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e2 enzyme  (R&D Systems)


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    Structured Review

    R&D Systems e2 enzyme
    PIP 2 and sHSPs regulate the ubiquitination function of MDM2. A , for MDM2 autoubiquitination, 100 nM of E1 enzyme, 1 μM of <t>E2</t> enzyme, 1 μM of MDM2, E3 ligase reaction buffer, 10 mM of MgATP solution and 100 μM of ubiquitin were incubated with different concentrations of αBC, HSP27 (0.9, 1.8, or 2.7 μM), or PIP 2 (10, 20, or 30 μM) for 1 h. Ubiquitin, MDM2, αBC and HSP27 were analyzed by IB, and ubiquitin IBs were quantified. The graphs are shown as mean ± s.d. of n = 3 independent experiments. B , for in vitro ubiquitination, 100 nM of E1 enzyme, 1 μM of E2 enzyme, 1 μM of His- and FLAG-tagged MDM2, E3 ligase reaction buffer, 10 mM of MgATP solution and 100 μM of ubiquitin were incubated with 1 μM of His- and FLAG-tagged p53 for 1 h. For IP, samples were incubated with anti-p53-conjugated agarose overnight. Ubiquitin, MDM2, and p53 were analyzed by IB, and ubiquitin IBs were quantified. The graphs are shown as mean ± s.d. of n = 3 independent experiments. C , MDA-MB-231 cells were transfected with siRNAs for PIPKIα and treated with vehicle or 30 μM cisplatin for 24 h. Empty vector (Mock) was used as a negative control. After cells were treated with 10 μM of MG132 for 4 h, cells were harvested for IP of MDM2 and p53. Expression of the indicated proteins was analyzed by IB, and ubiquitin IBs were quantified. The graph is shown as mean ± s.d. of n = 3 independent experiments. KD, knockdown; UT, untreated; Cis, cisplatin treated; Cis/MG132, Cisplatin/MG132 treated. D , MDA-MB-468 cells were transfected with siRNAs for αBC and HSP27 for 48 h in absence or presence of MG132. Empty vector (Mock) was used as a negative control. Cells were processed for IP of MDM2. IB was used to analyze indicated proteins, and ubiquitin IBs were quantified. The graphs are shown as mean ± s.d. of n = 3 independent experiments. KD, knockdown. E , a model of PIP 2 regulation of the interaction between MDM2 and sHSPs, which differentially control the stability of MDM2 and function of of MDM2. In the presence of PIPKIα, PIP 2 is linked to MDM2, which recruits αBC to MDM2 to stabilize it and enhances p53 binding. Conversely, in the absence of PIPKIα and PIP 2 , HSP27 is recruited to MDM2, which increases the ubiquitin E3 ligase activity of MDM2.
    E2 Enzyme, supplied by R&D Systems, used in various techniques. Bioz Stars score: 95/100, based on 52 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "Regulation of the MDM2-p53 nexus by a nuclear phosphoinositide and small heat shock protein complex"

    Article Title: Regulation of the MDM2-p53 nexus by a nuclear phosphoinositide and small heat shock protein complex

    Journal: The Journal of Biological Chemistry

    doi: 10.1016/j.jbc.2025.110527

    PIP 2 and sHSPs regulate the ubiquitination function of MDM2. A , for MDM2 autoubiquitination, 100 nM of E1 enzyme, 1 μM of E2 enzyme, 1 μM of MDM2, E3 ligase reaction buffer, 10 mM of MgATP solution and 100 μM of ubiquitin were incubated with different concentrations of αBC, HSP27 (0.9, 1.8, or 2.7 μM), or PIP 2 (10, 20, or 30 μM) for 1 h. Ubiquitin, MDM2, αBC and HSP27 were analyzed by IB, and ubiquitin IBs were quantified. The graphs are shown as mean ± s.d. of n = 3 independent experiments. B , for in vitro ubiquitination, 100 nM of E1 enzyme, 1 μM of E2 enzyme, 1 μM of His- and FLAG-tagged MDM2, E3 ligase reaction buffer, 10 mM of MgATP solution and 100 μM of ubiquitin were incubated with 1 μM of His- and FLAG-tagged p53 for 1 h. For IP, samples were incubated with anti-p53-conjugated agarose overnight. Ubiquitin, MDM2, and p53 were analyzed by IB, and ubiquitin IBs were quantified. The graphs are shown as mean ± s.d. of n = 3 independent experiments. C , MDA-MB-231 cells were transfected with siRNAs for PIPKIα and treated with vehicle or 30 μM cisplatin for 24 h. Empty vector (Mock) was used as a negative control. After cells were treated with 10 μM of MG132 for 4 h, cells were harvested for IP of MDM2 and p53. Expression of the indicated proteins was analyzed by IB, and ubiquitin IBs were quantified. The graph is shown as mean ± s.d. of n = 3 independent experiments. KD, knockdown; UT, untreated; Cis, cisplatin treated; Cis/MG132, Cisplatin/MG132 treated. D , MDA-MB-468 cells were transfected with siRNAs for αBC and HSP27 for 48 h in absence or presence of MG132. Empty vector (Mock) was used as a negative control. Cells were processed for IP of MDM2. IB was used to analyze indicated proteins, and ubiquitin IBs were quantified. The graphs are shown as mean ± s.d. of n = 3 independent experiments. KD, knockdown. E , a model of PIP 2 regulation of the interaction between MDM2 and sHSPs, which differentially control the stability of MDM2 and function of of MDM2. In the presence of PIPKIα, PIP 2 is linked to MDM2, which recruits αBC to MDM2 to stabilize it and enhances p53 binding. Conversely, in the absence of PIPKIα and PIP 2 , HSP27 is recruited to MDM2, which increases the ubiquitin E3 ligase activity of MDM2.
    Figure Legend Snippet: PIP 2 and sHSPs regulate the ubiquitination function of MDM2. A , for MDM2 autoubiquitination, 100 nM of E1 enzyme, 1 μM of E2 enzyme, 1 μM of MDM2, E3 ligase reaction buffer, 10 mM of MgATP solution and 100 μM of ubiquitin were incubated with different concentrations of αBC, HSP27 (0.9, 1.8, or 2.7 μM), or PIP 2 (10, 20, or 30 μM) for 1 h. Ubiquitin, MDM2, αBC and HSP27 were analyzed by IB, and ubiquitin IBs were quantified. The graphs are shown as mean ± s.d. of n = 3 independent experiments. B , for in vitro ubiquitination, 100 nM of E1 enzyme, 1 μM of E2 enzyme, 1 μM of His- and FLAG-tagged MDM2, E3 ligase reaction buffer, 10 mM of MgATP solution and 100 μM of ubiquitin were incubated with 1 μM of His- and FLAG-tagged p53 for 1 h. For IP, samples were incubated with anti-p53-conjugated agarose overnight. Ubiquitin, MDM2, and p53 were analyzed by IB, and ubiquitin IBs were quantified. The graphs are shown as mean ± s.d. of n = 3 independent experiments. C , MDA-MB-231 cells were transfected with siRNAs for PIPKIα and treated with vehicle or 30 μM cisplatin for 24 h. Empty vector (Mock) was used as a negative control. After cells were treated with 10 μM of MG132 for 4 h, cells were harvested for IP of MDM2 and p53. Expression of the indicated proteins was analyzed by IB, and ubiquitin IBs were quantified. The graph is shown as mean ± s.d. of n = 3 independent experiments. KD, knockdown; UT, untreated; Cis, cisplatin treated; Cis/MG132, Cisplatin/MG132 treated. D , MDA-MB-468 cells were transfected with siRNAs for αBC and HSP27 for 48 h in absence or presence of MG132. Empty vector (Mock) was used as a negative control. Cells were processed for IP of MDM2. IB was used to analyze indicated proteins, and ubiquitin IBs were quantified. The graphs are shown as mean ± s.d. of n = 3 independent experiments. KD, knockdown. E , a model of PIP 2 regulation of the interaction between MDM2 and sHSPs, which differentially control the stability of MDM2 and function of of MDM2. In the presence of PIPKIα, PIP 2 is linked to MDM2, which recruits αBC to MDM2 to stabilize it and enhances p53 binding. Conversely, in the absence of PIPKIα and PIP 2 , HSP27 is recruited to MDM2, which increases the ubiquitin E3 ligase activity of MDM2.

    Techniques Used: Ubiquitin Proteomics, Incubation, In Vitro, Transfection, Plasmid Preparation, Negative Control, Expressing, Knockdown, Control, Binding Assay, Activity Assay



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    Figure 7. Role of Siglecs in SARS-CoV-2 Spike capture. (A) Histograms show mean fluorescence of conjugated <t>recombinant</t> proteins and antibody on nanobeads that are coated with indicated SARS-CoV-2 Spike proteins. Background signal (weak gray) measured with uncoated beads. No protein (gray) means that uncoated beads were incubated with indicated labeled recombinant protein or antibody. (B) Flow cytometry assessment of indicated Spike proteins binding to HEK293 cell permanently transfected with angiotensin converting enzyme II <t>(ACE2),</t> various Siglecs, or a combination. Dual transfected HEK293 cells noted as Siglec-5/8+, ACE2/Siglec-5+, and ACE2/Siglec-8+. Labeled recombinant proteins were incubated with 5×103 HEK293 cells on ice for 30 min. Data shown as mean fluorescent intensity. (C) DIC and confocal micrographs showing SARS-CoV-2 Spike (Trimer, red) protein acquisition by human Siglec-5-GFP transfected HEK293. ROI-1 in the middle panel is enlarged at the right panel. A 3D-reconstituted volume image of Siglec-5 transfected cell (far right) shows Siglec-5-mediated Spike protein acquisition. Scale bars, 30 and 10 μm. (D) DIC and confocal images show SARSCoV-2 Spike protein acquisition by human Siglec-5-GFP or ACE2-OFP transfected HEK293. Equal numbers of stable transfectants expressing Siglec-5-GFP or ACE2-OFP, and non-transfectant were seeded together. Spike protein (Trimer, blue) was added 1 hr prior to imaging. In a region of
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    PIP 2 and sHSPs regulate the ubiquitination function of MDM2. A , for MDM2 autoubiquitination, 100 nM of E1 enzyme, 1 μM of <t>E2</t> enzyme, 1 μM of MDM2, E3 ligase reaction buffer, 10 mM of MgATP solution and 100 μM of ubiquitin were incubated with different concentrations of αBC, HSP27 (0.9, 1.8, or 2.7 μM), or PIP 2 (10, 20, or 30 μM) for 1 h. Ubiquitin, MDM2, αBC and HSP27 were analyzed by IB, and ubiquitin IBs were quantified. The graphs are shown as mean ± s.d. of n = 3 independent experiments. B , for in vitro ubiquitination, 100 nM of E1 enzyme, 1 μM of E2 enzyme, 1 μM of His- and FLAG-tagged MDM2, E3 ligase reaction buffer, 10 mM of MgATP solution and 100 μM of ubiquitin were incubated with 1 μM of His- and FLAG-tagged p53 for 1 h. For IP, samples were incubated with anti-p53-conjugated agarose overnight. Ubiquitin, MDM2, and p53 were analyzed by IB, and ubiquitin IBs were quantified. The graphs are shown as mean ± s.d. of n = 3 independent experiments. C , MDA-MB-231 cells were transfected with siRNAs for PIPKIα and treated with vehicle or 30 μM cisplatin for 24 h. Empty vector (Mock) was used as a negative control. After cells were treated with 10 μM of MG132 for 4 h, cells were harvested for IP of MDM2 and p53. Expression of the indicated proteins was analyzed by IB, and ubiquitin IBs were quantified. The graph is shown as mean ± s.d. of n = 3 independent experiments. KD, knockdown; UT, untreated; Cis, cisplatin treated; Cis/MG132, Cisplatin/MG132 treated. D , MDA-MB-468 cells were transfected with siRNAs for αBC and HSP27 for 48 h in absence or presence of MG132. Empty vector (Mock) was used as a negative control. Cells were processed for IP of MDM2. IB was used to analyze indicated proteins, and ubiquitin IBs were quantified. The graphs are shown as mean ± s.d. of n = 3 independent experiments. KD, knockdown. E , a model of PIP 2 regulation of the interaction between MDM2 and sHSPs, which differentially control the stability of MDM2 and function of of MDM2. In the presence of PIPKIα, PIP 2 is linked to MDM2, which recruits αBC to MDM2 to stabilize it and enhances p53 binding. Conversely, in the absence of PIPKIα and PIP 2 , HSP27 is recruited to MDM2, which increases the ubiquitin E3 ligase activity of MDM2.
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    Figure 7. Role of Siglecs in SARS-CoV-2 Spike capture. (A) Histograms show mean fluorescence of conjugated recombinant proteins and antibody on nanobeads that are coated with indicated SARS-CoV-2 Spike proteins. Background signal (weak gray) measured with uncoated beads. No protein (gray) means that uncoated beads were incubated with indicated labeled recombinant protein or antibody. (B) Flow cytometry assessment of indicated Spike proteins binding to HEK293 cell permanently transfected with angiotensin converting enzyme II (ACE2), various Siglecs, or a combination. Dual transfected HEK293 cells noted as Siglec-5/8+, ACE2/Siglec-5+, and ACE2/Siglec-8+. Labeled recombinant proteins were incubated with 5×103 HEK293 cells on ice for 30 min. Data shown as mean fluorescent intensity. (C) DIC and confocal micrographs showing SARS-CoV-2 Spike (Trimer, red) protein acquisition by human Siglec-5-GFP transfected HEK293. ROI-1 in the middle panel is enlarged at the right panel. A 3D-reconstituted volume image of Siglec-5 transfected cell (far right) shows Siglec-5-mediated Spike protein acquisition. Scale bars, 30 and 10 μm. (D) DIC and confocal images show SARSCoV-2 Spike protein acquisition by human Siglec-5-GFP or ACE2-OFP transfected HEK293. Equal numbers of stable transfectants expressing Siglec-5-GFP or ACE2-OFP, and non-transfectant were seeded together. Spike protein (Trimer, blue) was added 1 hr prior to imaging. In a region of

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    Figure Lengend Snippet: Figure 7. Role of Siglecs in SARS-CoV-2 Spike capture. (A) Histograms show mean fluorescence of conjugated recombinant proteins and antibody on nanobeads that are coated with indicated SARS-CoV-2 Spike proteins. Background signal (weak gray) measured with uncoated beads. No protein (gray) means that uncoated beads were incubated with indicated labeled recombinant protein or antibody. (B) Flow cytometry assessment of indicated Spike proteins binding to HEK293 cell permanently transfected with angiotensin converting enzyme II (ACE2), various Siglecs, or a combination. Dual transfected HEK293 cells noted as Siglec-5/8+, ACE2/Siglec-5+, and ACE2/Siglec-8+. Labeled recombinant proteins were incubated with 5×103 HEK293 cells on ice for 30 min. Data shown as mean fluorescent intensity. (C) DIC and confocal micrographs showing SARS-CoV-2 Spike (Trimer, red) protein acquisition by human Siglec-5-GFP transfected HEK293. ROI-1 in the middle panel is enlarged at the right panel. A 3D-reconstituted volume image of Siglec-5 transfected cell (far right) shows Siglec-5-mediated Spike protein acquisition. Scale bars, 30 and 10 μm. (D) DIC and confocal images show SARSCoV-2 Spike protein acquisition by human Siglec-5-GFP or ACE2-OFP transfected HEK293. Equal numbers of stable transfectants expressing Siglec-5-GFP or ACE2-OFP, and non-transfectant were seeded together. Spike protein (Trimer, blue) was added 1 hr prior to imaging. In a region of

    Article Snippet: (species) or resource Designation Source or reference Identifiers Additional information Recombinant DNA reagent SIGLEC5 (NM_003830) Human Tagged ORF Clone Origene RG206610 Recombinant DNA reagent Human Siglec- 8 (NP_055257) VersaClone cDNA Origene RDC1496 Recombinant DNA reagent SARS- CoV- 2 Spike- S Addgene Plasmid # 154754 Hsieh et al., 2020 Recombinant DNA reagent HIV- 1 NL4- 3 Gag- iGFP ΔEnv NIH AIDS Reagent Program 12455 Recombinant DNA reagent Human Coronavirus Spike glycoprotein Gene ORF cDNA clone expression plasmid (Codon Optimized) HCoVHKU1 SinoBiological VG40021- UT Recombinant DNA reagent Human coronavirus (HCoV- 229E) Spike Gene ORF cDNA clone expression plasmid (Codon Optimized) HCoV- 229E SinoBiological VG40605- UT Recombinant DNA reagent ACE2 cDNA ORF Clone, Human, C- OFPSpark tag SinoBiological HG10108- ACR Recombinant DNA reagent pCMV- dR8.2 dvpr Addgene 8455 Recombinant DNA reagent pLentipuro3 TO V5- GW EGFP- Firefly Luciferase Addgene 119816 Peptide, recombinant protein ACE2 Protein, Human, Recombinant (mFc Tag) SinoBiological 10108- H05H Peptide, recombinant protein Human coronavirus HKU1 (isolate N5) (HCoV- HKU1) Spike/S1 Protein (S1 Subunit, His Tag) SinoBiological 40602- V08H Peptide, recombinant protein Human coronavirus (HCoV- 229E) Spike Protein (S1+S2 ECD, His Tag) SinoBiological 40605- V08B Peptide, recombinant protein SIGLEC5 Protein, Human, Recombinant (hFc Tag) SinoBiological 11798- H02H Peptide, recombinant protein Recombinant Mouse Siglec- F Fc Chimera Protein, CF R&D Systems 1706- SF- 050 Peptide, recombinant protein Recombinant Human Siglec- 8 Fc Chimera Protein, CF R&D Systems 9045- SL- 050 Strain, strain background (mouse) C57BL/6J Jackson Lab. IMSR_JAX:000664 Jax stock 000664 Strain, strain background (mouse) K18- hACE2 (B6.Cg- Tg(K18- ACE2) 2Prlmn/J) Jackson Lab. IMSR_JAX:034860 Jax stock 034860 Other Liberase TL(Thermolysin Low) Research Grade Roche Applied Science 5401020001 Enzyme Other Opti- MEM Thermo Fisher Scientific Inc. 31985070 Cell culture media Other RPMI 1640 Media Thermo Fisher Scientific Inc. 11875093 Cell culture media Other TransIT- 293 Transfection Reagent Mirus Bio LLC MIR 2704 Cell culture media Other FreeStyle 293 Expression Medium Thermo Fisher Scientific Inc. 12338018 Cell culture media Other FreeStyle CHO Expression Medium Thermo Fisher Scientific Inc. 12651014 Cell culture media Continued

    Techniques: Fluorescence, Recombinant, Incubation, Labeling, Flow Cytometry, Binding Assay, Transfection, Expressing, Imaging

    PIP 2 and sHSPs regulate the ubiquitination function of MDM2. A , for MDM2 autoubiquitination, 100 nM of E1 enzyme, 1 μM of E2 enzyme, 1 μM of MDM2, E3 ligase reaction buffer, 10 mM of MgATP solution and 100 μM of ubiquitin were incubated with different concentrations of αBC, HSP27 (0.9, 1.8, or 2.7 μM), or PIP 2 (10, 20, or 30 μM) for 1 h. Ubiquitin, MDM2, αBC and HSP27 were analyzed by IB, and ubiquitin IBs were quantified. The graphs are shown as mean ± s.d. of n = 3 independent experiments. B , for in vitro ubiquitination, 100 nM of E1 enzyme, 1 μM of E2 enzyme, 1 μM of His- and FLAG-tagged MDM2, E3 ligase reaction buffer, 10 mM of MgATP solution and 100 μM of ubiquitin were incubated with 1 μM of His- and FLAG-tagged p53 for 1 h. For IP, samples were incubated with anti-p53-conjugated agarose overnight. Ubiquitin, MDM2, and p53 were analyzed by IB, and ubiquitin IBs were quantified. The graphs are shown as mean ± s.d. of n = 3 independent experiments. C , MDA-MB-231 cells were transfected with siRNAs for PIPKIα and treated with vehicle or 30 μM cisplatin for 24 h. Empty vector (Mock) was used as a negative control. After cells were treated with 10 μM of MG132 for 4 h, cells were harvested for IP of MDM2 and p53. Expression of the indicated proteins was analyzed by IB, and ubiquitin IBs were quantified. The graph is shown as mean ± s.d. of n = 3 independent experiments. KD, knockdown; UT, untreated; Cis, cisplatin treated; Cis/MG132, Cisplatin/MG132 treated. D , MDA-MB-468 cells were transfected with siRNAs for αBC and HSP27 for 48 h in absence or presence of MG132. Empty vector (Mock) was used as a negative control. Cells were processed for IP of MDM2. IB was used to analyze indicated proteins, and ubiquitin IBs were quantified. The graphs are shown as mean ± s.d. of n = 3 independent experiments. KD, knockdown. E , a model of PIP 2 regulation of the interaction between MDM2 and sHSPs, which differentially control the stability of MDM2 and function of of MDM2. In the presence of PIPKIα, PIP 2 is linked to MDM2, which recruits αBC to MDM2 to stabilize it and enhances p53 binding. Conversely, in the absence of PIPKIα and PIP 2 , HSP27 is recruited to MDM2, which increases the ubiquitin E3 ligase activity of MDM2.

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    Article Title: Regulation of the MDM2-p53 nexus by a nuclear phosphoinositide and small heat shock protein complex

    doi: 10.1016/j.jbc.2025.110527

    Figure Lengend Snippet: PIP 2 and sHSPs regulate the ubiquitination function of MDM2. A , for MDM2 autoubiquitination, 100 nM of E1 enzyme, 1 μM of E2 enzyme, 1 μM of MDM2, E3 ligase reaction buffer, 10 mM of MgATP solution and 100 μM of ubiquitin were incubated with different concentrations of αBC, HSP27 (0.9, 1.8, or 2.7 μM), or PIP 2 (10, 20, or 30 μM) for 1 h. Ubiquitin, MDM2, αBC and HSP27 were analyzed by IB, and ubiquitin IBs were quantified. The graphs are shown as mean ± s.d. of n = 3 independent experiments. B , for in vitro ubiquitination, 100 nM of E1 enzyme, 1 μM of E2 enzyme, 1 μM of His- and FLAG-tagged MDM2, E3 ligase reaction buffer, 10 mM of MgATP solution and 100 μM of ubiquitin were incubated with 1 μM of His- and FLAG-tagged p53 for 1 h. For IP, samples were incubated with anti-p53-conjugated agarose overnight. Ubiquitin, MDM2, and p53 were analyzed by IB, and ubiquitin IBs were quantified. The graphs are shown as mean ± s.d. of n = 3 independent experiments. C , MDA-MB-231 cells were transfected with siRNAs for PIPKIα and treated with vehicle or 30 μM cisplatin for 24 h. Empty vector (Mock) was used as a negative control. After cells were treated with 10 μM of MG132 for 4 h, cells were harvested for IP of MDM2 and p53. Expression of the indicated proteins was analyzed by IB, and ubiquitin IBs were quantified. The graph is shown as mean ± s.d. of n = 3 independent experiments. KD, knockdown; UT, untreated; Cis, cisplatin treated; Cis/MG132, Cisplatin/MG132 treated. D , MDA-MB-468 cells were transfected with siRNAs for αBC and HSP27 for 48 h in absence or presence of MG132. Empty vector (Mock) was used as a negative control. Cells were processed for IP of MDM2. IB was used to analyze indicated proteins, and ubiquitin IBs were quantified. The graphs are shown as mean ± s.d. of n = 3 independent experiments. KD, knockdown. E , a model of PIP 2 regulation of the interaction between MDM2 and sHSPs, which differentially control the stability of MDM2 and function of of MDM2. In the presence of PIPKIα, PIP 2 is linked to MDM2, which recruits αBC to MDM2 to stabilize it and enhances p53 binding. Conversely, in the absence of PIPKIα and PIP 2 , HSP27 is recruited to MDM2, which increases the ubiquitin E3 ligase activity of MDM2.

    Article Snippet: For the in vitro ubiquitination assay targeting MDM2 autoubiquitination, 100 nM of E1 enzyme (#E304, R&D Systems), 1 μM of E2 enzyme (#E2627, R&D Systems), 1 μM of MDM2, E3 ligase reaction buffer (#B71, R&D Systems), 10 mM of MgATP solution (#B20, R&D Systems) and 100 μM of ubiquitin (#U100H, R&D Systems) were incubated with different concentrations of αBC, HSP27 (0.9, 1.8, or 2.7 μM), or PIP 2 (10, 20, or 30 μM).

    Techniques: Ubiquitin Proteomics, Incubation, In Vitro, Transfection, Plasmid Preparation, Negative Control, Expressing, Knockdown, Control, Binding Assay, Activity Assay

    Journal: iScience

    Article Title: Trichinella spiralis inhibits myoblast differentiation by targeting SQSTM1/p62 with a secreted E3 ubiquitin ligase

    doi: 10.1016/j.isci.2024.109102

    Figure Lengend Snippet:

    Article Snippet: Ubiquitin E2 Enzyme UbcH7 , Boston Biochem, USA , Cat#E2-640.

    Techniques: Recombinant, Ubiquitin Proteomics, Conjugation Assay, Transfection, Plasmid Preparation, Software