintech), PTP4A2 (1:500, #PA5120349, ThermoFisher Scientific), actin (1:2000; #5125, clone 13E5, Cell Signaling Technology), HSP90 (1:1000; #79641, clone C45G5, Cell Signaling Technology) and GAPDH (1:1000; #2118, clone 14C10, Cell Signaling Technology). .. Membranes were washed in TBST prior to incubation with a 1:2000 or 1:10,000 dilution of goat anti-rabbit HRP-conjugated IgG antibody (Fisher Scientific 12348MI or Cell Signaling Technology, #7074), a 1:1000 dilution of horse anti-mouse HRP-conjugated IgG antibody (Cell Signaling Technology, #7076), or a 1:1000 dilution of rabbit anti-goat HRP-conjugated IgG antibody (R&D, #HAF017) for 1 hour at room temperature.



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    p akt ser473  (ABclonal Biotechnology)
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    Phosphorylation of AKT1 at <t>Ser473</t> enhances its binding to Lys140 of Insig1. (A) The interaction between endogenous AKT1 and Insig1 in NIH‐3T3 cells was demonstrated by co‐immunoprecipitation. (B) The molecular docking mode of the interaction between AKT1 and Insig1. (C) RMSD (up) and RMSF (down) analysis showing the binding of AKT1 and Insig1. Red, black, and blue represent AKT1, Insig1, and the complex, respectively. (D) Molecular mechanics‐Poisson‐Boltzmann surface area (MM‐PBSA) analysis of AKT1–Insig1 and pAKT1 (Ser473+Thr308)–Insig1 complexes. Calculation of energy terms (kcal per mol) from the 100 ns trajectory. Van der Waals Energy (ΔvdW) indicated nonpolar interactions between molecules. Electrostatic Energy (ΔEEL) indicated electrostatic interaction energy between charges. Polar solvation energy (ΔEPB) represents the solvation energy of molecules in polar solvents, calculated by employing the Poisson–Boltzmann equation. Nonpolar Solvation Energy (ΔESA) was typically calculated based on the solvent‐accessible surface area multiplied by an empirical coefficient. Δ G bind (Δ E tot ) represented the overall binding affinity between interacting molecules. (E) FEL of the two complexes, constructed using RMSD and R g as variables, displaying the energy distribution in different conformational states between 0 and 100 ns (left). H‐bonds and hydrophobic interactions by LigPlus illustrating interactions between AKT1 and Insig1 in two different states, which are displayed in green dotted lines and red or pink spikes, respectively. The main panel shows hydrogen bonds and hydrophobic interactions surrounding AKT1 Ser473 and pSer473 with Insig1 (right). (F,G) Co‐IP analysis to assess AKT1–Insig1 interaction in the dTNF‐InSen NIH‐3T3 cells after transfection of Insig1 K140A vector under conditions of AKT1 WT overexpression or AKT1 S473A vector under the condition of Insig1 WT overexpression. (H,I) The expression of γ‐H2AX ( n = 60 per group), Il‐6 ( n = 3 per group), and Mmp13 ( n = 3 per group) in the dTNF‐InSen FLSs after the transfection of AKT1 WT or AKT1 S473A vector under the condition of Insig1 WT overexpression, compared to the controls. All statistical tests were two‐sided. Fisher's exact test (H). Student's t ‐test (I). dTNF‐InSen, induction of senescence by double treatment of TNF‐α; RMSD, protein backbone root mean square deviation; RMSF, root mean square fluctuation; FEL, free energy landscape; R g , radius of gyration.
    P Akt Ser473, supplied by ABclonal Biotechnology, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    p akt  (Cell Signaling Technology Inc)
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    Phosphorylation of AKT1 at <t>Ser473</t> enhances its binding to Lys140 of Insig1. (A) The interaction between endogenous AKT1 and Insig1 in NIH‐3T3 cells was demonstrated by co‐immunoprecipitation. (B) The molecular docking mode of the interaction between AKT1 and Insig1. (C) RMSD (up) and RMSF (down) analysis showing the binding of AKT1 and Insig1. Red, black, and blue represent AKT1, Insig1, and the complex, respectively. (D) Molecular mechanics‐Poisson‐Boltzmann surface area (MM‐PBSA) analysis of AKT1–Insig1 and pAKT1 (Ser473+Thr308)–Insig1 complexes. Calculation of energy terms (kcal per mol) from the 100 ns trajectory. Van der Waals Energy (ΔvdW) indicated nonpolar interactions between molecules. Electrostatic Energy (ΔEEL) indicated electrostatic interaction energy between charges. Polar solvation energy (ΔEPB) represents the solvation energy of molecules in polar solvents, calculated by employing the Poisson–Boltzmann equation. Nonpolar Solvation Energy (ΔESA) was typically calculated based on the solvent‐accessible surface area multiplied by an empirical coefficient. Δ G bind (Δ E tot ) represented the overall binding affinity between interacting molecules. (E) FEL of the two complexes, constructed using RMSD and R g as variables, displaying the energy distribution in different conformational states between 0 and 100 ns (left). H‐bonds and hydrophobic interactions by LigPlus illustrating interactions between AKT1 and Insig1 in two different states, which are displayed in green dotted lines and red or pink spikes, respectively. The main panel shows hydrogen bonds and hydrophobic interactions surrounding AKT1 Ser473 and pSer473 with Insig1 (right). (F,G) Co‐IP analysis to assess AKT1–Insig1 interaction in the dTNF‐InSen NIH‐3T3 cells after transfection of Insig1 K140A vector under conditions of AKT1 WT overexpression or AKT1 S473A vector under the condition of Insig1 WT overexpression. (H,I) The expression of γ‐H2AX ( n = 60 per group), Il‐6 ( n = 3 per group), and Mmp13 ( n = 3 per group) in the dTNF‐InSen FLSs after the transfection of AKT1 WT or AKT1 S473A vector under the condition of Insig1 WT overexpression, compared to the controls. All statistical tests were two‐sided. Fisher's exact test (H). Student's t ‐test (I). dTNF‐InSen, induction of senescence by double treatment of TNF‐α; RMSD, protein backbone root mean square deviation; RMSF, root mean square fluctuation; FEL, free energy landscape; R g , radius of gyration.
    P Akt, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Phosphorylation of AKT1 at <t>Ser473</t> enhances its binding to Lys140 of Insig1. (A) The interaction between endogenous AKT1 and Insig1 in NIH‐3T3 cells was demonstrated by co‐immunoprecipitation. (B) The molecular docking mode of the interaction between AKT1 and Insig1. (C) RMSD (up) and RMSF (down) analysis showing the binding of AKT1 and Insig1. Red, black, and blue represent AKT1, Insig1, and the complex, respectively. (D) Molecular mechanics‐Poisson‐Boltzmann surface area (MM‐PBSA) analysis of AKT1–Insig1 and pAKT1 (Ser473+Thr308)–Insig1 complexes. Calculation of energy terms (kcal per mol) from the 100 ns trajectory. Van der Waals Energy (ΔvdW) indicated nonpolar interactions between molecules. Electrostatic Energy (ΔEEL) indicated electrostatic interaction energy between charges. Polar solvation energy (ΔEPB) represents the solvation energy of molecules in polar solvents, calculated by employing the Poisson–Boltzmann equation. Nonpolar Solvation Energy (ΔESA) was typically calculated based on the solvent‐accessible surface area multiplied by an empirical coefficient. Δ G bind (Δ E tot ) represented the overall binding affinity between interacting molecules. (E) FEL of the two complexes, constructed using RMSD and R g as variables, displaying the energy distribution in different conformational states between 0 and 100 ns (left). H‐bonds and hydrophobic interactions by LigPlus illustrating interactions between AKT1 and Insig1 in two different states, which are displayed in green dotted lines and red or pink spikes, respectively. The main panel shows hydrogen bonds and hydrophobic interactions surrounding AKT1 Ser473 and pSer473 with Insig1 (right). (F,G) Co‐IP analysis to assess AKT1–Insig1 interaction in the dTNF‐InSen NIH‐3T3 cells after transfection of Insig1 K140A vector under conditions of AKT1 WT overexpression or AKT1 S473A vector under the condition of Insig1 WT overexpression. (H,I) The expression of γ‐H2AX ( n = 60 per group), Il‐6 ( n = 3 per group), and Mmp13 ( n = 3 per group) in the dTNF‐InSen FLSs after the transfection of AKT1 WT or AKT1 S473A vector under the condition of Insig1 WT overexpression, compared to the controls. All statistical tests were two‐sided. Fisher's exact test (H). Student's t ‐test (I). dTNF‐InSen, induction of senescence by double treatment of TNF‐α; RMSD, protein backbone root mean square deviation; RMSF, root mean square fluctuation; FEL, free energy landscape; R g , radius of gyration.
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    Phosphorylation of AKT1 at <t>Ser473</t> enhances its binding to Lys140 of Insig1. (A) The interaction between endogenous AKT1 and Insig1 in NIH‐3T3 cells was demonstrated by co‐immunoprecipitation. (B) The molecular docking mode of the interaction between AKT1 and Insig1. (C) RMSD (up) and RMSF (down) analysis showing the binding of AKT1 and Insig1. Red, black, and blue represent AKT1, Insig1, and the complex, respectively. (D) Molecular mechanics‐Poisson‐Boltzmann surface area (MM‐PBSA) analysis of AKT1–Insig1 and pAKT1 (Ser473+Thr308)–Insig1 complexes. Calculation of energy terms (kcal per mol) from the 100 ns trajectory. Van der Waals Energy (ΔvdW) indicated nonpolar interactions between molecules. Electrostatic Energy (ΔEEL) indicated electrostatic interaction energy between charges. Polar solvation energy (ΔEPB) represents the solvation energy of molecules in polar solvents, calculated by employing the Poisson–Boltzmann equation. Nonpolar Solvation Energy (ΔESA) was typically calculated based on the solvent‐accessible surface area multiplied by an empirical coefficient. Δ G bind (Δ E tot ) represented the overall binding affinity between interacting molecules. (E) FEL of the two complexes, constructed using RMSD and R g as variables, displaying the energy distribution in different conformational states between 0 and 100 ns (left). H‐bonds and hydrophobic interactions by LigPlus illustrating interactions between AKT1 and Insig1 in two different states, which are displayed in green dotted lines and red or pink spikes, respectively. The main panel shows hydrogen bonds and hydrophobic interactions surrounding AKT1 Ser473 and pSer473 with Insig1 (right). (F,G) Co‐IP analysis to assess AKT1–Insig1 interaction in the dTNF‐InSen NIH‐3T3 cells after transfection of Insig1 K140A vector under conditions of AKT1 WT overexpression or AKT1 S473A vector under the condition of Insig1 WT overexpression. (H,I) The expression of γ‐H2AX ( n = 60 per group), Il‐6 ( n = 3 per group), and Mmp13 ( n = 3 per group) in the dTNF‐InSen FLSs after the transfection of AKT1 WT or AKT1 S473A vector under the condition of Insig1 WT overexpression, compared to the controls. All statistical tests were two‐sided. Fisher's exact test (H). Student's t ‐test (I). dTNF‐InSen, induction of senescence by double treatment of TNF‐α; RMSD, protein backbone root mean square deviation; RMSF, root mean square fluctuation; FEL, free energy landscape; R g , radius of gyration.
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    Phosphorylation of AKT1 at <t>Ser473</t> enhances its binding to Lys140 of Insig1. (A) The interaction between endogenous AKT1 and Insig1 in NIH‐3T3 cells was demonstrated by co‐immunoprecipitation. (B) The molecular docking mode of the interaction between AKT1 and Insig1. (C) RMSD (up) and RMSF (down) analysis showing the binding of AKT1 and Insig1. Red, black, and blue represent AKT1, Insig1, and the complex, respectively. (D) Molecular mechanics‐Poisson‐Boltzmann surface area (MM‐PBSA) analysis of AKT1–Insig1 and pAKT1 (Ser473+Thr308)–Insig1 complexes. Calculation of energy terms (kcal per mol) from the 100 ns trajectory. Van der Waals Energy (ΔvdW) indicated nonpolar interactions between molecules. Electrostatic Energy (ΔEEL) indicated electrostatic interaction energy between charges. Polar solvation energy (ΔEPB) represents the solvation energy of molecules in polar solvents, calculated by employing the Poisson–Boltzmann equation. Nonpolar Solvation Energy (ΔESA) was typically calculated based on the solvent‐accessible surface area multiplied by an empirical coefficient. Δ G bind (Δ E tot ) represented the overall binding affinity between interacting molecules. (E) FEL of the two complexes, constructed using RMSD and R g as variables, displaying the energy distribution in different conformational states between 0 and 100 ns (left). H‐bonds and hydrophobic interactions by LigPlus illustrating interactions between AKT1 and Insig1 in two different states, which are displayed in green dotted lines and red or pink spikes, respectively. The main panel shows hydrogen bonds and hydrophobic interactions surrounding AKT1 Ser473 and pSer473 with Insig1 (right). (F,G) Co‐IP analysis to assess AKT1–Insig1 interaction in the dTNF‐InSen NIH‐3T3 cells after transfection of Insig1 K140A vector under conditions of AKT1 WT overexpression or AKT1 S473A vector under the condition of Insig1 WT overexpression. (H,I) The expression of γ‐H2AX ( n = 60 per group), Il‐6 ( n = 3 per group), and Mmp13 ( n = 3 per group) in the dTNF‐InSen FLSs after the transfection of AKT1 WT or AKT1 S473A vector under the condition of Insig1 WT overexpression, compared to the controls. All statistical tests were two‐sided. Fisher's exact test (H). Student's t ‐test (I). dTNF‐InSen, induction of senescence by double treatment of TNF‐α; RMSD, protein backbone root mean square deviation; RMSF, root mean square fluctuation; FEL, free energy landscape; R g , radius of gyration.
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    Phosphorylation of AKT1 at <t>Ser473</t> enhances its binding to Lys140 of Insig1. (A) The interaction between endogenous AKT1 and Insig1 in NIH‐3T3 cells was demonstrated by co‐immunoprecipitation. (B) The molecular docking mode of the interaction between AKT1 and Insig1. (C) RMSD (up) and RMSF (down) analysis showing the binding of AKT1 and Insig1. Red, black, and blue represent AKT1, Insig1, and the complex, respectively. (D) Molecular mechanics‐Poisson‐Boltzmann surface area (MM‐PBSA) analysis of AKT1–Insig1 and pAKT1 (Ser473+Thr308)–Insig1 complexes. Calculation of energy terms (kcal per mol) from the 100 ns trajectory. Van der Waals Energy (ΔvdW) indicated nonpolar interactions between molecules. Electrostatic Energy (ΔEEL) indicated electrostatic interaction energy between charges. Polar solvation energy (ΔEPB) represents the solvation energy of molecules in polar solvents, calculated by employing the Poisson–Boltzmann equation. Nonpolar Solvation Energy (ΔESA) was typically calculated based on the solvent‐accessible surface area multiplied by an empirical coefficient. Δ G bind (Δ E tot ) represented the overall binding affinity between interacting molecules. (E) FEL of the two complexes, constructed using RMSD and R g as variables, displaying the energy distribution in different conformational states between 0 and 100 ns (left). H‐bonds and hydrophobic interactions by LigPlus illustrating interactions between AKT1 and Insig1 in two different states, which are displayed in green dotted lines and red or pink spikes, respectively. The main panel shows hydrogen bonds and hydrophobic interactions surrounding AKT1 Ser473 and pSer473 with Insig1 (right). (F,G) Co‐IP analysis to assess AKT1–Insig1 interaction in the dTNF‐InSen NIH‐3T3 cells after transfection of Insig1 K140A vector under conditions of AKT1 WT overexpression or AKT1 S473A vector under the condition of Insig1 WT overexpression. (H,I) The expression of γ‐H2AX ( n = 60 per group), Il‐6 ( n = 3 per group), and Mmp13 ( n = 3 per group) in the dTNF‐InSen FLSs after the transfection of AKT1 WT or AKT1 S473A vector under the condition of Insig1 WT overexpression, compared to the controls. All statistical tests were two‐sided. Fisher's exact test (H). Student's t ‐test (I). dTNF‐InSen, induction of senescence by double treatment of TNF‐α; RMSD, protein backbone root mean square deviation; RMSF, root mean square fluctuation; FEL, free energy landscape; R g , radius of gyration.
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    p s6  (Cell Signaling Technology Inc)
    99
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    Phosphorylation of AKT1 at <t>Ser473</t> enhances its binding to Lys140 of Insig1. (A) The interaction between endogenous AKT1 and Insig1 in NIH‐3T3 cells was demonstrated by co‐immunoprecipitation. (B) The molecular docking mode of the interaction between AKT1 and Insig1. (C) RMSD (up) and RMSF (down) analysis showing the binding of AKT1 and Insig1. Red, black, and blue represent AKT1, Insig1, and the complex, respectively. (D) Molecular mechanics‐Poisson‐Boltzmann surface area (MM‐PBSA) analysis of AKT1–Insig1 and pAKT1 (Ser473+Thr308)–Insig1 complexes. Calculation of energy terms (kcal per mol) from the 100 ns trajectory. Van der Waals Energy (ΔvdW) indicated nonpolar interactions between molecules. Electrostatic Energy (ΔEEL) indicated electrostatic interaction energy between charges. Polar solvation energy (ΔEPB) represents the solvation energy of molecules in polar solvents, calculated by employing the Poisson–Boltzmann equation. Nonpolar Solvation Energy (ΔESA) was typically calculated based on the solvent‐accessible surface area multiplied by an empirical coefficient. Δ G bind (Δ E tot ) represented the overall binding affinity between interacting molecules. (E) FEL of the two complexes, constructed using RMSD and R g as variables, displaying the energy distribution in different conformational states between 0 and 100 ns (left). H‐bonds and hydrophobic interactions by LigPlus illustrating interactions between AKT1 and Insig1 in two different states, which are displayed in green dotted lines and red or pink spikes, respectively. The main panel shows hydrogen bonds and hydrophobic interactions surrounding AKT1 Ser473 and pSer473 with Insig1 (right). (F,G) Co‐IP analysis to assess AKT1–Insig1 interaction in the dTNF‐InSen NIH‐3T3 cells after transfection of Insig1 K140A vector under conditions of AKT1 WT overexpression or AKT1 S473A vector under the condition of Insig1 WT overexpression. (H,I) The expression of γ‐H2AX ( n = 60 per group), Il‐6 ( n = 3 per group), and Mmp13 ( n = 3 per group) in the dTNF‐InSen FLSs after the transfection of AKT1 WT or AKT1 S473A vector under the condition of Insig1 WT overexpression, compared to the controls. All statistical tests were two‐sided. Fisher's exact test (H). Student's t ‐test (I). dTNF‐InSen, induction of senescence by double treatment of TNF‐α; RMSD, protein backbone root mean square deviation; RMSF, root mean square fluctuation; FEL, free energy landscape; R g , radius of gyration.
    P S6, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    rabbit monoclonal p akt ser473  (Cell Signaling Technology Inc)
    86
    Cell Signaling Technology Inc rabbit monoclonal p akt ser473
    Phosphorylation of AKT1 at <t>Ser473</t> enhances its binding to Lys140 of Insig1. (A) The interaction between endogenous AKT1 and Insig1 in NIH‐3T3 cells was demonstrated by co‐immunoprecipitation. (B) The molecular docking mode of the interaction between AKT1 and Insig1. (C) RMSD (up) and RMSF (down) analysis showing the binding of AKT1 and Insig1. Red, black, and blue represent AKT1, Insig1, and the complex, respectively. (D) Molecular mechanics‐Poisson‐Boltzmann surface area (MM‐PBSA) analysis of AKT1–Insig1 and pAKT1 (Ser473+Thr308)–Insig1 complexes. Calculation of energy terms (kcal per mol) from the 100 ns trajectory. Van der Waals Energy (ΔvdW) indicated nonpolar interactions between molecules. Electrostatic Energy (ΔEEL) indicated electrostatic interaction energy between charges. Polar solvation energy (ΔEPB) represents the solvation energy of molecules in polar solvents, calculated by employing the Poisson–Boltzmann equation. Nonpolar Solvation Energy (ΔESA) was typically calculated based on the solvent‐accessible surface area multiplied by an empirical coefficient. Δ G bind (Δ E tot ) represented the overall binding affinity between interacting molecules. (E) FEL of the two complexes, constructed using RMSD and R g as variables, displaying the energy distribution in different conformational states between 0 and 100 ns (left). H‐bonds and hydrophobic interactions by LigPlus illustrating interactions between AKT1 and Insig1 in two different states, which are displayed in green dotted lines and red or pink spikes, respectively. The main panel shows hydrogen bonds and hydrophobic interactions surrounding AKT1 Ser473 and pSer473 with Insig1 (right). (F,G) Co‐IP analysis to assess AKT1–Insig1 interaction in the dTNF‐InSen NIH‐3T3 cells after transfection of Insig1 K140A vector under conditions of AKT1 WT overexpression or AKT1 S473A vector under the condition of Insig1 WT overexpression. (H,I) The expression of γ‐H2AX ( n = 60 per group), Il‐6 ( n = 3 per group), and Mmp13 ( n = 3 per group) in the dTNF‐InSen FLSs after the transfection of AKT1 WT or AKT1 S473A vector under the condition of Insig1 WT overexpression, compared to the controls. All statistical tests were two‐sided. Fisher's exact test (H). Student's t ‐test (I). dTNF‐InSen, induction of senescence by double treatment of TNF‐α; RMSD, protein backbone root mean square deviation; RMSF, root mean square fluctuation; FEL, free energy landscape; R g , radius of gyration.
    Rabbit Monoclonal P Akt Ser473, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Phosphorylation of AKT1 at Ser473 enhances its binding to Lys140 of Insig1. (A) The interaction between endogenous AKT1 and Insig1 in NIH‐3T3 cells was demonstrated by co‐immunoprecipitation. (B) The molecular docking mode of the interaction between AKT1 and Insig1. (C) RMSD (up) and RMSF (down) analysis showing the binding of AKT1 and Insig1. Red, black, and blue represent AKT1, Insig1, and the complex, respectively. (D) Molecular mechanics‐Poisson‐Boltzmann surface area (MM‐PBSA) analysis of AKT1–Insig1 and pAKT1 (Ser473+Thr308)–Insig1 complexes. Calculation of energy terms (kcal per mol) from the 100 ns trajectory. Van der Waals Energy (ΔvdW) indicated nonpolar interactions between molecules. Electrostatic Energy (ΔEEL) indicated electrostatic interaction energy between charges. Polar solvation energy (ΔEPB) represents the solvation energy of molecules in polar solvents, calculated by employing the Poisson–Boltzmann equation. Nonpolar Solvation Energy (ΔESA) was typically calculated based on the solvent‐accessible surface area multiplied by an empirical coefficient. Δ G bind (Δ E tot ) represented the overall binding affinity between interacting molecules. (E) FEL of the two complexes, constructed using RMSD and R g as variables, displaying the energy distribution in different conformational states between 0 and 100 ns (left). H‐bonds and hydrophobic interactions by LigPlus illustrating interactions between AKT1 and Insig1 in two different states, which are displayed in green dotted lines and red or pink spikes, respectively. The main panel shows hydrogen bonds and hydrophobic interactions surrounding AKT1 Ser473 and pSer473 with Insig1 (right). (F,G) Co‐IP analysis to assess AKT1–Insig1 interaction in the dTNF‐InSen NIH‐3T3 cells after transfection of Insig1 K140A vector under conditions of AKT1 WT overexpression or AKT1 S473A vector under the condition of Insig1 WT overexpression. (H,I) The expression of γ‐H2AX ( n = 60 per group), Il‐6 ( n = 3 per group), and Mmp13 ( n = 3 per group) in the dTNF‐InSen FLSs after the transfection of AKT1 WT or AKT1 S473A vector under the condition of Insig1 WT overexpression, compared to the controls. All statistical tests were two‐sided. Fisher's exact test (H). Student's t ‐test (I). dTNF‐InSen, induction of senescence by double treatment of TNF‐α; RMSD, protein backbone root mean square deviation; RMSF, root mean square fluctuation; FEL, free energy landscape; R g , radius of gyration.

    Journal: Advanced Science

    Article Title: HMGCR‐Driven Cholesterol Metabolism Promotes Osteoarthritis Progression by Accelerating Synovial Fibroblast Senescence

    doi: 10.1002/advs.76498

    Figure Lengend Snippet: Phosphorylation of AKT1 at Ser473 enhances its binding to Lys140 of Insig1. (A) The interaction between endogenous AKT1 and Insig1 in NIH‐3T3 cells was demonstrated by co‐immunoprecipitation. (B) The molecular docking mode of the interaction between AKT1 and Insig1. (C) RMSD (up) and RMSF (down) analysis showing the binding of AKT1 and Insig1. Red, black, and blue represent AKT1, Insig1, and the complex, respectively. (D) Molecular mechanics‐Poisson‐Boltzmann surface area (MM‐PBSA) analysis of AKT1–Insig1 and pAKT1 (Ser473+Thr308)–Insig1 complexes. Calculation of energy terms (kcal per mol) from the 100 ns trajectory. Van der Waals Energy (ΔvdW) indicated nonpolar interactions between molecules. Electrostatic Energy (ΔEEL) indicated electrostatic interaction energy between charges. Polar solvation energy (ΔEPB) represents the solvation energy of molecules in polar solvents, calculated by employing the Poisson–Boltzmann equation. Nonpolar Solvation Energy (ΔESA) was typically calculated based on the solvent‐accessible surface area multiplied by an empirical coefficient. Δ G bind (Δ E tot ) represented the overall binding affinity between interacting molecules. (E) FEL of the two complexes, constructed using RMSD and R g as variables, displaying the energy distribution in different conformational states between 0 and 100 ns (left). H‐bonds and hydrophobic interactions by LigPlus illustrating interactions between AKT1 and Insig1 in two different states, which are displayed in green dotted lines and red or pink spikes, respectively. The main panel shows hydrogen bonds and hydrophobic interactions surrounding AKT1 Ser473 and pSer473 with Insig1 (right). (F,G) Co‐IP analysis to assess AKT1–Insig1 interaction in the dTNF‐InSen NIH‐3T3 cells after transfection of Insig1 K140A vector under conditions of AKT1 WT overexpression or AKT1 S473A vector under the condition of Insig1 WT overexpression. (H,I) The expression of γ‐H2AX ( n = 60 per group), Il‐6 ( n = 3 per group), and Mmp13 ( n = 3 per group) in the dTNF‐InSen FLSs after the transfection of AKT1 WT or AKT1 S473A vector under the condition of Insig1 WT overexpression, compared to the controls. All statistical tests were two‐sided. Fisher's exact test (H). Student's t ‐test (I). dTNF‐InSen, induction of senescence by double treatment of TNF‐α; RMSD, protein backbone root mean square deviation; RMSF, root mean square fluctuation; FEL, free energy landscape; R g , radius of gyration.

    Article Snippet: The primary antibodies were as follows: HMGCR (Huabo, ET1702‐41), p16 (Abcam, ab189034), p53 (CST, 2524S), p21 (CST, 37543T), AKT1 (CST, 2938S), p‐AKT ser473 (ABclonal, AP0637), Insig1 (Santa, sc‐390504), phosphoserine/threonine (p‐Ser/Thr; BD Biosciences, 612549), SCAP (Proteintech, 12266‐1‐AP), IL‐6 (Proteintech, 26404‐1‐AP), MMP13 (Abcam, ab39012), Myc (CST, 2276), Flag (CST, 14793), β‐actin (Proteintech, 66009‐1‐AP).

    Techniques: Phospho-proteomics, Binding Assay, Immunoprecipitation, Solvent, Construct, Co-Immunoprecipitation Assay, Transfection, Plasmid Preparation, Over Expression, Expressing