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Sumoylation

Sumoylation is a post-translational modification process in which the Small Ubiquitin-like Modifier (SUMO) protein is covalently attached to target proteins.
This dynamic and reversible process plays a crucial role in regulating protein function, localization, and stability.
Sumoylation is invloved in diverse cellular processes, including transcription, DNA repair, cell cycle progression, and stress response.
Disruption of sumoylation has been implicated in the pathogenesis of various diseases, making it an important area of biomedical research.
Understanding the mechanisms and implications of sumoylation is crucial for developing effective therapeutic interventions targeting this critical regulatory system.

Most cited protocols related to «Sumoylation»

1
Quantifying Protein-Protein Interactions via FRET
Recombinant CyPet–SUMO1 and YPet–Ubc9 proteins were mixed and diluted with phosphate buffered saline (PBS) to a total volume of 30 μL. The final concentration of CyPet–SUMO1 was fixed to 1 μM and the final concentration of YPet–Ubc9 varied from 0 to 4 μM. The mixtures were transferred into a 384-well plate (Falcon) and the fluorescence emission spectrum of each well was measured with a fluorescence multi-well plate reader (Molecular Devices, FlexstationII384). Two excitation wavelengths were used: 414 nm to excite CyPet, and 475 nm to excite YPet. Excited at 414 nm, CyPet has an emission peak at 475 nm (FLDD) (see Fig. 2). With FRET, another emission peak at 530 nm (Emtotal) can be observed which results from the energy transferred from CyPet to YPet. When the mixture is excited at 475 nm, an emission peak at 530 nm (FLAA) can be observed which is from the direct excitation of YPet but not CyPet.

Design and detection of high sensitive FRET-based detection for protein interactions in sumoylation conjugation cascade. (a) The diagram of FRET-based detection of SUMO1 and its E2 ligase, Ubc9, interaction. (b) Emission spectra of protein mixtures with [CyPet–SUMO1] fixed as 1 μM and [YPet–Ubc9] increased from 0 to 7.5 μM. Excitation wavelength is 414 nm

When a mixture of CyPet–SUMO1 and YPet–Ubc9 recombinant proteins was excited at 414 nm, the emission intensity at 530 nm was consisted of three components: the direct emission of CyPet, the sensitized emission of YPet and the direct emission of YPet. Because the sensitized emission from YPet–Ubc9 (EmFRET) is proportional to the amount of YPet–Ubc9 bound to CyPet–SUMO1 ([YPetUbc9]bound), we can convert the concentration of YPet–Ubc9 in both free ([YPetUbc9]free) and bound ([YPetUbc9]bound) forms to functions of EmFRET. Therefore, we can derive the relationship between EmFRET and the total concentration of YPet–Ubc9 ([YPetUbc9]total), and calculate the Kd between CyPet–SUMO1 and YPet–Ubc9 based on the algorithm we developed. Data were processed in Prism 5 (GraphPad Software).
Song Y., Madahar V, & Liao J. (2010). Development of FRET Assay into Quantitative and High-throughput Screening Technology Platforms for Protein–Protein Interactions. Annals of Biomedical Engineering, 39(4), 1224-1234.
Publication 2010
Fluorescence Fluorescence Resonance Energy Transfer Ligase Medical Devices Phosphates prisma protein B Proteins Recombinant Proteins Saline Solution SUMO1 protein, human Sumoylation TYRP1 protein, human
2
Bioinformatics Analysis of Disordered CTA Proteins
Disorder predictions in the CTAs were done applying the Foldindex [Prilusky et al., 2005 (link)] and RONN [Yang et al., 2005 (link)] algorithms and in some cases, metaPrDOS [Ishida and Kinoshita, 2008 (link)] was also employed in addition. To discern the effect of helical regions on protein disorder prediction, we compiled data using psiPred (http://bioinf.cs.ucl.ac.uk/psipred/) and JPred (http://www.compbio.dundee.ac.uk/www-jpred/) on a set of CT-X and non-X CTAs selected randomly before and after masking these regions. However, we found no difference in the prediction results presumably due to the paucity of helical regions in the disordered portions and therefore, we did not mask them in any of the analyses presented here. Based on the fraction of the sequence that was predicted to be disordered, we classified the CT-X and non-X CTAs into one of three classes: Highly ordered, (0–10% of the sequence is disordered), moderately disordered, (11%–30% of the sequence is disordered) and highly disordered (31%–100% of the sequence is disordered). To normalize for the varying protein lengths, we calculated the number of sequence motifs per 100 amino acids. PEST motifs were predicted using the epestfind algorithm of the EMBOSS package (http://emboss.bioinformatics.nl/cgi-bin/emboss/epestfind). Only motifs with a threshold PEST score >5 were considered. Ubiquitylation sites were predicted using UbPred [Radivojac et al., 2010 (link)]. Only the ubiquitylation sites with a high confidence score (range 0.84 ≥ s ≤ 1.00) were considered. CTAs with percent ubiquitylation having a minimum value of 2, was used as a cutoff. Phosphorylation sites were predicted using KinasePhos 2.0 [Wong et al., 2007 (link)] which predicts the location of phosphorylation sites on S, T and Y residues with a prediction specificity of 100%. CTAs with per cent phosphorylation having a minimum value of 2, was used as a cutoff. Acetylation sites were predicted using PAIL [Li et al., 2006 (link)] which predicts the acetylation sites on lysine residues with a high stringency and threshold score ≥0.5. Again, CTAs with percent acetylation having a minimum value of 3 was used as a cutoff. The probability to bind DNA was predicted using DBSPred [Ahmad et al., 2004 (link)] with a sensitivity setting of ‘strict’. Arginine methylation sites were predicted using MEMO [Chen et al., 2006 (link)] and sumoylation sites were predicted using SUMOsp 2.0 [Ren et al., 2009 (link)]. Protein–protein interactions were predicted using the STRING interaction database [Jensen et al., 2009 (link)] at medium confidence setting (0.4-0.7) with no more than 10 interactions. The statistical analyses used to estimate significance were, Wilcoxon rank-sum, two sample T test, and Chi square test as described in the text. The TATA box in the CTA promoter regions and specific sequence motifs in the mRNAs representing various polyadenylation and stability signals were searched by writing PERL scripts for each motif. Data in the CIRCOS plots were displayed by employing specific PERL scripts.
Rajagopalan K., Mooney S.M., Parekh N., Getzenberg R.H, & Kulkarni P. (2011). A Majority of the Cancer/Testis Antigens are Intrinsically Disordered Proteins. Journal of cellular biochemistry, 112(11), 3256-3267.
Publication 2011
Acetylation Amino Acids Arginine Helix (Snails) Hypersensitivity Lysine Methylation Phosphorylation Plague Polyadenylation Proteins RNA, Messenger Sumoylation TATA Box Ubiquitination
3
Immunoblotting for Protein SUMOylation
Cells were harvested, washed twice with 1× D-PBS (Sigma-Aldrich), and pelleted for protein extraction by using 1× radioimmunoprecipitation assay (RIPA) buffer (Upstate, EMD Millipore) containing broad-spectrum protease inhibitors (Thermo Fisher Scientific). Protein concentrations were determined by a BCA protein assay kit (Thermo Fisher Scientific), followed by the electrophoresis on 4 to 20% Tris-Glycine mini gels (Invitrogen). The separated proteins were then transferred to PVDF membranes by an iBlot 2 system (Invitrogen). The membranes were blocked with nonfat milk and incubated overnight with primary antibodies at 4°C with constant rocking. The membranes were washed with 1× PBS-Tween (PBST) and further incubated with secondary antibodies. The membranes were thoroughly washed with 1× PBST and incubated with Clarity Max Western ECL Substrate (Bio-Rad). The immunoblotting images were captured by a FluorChem E imaging system (ProteinSimple). An AlphaView software was used to quantify the intensity of protein bands, which were normalized to the internal loading controls. To determine the PLK1 SUMOylation, endogenous PLK1 was IPed. Pierce Protein A/G Magnetic Beads (Thermo Fisher Scientific) were prewashed with 1× RIPA buffer containing broad-spectrum protease inhibitors. Cellular lysates were precleared with empty magnetic beads for 1 hour at 4°C on a 360° tube rocker. Anti-PLK1 or control IgG antibody was mixed with cellular lysates for incubation overnight at 4°C with constant rotation. New prewashed magnetic beads were added into cellular lysates for another incubation at 4°C for 1 hour with rotation, followed by the centrifugation to collect magnetic beads. Beads containing protein immunocomplexes were washed and subjected to immunoblotting.
Zhou D., Hayashi T., Jean M., Kong W., Fiches G., Biswas A., Liu S., Yosief H.O., Zhang X., Bradner J., Qi J., Zhang W., Santoso N, & Zhu J. (2020). Inhibition of Polo-like kinase 1 (PLK1) facilitates the elimination of HIV-1 viral reservoirs in CD4+ T cells ex vivo. Science Advances, 6(29), eaba1941.
Publication 2020
Antibodies Biological Assay Buffers Cells Centrifugation Electrophoresis G-substrate Gels Glycine Immunoglobulin G Milk, Cow's PLK1 protein, human polyvinylidene fluoride Protease Inhibitors Proteins Radioimmunoprecipitation Assay Staphylococcal Protein A Sumoylation Tissue, Membrane Tromethamine Tweens
4
Quantitative SUMO Conjugation Kinetics
SUMO can be conjugated to many substrates using only E1 and E2 (Ubc9) in the presence of SUMO, the substrate, magnesium, and ATP. These assays contain a complex mixture of reagents, and each reactant must interact with at least one or more of the other reactants. As such, extraction of relevant kinetic parameters during substrate conjugation remains difficult under conditions of multiple turnover. To address this issue, we have utilized single turnover assays for SUMO conjugation. This is achieved by isolating Ubc9~SUMO (where ‘~’ indicates a thioester adduct) in the absence of E3 and substrate using E1, E2, SUMO and ATP. In this section we describe the methods to conduct single turnover assays using Ubc9~SUMO in conjunction with substrate titrations in the presence or absence of an E3 ligase. We will also describe methods to determine pK values during conjugation. In addition, we will describe methodologies to extract kinetic parameters from these assays.
Yunus A.A, & Lima C.D. (2009). Purification of SUMO conjugating enzymes and kinetic analysis of substrate conjugation. Methods in molecular biology (Clifton, N.J.), 497, 167-186.
Publication 2009
Biological Assay Cell Motility Assays Complex Mixtures Kinetics Ligase, Ubiquitin-Protein Magnesium Sumoylation Titrimetry
5
Cultivation and Characterization of Macrophage and DC Lines
RAW 264.7 (RAW), NIH3T3, and 293T cells (American Type Culture Collection) were maintained in DMEM with 10% FBS or 10% donor serum (for NIH3T3). IRF8−/− macrophage cell line, CL2 cells were cultured in RPMI 1640 and 10% FBS plus rM-CSF (5 ng/ml) (32 (link)). Bone marrow (BM)-derived macrophages were obtained by culturing BM mononuclear cells in the presence of 20 ng/ml M-CSF (Invitrogen) for 5–6 d. BM-derived IRF8−/− DCs were cultured in the presence of Flt3L for ∼4 wk. These cells exhibited a DC progenitor-like property and differentiated into DCs after IRF8 transduction. Detailed procedures and the properties of these DCs will be presented elsewhere (P. Tailor, unpublished observations). Procedures for quantitative RT-PCR (qRT-PCR), in vivo SUMOylation, and coimmunoprecipitation assays were performed, as described (19 (link)).
Chang T.H., Xu S., Tailor P., Kanno T, & Ozato K. (2012). The Small Ubiquitin-like Modifier-Deconjugating Enzyme Sentrin-Specific Peptidase 1 Switches IFN Regulatory Factor 8 from a Repressor to an Activator during Macrophage Activation. Journal of immunology (Baltimore, Md. : 1950), 189(7), 3548-3556.
Publication 2012
Biological Assay Bone Marrow Bone Marrow Cells Cell Lines Cells Co-Immunoprecipitation HEK293 Cells interferon regulatory factor-8 Macrophage Macrophage Colony-Stimulating Factor NIH 3T3 Cells Reverse Transcriptase Polymerase Chain Reaction Serum Sumoylation Tissue Donors

Most recents protocols related to «Sumoylation»

1
PROX1 Sumoylation Assay Protocol
The cells were lysed with the appropriate volume of Pierce™ IP Lysis Buffer (Thermo Fisher Scientific) supplemented with 1X PIC and 1X PMSF and 25 mM of N-ethylmaleimide (NEM) (Thermo Fisher Scientific). Lysates were placed on ice for 10 min and centrifuged at 4 °C for 15 min at 15,000× g to collect protein lysates. For immunoprecipitation, 500 µL of cell lysate (1 mg/mL) was diluted with the Pierce™ IP Lysis Buffer supplemented with PIC, PMSF, and NEM and incubated with PROX1 antibody (Cell Signaling Technology, Danvers, MA, USA) and as the control normal rabbit IgG (Cell Signaling Technology) overnight at 4 °C with rotation. After overnight incubation, 50 mL of protein A/G agarose beads were washed twice with the IP lysis buffer, were added to each sample, and incubated at room temperature for 2 h with gentle rotation, followed by elution with IgG Elution Buffer (ThermoScientific). As described above, the eluted samples were run in 12%, Bis-Tris, 1.0 mm, Mini Protein Gel. The PROX1 SUMOylation was detected by probing the blot with an anti-SUMO1 antibody (Cell Signaling Technology) [17 (link)].
Banerjee P., Kumaravel S., Roy S., Gaddam N., Odeh J., Bayless K.J., Glaser S, & Chakraborty S. (2023). Conjugated Bile Acids Promote Lymphangiogenesis by Modulation of the Reactive Oxygen Species–p90RSK–Vascular Endothelial Growth Factor Receptor 3 Pathway. Cells, 12(4), 526.
Publication 2023
Antibodies, Anti-Idiotypic Bistris Buffers Cells Ethylmaleimide G-substrate GTP-Binding Proteins Immunoglobulins Immunoprecipitation Proteins Rabbits Sepharose Staphylococcal Protein A SUMO1 protein, human Sumoylation
2
Immunization of BALB/c Mice with JUNV VLP
Groups of seven female BALB/c mice were purchased from Charles River UK at 5 weeks of age. Mice were housed for 2 weeks before the initiation of experimental procedures, at which point samples of preimmune sera were collected (approximately 50 μL total blood volume) via the tail vein. Mice were then immunized three times at 2-week intervals subcutaneously in the rear upper flank with a total volume of 100 μL per dose. Vaccines were composed of 1 μg of VLP (HBcAg or VelcroVax) (Fig. S6) and 1 μg of JUNV gp1 in the presence of 2.5 nmol of the murine TLR9-stimulatory molecule CpG ODN1668 (Invivogen). Samples were assembled 24 h preimmunization to facilitate SUMO-linked conjugation of JUNV gp1 to VLP and stored at 4°C until used. All vaccine components were tested for endotoxin content and immunizations contained less than 2.5 EU/dose (Pierce LAL Chromogenic Endotoxin Quantitation kit; Thermo Scientific). Serum samples were collected on days 13 and 27 (as above) (Fig. S5). On day 41, final blood samples were taken via cardiac puncture while mice were euthanized under sodium pentobarbitone. All animals were housed under specific pathogen-free conditions and monitored for well-being. All animal procedures were performed in strict accordance with UK Home Office guidelines, under license PP2876504 granted by the Secretary of State for the Home Office, which approved the work described, in accordance with local ethical guidelines and internal committee approval for animal welfare at NIBSC. This study conforms to all relevant ethical regulations for animal work in the United Kingdom. We elected to use seven animals in this trial due to the sensitivity of our assays to detect minor differences in immune outcomes between animals, and the moderate variability of responses generated within immunization groups, offering good statistical power and minimizing animal use.
Kingston N.J., Grehan K., Snowden J.S., Hassall M., Alzahrani J., Paesen G.C., Sherry L., Hayward C., Roe A., Stephen S., Tomlinson D., Zeltina A., Doores K.J., Ranson N.A., Stacey M., Page M., Rose N.J., Bowden T.A., Rowlands D.J, & Stonehouse N.J. (2023). VelcroVax: a “Bolt-On” Vaccine Platform for Glycoprotein Display. mSphere, 8(1), e00568-22.
Publication 2023
Animals azo rubin S Biological Assay BLOOD Blood Volume Endotoxins Females Heart Hepatitis B Core Antigen Hypersensitivity Immunization Mice, House Mice, Inbred BALB C Mus Pentobarbital Sodium Punctures Rivers Serum Specific Pathogen Free Sumoylation Tail Vaccination Vaccines Veins
3
Quantifying Sumoylation Using Western Blot
Protein samples were analyzed by standard polyacrylamide gel electrophoresis (PAGE) techniques. For preferential detection of high-molecular weight SUMO conjugates, PAGE was performed with lysates followed by wet transfer (100 V for 1 h) in a buffer consisting of 0.1% SDS, 10% methanol, 50 mM Tris-HCl, and 380 mM glycine. For preferential detection of free SUMO and lower molecular-weight SUMO conjugates, TCA extracts were analyzed by PAGE, followed by semi-dry transfer using a Power Blotter system (Thermo Fisher). Chemiluminescence-based imaging was performed using the MicroChemi imager (DNR). For quantification of signals, TIFF-format images were analyzed using ImageJ software (version 1.52a; NIH). Specifically for determining sumoylation levels, all SUMO signals (above the Ubc9-SUMO band, if it was present) were considered SUMO conjugates, and normalization was made to the corresponding signal from GAPDH immunoblots. Antibodies used for immunoblot analyses were: 1:500–1:1000 SUMO/Smt3 (y-84; Santa Cruz, sc-28649); 1:3000 GAPDH (Sigma, G9545); 1:500 Ubc9 (Santa Cruz, sc-6721); 1:3000 histone H3 (Abcam, ab1791); 1:1000 Myc epitope tag (Sigma, 05-724); 1:1000 Rpb3 (Abcam, ab202893); 1:5000 HA (12CA5; Sigma, 11583816001). The RPL3 antibody, which we used at a dilution of 1:200, was deposited to the DSHB by Warner, J. R. (DSHB Hybridoma Product ScRPL3 supernatant).
Moallem M., Akhter A., Burke G.L., Babu J., Bergey B.G., McNeil J.B., Baig M.S, & Rosonina E. (2023). Sumoylation is Largely Dispensable for Normal Growth but Facilitates Heat Tolerance in Yeast. Molecular and Cellular Biology, 43(1), 64-84.
Publication 2023
Antibodies Buffers Chemiluminescence Epitopes GAPDH protein, human Glycine Histone H3 Hybridomas Immunoblotting Immunoglobulins Methanol Polyacrylamide Gel Electrophoresis Proteins Sumoylation Technique, Dilution Tromethamine
4
Murine Macrophage Activation and SUMOylation Modulation
Recombinant murine LPS (L4130) and recombinant murine M-CSF (catalog 315-02-250) were from PeproTech (Wuhan, China). Ovalbumin (OVA 257–264; catalog S7951) was from Sigma-Aldrich. Anti-STAT4 (2653S), anti-FLAG (catalog 2368), and anti-ubiquitin (catalog 3936s) were from Cell Signaling Technology. Anti-CD8 (catalog ab217344) and anti-UBC9 (catalog ab75854) were from Abcam. Anti-CD68 (catalog 66231-2-Ig) was from Proteintech (Wuhan, China). Anti-SUMO1 was from Youke Group (Shanghai, China). BV510–anti–mouse CD45.2 (catalog 109837), FITC–anti–mouse F4/80 (catalog 123108), PE–anti–mouse CD11b (catalog 101208), BV421–anti–mouse F4/80 (catalog 123132), PE/Cy7–anti–mouse CD86 (catalog 105014), APC–anti–mouse MHC I (catalog 116418), FITC–anti–mouse MHC II (catalog 107606), FITC–anti–mouse CD4 (catalog 100406), PE/Cy7–anti–mouse CD8 (catalog 140416), APC–anti–mouse PD-1 (catalog 135210), APC–anti–mouse IFN-γ (catalog 505810), BV421–anti–mouse TNF-α (catalog 506327), APC–anti–mouse granzyme B (catalog 372204), and PE–anti–mouse Ki67 (catalog 151210) were from BioLegend. Dynabeads Protein G (catalog 1004d) was purchased from Invitrogen. N-Ethylmaleimide (catalog 23030.0) was purchased from Sigma-Aldrich. The GFP-labeled Stat4-WT (FLAG tagged), Stat4-K350R (FLAG tagged), and Ubc9-overexpressing adenoviruses were from Dianjun Biotech Co. Ltd. Percoll (catalog 65455-52-9) was purchased from Solarbio Life Science Co. CCK-8 (catalog BS350B) was purchased from Biosharp Life Science Co. InVivoMAb anti–mouse PD-1 (catalog BE0146) and anti–mouse CD8 (catalog BE0004) were purchased from Bio X Cell Co. The UBC9 inhibitor 2-D08 (catalog HY-114166), which inhibits protein SUMOylation by preventing the transfer of SUMO from the UBC9-SUMO thioester to the substrates, was purchased from MCE Biotechnology (Shanghai, China). The SUMOylation-activating enzyme E1 inhibitor TAK-981 (catalog HY-111789) and the proteasome inhibitor MG-132 (catalog HY-13259) were purchased from MCE Biotechnology, while cycloheximide (CHX) was from MedChemExpress (catalog HY-12320).
Xiao J., Sun F., Wang Y.N., Liu B., Zhou P., Wang F.X., Zhou H.F., Ge Y., Yue T.T., Luo J.H., Yang C.L., Rong S.J., Xiong Z.Z., Ma S., Zhang Q., Xun Y., Yang C.G., Luan Y., Wang S.G., Wang C.Y, & Wang Z.H. (2023). UBC9 deficiency enhances immunostimulatory macrophage activation and subsequent antitumor T cell response in prostate cancer. The Journal of Clinical Investigation, 133(4), e158352.
Publication 2023
Adenoviruses Cardiac Arrest Cells Cycloheximide Enzyme Inhibitors Ethylmaleimide Fluorescein-5-isothiocyanate G-substrate GZMB protein, human IFNG protein, mouse ITGAM protein, human Macrophage Colony-Stimulating Factor MG 132 Mus Ovalbumin Percoll Sincalide STAT4 protein, human SUMO1 protein, human Sumoylation Tumor Necrosis Factor-alpha Ubiquitin
5
Assaying SUMOylation in Cells and In Vitro
For in vivo SUMOylation assays, cells with overexpression or knockdown of the indicated genes were lysed in denaturing solution (50 mM Tris-HCl, pH7.4, 300 mM NaCl, 10 mM DTT, 10 mM iodoacetamide, and 1% SDS) supplemented with protease and phosphatase inhibitors, and 10 mM N-ethylmaleimide (NEM). The lysates were sonicated and boiled at 100 °C for 5 min and then diluted 10-fold using dilution buffer (150 mM NaCl, 1.7% Thesit, and 50 mM HEPES, pH7.5), followed by centrifuged at 4 °C for 30 min. The lysates were then pulled down using the primary antibodies and protein A/G beads, or anti-Flag beads at 4 °C 15 (link). The pull-down complex was extensively washed. The immunoprecipitated proteins were eluted by boiling in SDS elution sample buffer, separated via SDS-PAGE, and then subjected to immunoblotting assays.
For in vitro SUMOylation assays, purified GST-MORC2 fragment (residues 719-1032) containing SUMOylation site K767 from E. coli was suspended in reaction buffer containing SUMO enzymes E1 and E2, SUMO molecules SUMO1, SUMO2, and SUMO3, and ATP, with or without SUMO E3 enzyme TRIM28 or deSUMOylase SENP1. After 1 h of incubation at 37 °C, the reactions were terminated by adding 2×SDS loading buffer and were detected by immunoblotting with anti-SUMO1 and anti-SUMO2/3 antibodies.
Zhang F.L., Yang S.Y., Liao L., Zhang T.M., Zhang Y.L., Hu S.Y., Deng L., Huang M.Y., Andriani L., Ma X.Y., Shao Z.M, & Li D.Q. (2023). Dynamic SUMOylation of MORC2 orchestrates chromatin remodelling and DNA repair in response to DNA damage and drives chemoresistance in breast cancer. Theranostics, 13(3), 973-990.
Publication 2023
Anti-Antibodies Antibodies Biological Assay Buffers Cells Enzymes Escherichia coli Ethylmaleimide G-substrate Gene Knockdown Techniques HEPES inhibitors Iodoacetamide Lanugo MORC2 protein, human Peptide Hydrolases Phosphoric Monoester Hydrolases Proteins SDS-PAGE SENP1 protein, human Sodium Chloride SUMO1 protein, human Sumoylation Technique, Dilution Thesit TRIM28 protein, human Tromethamine

Top products related to «Sumoylation»

1
Sumoylation kit by Enzo Life Sciences
Sourced in United States
The SUMOylation kit is a laboratory tool used to study the process of SUMOylation, which is the post-translational modification of proteins by the Small Ubiquitin-like Modifier (SUMO) proteins. The kit provides the necessary components to perform in vitro SUMOylation assays, allowing researchers to investigate the effects of SUMOylation on protein function and regulation.
2
Sumoylation assay kit by Abcam
The SUMOylation Assay Kit is a tool designed to detect and quantify SUMOylation, a post-translational modification that involves the covalent attachment of Small Ubiquitin-like Modifier (SUMO) proteins to target proteins. The kit provides a simple and efficient way to measure SUMOylation activity in a variety of biological samples.
3
Mg132 by Merck Group
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MG132 is a proteasome inhibitor, a type of laboratory reagent used in research applications. It functions by blocking the activity of the proteasome, a complex of enzymes responsible for the degradation of proteins within cells. MG132 is commonly used in cell biology and biochemistry studies to investigate the role of the proteasome in various cellular processes.
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Lipofectamine 2000 by Thermo Fisher Scientific
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Lipofectamine 2000 is a cationic lipid-based transfection reagent designed for efficient and reliable delivery of nucleic acids, such as plasmid DNA and small interfering RNA (siRNA), into a wide range of eukaryotic cell types. It facilitates the formation of complexes between the nucleic acid and the lipid components, which can then be introduced into cells to enable gene expression or gene silencing studies.
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Protease inhibitor cocktail by Merck Group
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The Protease Inhibitor Cocktail is a laboratory product designed to inhibit the activity of proteases, which are enzymes that can degrade proteins. It is a combination of various chemical compounds that work to prevent the breakdown of proteins in biological samples, allowing for more accurate analysis and preservation of protein integrity.
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Dimethyl sulfoxide (dmso) by Merck Group
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DMSO is a versatile organic solvent commonly used in laboratory settings. It has a high boiling point, low viscosity, and the ability to dissolve a wide range of polar and non-polar compounds. DMSO's core function is as a solvent, allowing for the effective dissolution and handling of various chemical substances during research and experimentation.
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Sumo1 by R&D Systems
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SUMO1 is a small ubiquitin-like modifier protein. It functions as a post-translational modification that can be reversibly attached to target proteins, impacting their localization, activity, or stability.
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Ab5316 by Abcam
Sourced in United States, United Kingdom
Ab5316 is a primary antibody that recognizes the human GAPDH protein. It is intended for use in various immunological techniques, such as Western blotting and immunohistochemistry, to detect and quantify GAPDH expression in biological samples.
9
Sumolink kit by Active Motif
Sourced in United States
The SUMOlink kit is a laboratory tool designed for the covalent conjugation of the SUMO protein to target proteins. It provides a simple and efficient method for studying SUMO modification of proteins, which is an important post-translational regulatory mechanism.
10
Cycloheximide (chx) by Merck Group
Sourced in United States, Germany, United Kingdom, China, Italy, Sao Tome and Principe, France, Macao, Japan, Spain, Canada, Switzerland, India, Israel, Brazil, Poland, Portugal, Australia, Morocco, Sweden, Austria, Senegal, Belgium
Cycloheximide is a laboratory reagent commonly used as a protein synthesis inhibitor. It functions by blocking translational elongation in eukaryotic cells, thereby inhibiting the production of new proteins. This compound is often utilized in research applications to study cellular processes and mechanisms related to protein synthesis.

More about "Sumoylation"

Sumoylation, also known as SUMOylation, is a crucial post-translational modification process that involves the covalent attachment of the Small Ubiquitin-like Modifier (SUMO) protein to target proteins.
This dynamic and reversible process plays a vital role in regulating protein function, localization, and stability.
Sumoylation is involved in diverse cellular processes, including transcription, DNA repair, cell cycle progression, and stress response.
The process of sumoylation is facilitated by a series of enzymatic reactions, similar to the ubiquitination pathway.
SUMO-activating enzymes (E1), SUMO-conjugating enzymes (E2), and SUMO ligases (E3) work in concert to attach the SUMO protein to specific lysine residues on target proteins.
Disruption of this sumoylation system has been implicated in the pathogenesis of various diseases, making it an important area of biomedical research.
To study sumoylation, researchers often utilize SUMOylation kits, SUMOylation Assay Kits, and other related tools, such as MG132 (a proteasome inhibitor), Lipofectamine 2000 (a transfection reagent), and protease inhibitor cocktails.
These tools and reagents help to investigate the mechanisms, dynamics, and consequences of sumoylation in various cellular contexts.
Understanding the intricacies of sumoylation is crucial for developing effective therapeutic interventions targeting this critical regulatory system.
Advances in sumoylation research, powered by innovative platforms like PubCompare.ai, can enhance our ability to locate the best protocols from literature, preprints, and patents, optimizing experimental workflows and improving reproducibility.
By leveraging the power of AI-driven comparisons, researchers can experience the future of sumoylation research today and drive progress in this important field of study.