Mouse Monoclonal SUMO1 Antibody

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     All lanes : Anti-SUMO1 Antibody at 1:4000 dilution Lane 1: HL-60 whole cell lysates Lane 2: Hela whole cell lysates Lane 3: Jurkat whole cell lysates Lysates/proteins at 20 μg per lane. Secondary Goat Anti-mouse IgG,  (H+L), Peroxidase conjugated at 1/10000 dilution Predicted band size : 12 kDa Blocking/Dilution buffer: 5% NFDM/TBST.    

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     Immunofluorescent analysis of 4% paraformaldehyde-fixed, 0.1% Triton X-100 permeabilized HeLa (human cervical epithelial adenocarcinoma cell line) cells labeling SUMO1 with P33128 at 1/25 dilution, followed by Dylight® 488-conjugated goat anti-mouse IgG   secondary antibody at 1/200 dilution (green). Immunofluorescence image showing nucleus and weak cytoplasm staining on HeLa cell line. Cytoplasmic actin is detected with Dylight® 554 Phalloidin  at 1/100 dilution (red).    

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     Overlay histogram showing Jurkat cells stained with P33128(green line).  The cells were fixed with 2% paraformaldehyde (10 min) and then permeabilized with 90% methanol for 10 min.  The cells were then icubated in 2% bovine serum albumin to block non-specific protein-protein interactions followed by the antibody (P33128,  1:25 dilution) for 60 min at 37ºC.  The secondary antibody used was Goat-Anti-Mouse IgG, DyLight® 488 Conjugated Highly Cross-Adsorbed(OJ192088) at 1/200 dilution for 40 min at 37ºC.  Isotype control antibody (blue line) was mouse IgG1 (1μg/1x10^6 cells) used under the same conditions.  Acquisition of >10, 000 events was performed.    

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     Immunohistochemical analysis of paraffin-embedded Human Lung adenocarcinoma section using Pink1(Cat#am1200a). am1200a was diluted at 1:50 dilution. A undiluted biotinylated goat polyvalent antibody was used as the secondary, followed by DAB staining.    

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     P33128 staining SUMO1 in human lung adenocarcinoma tissue sections by Immunohistochemistry (IHC-P - paraformaldehyde-fixed,  paraffin-embedded sections).  Tissue was fixed with formaldehyde and blocked with 3% BSA for 0. 5 hour at room temperature; antigen retrieval was by heat mediation with a citrate buffer (pH6).  Samples were incubated with primary antibody (1/25) for 1 hours at 37°C.  A undiluted biotinylated goat polyvalent antibody was used as the secondary antibody.    

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     P33128 staining SUMO1 in human breast carcinoma tissue sections by Immunohistochemistry (IHC-P - paraformaldehyde-fixed,  paraffin-embedded sections).  Tissue was fixed with formaldehyde and blocked with 3% BSA for 0. 5 hour at room temperature; antigen retrieval was by heat mediation with a citrate buffer (pH6).  Samples were incubated with primary antibody (1/25) for 1 hours at 37°C.  A undiluted biotinylated goat polyvalent antibody was used as the secondary antibody.    

SUMO1 antibodies are essential tools for studying the post-translational modification process called SUMOylation, which involves the covalent attachment of small ubiquitin-like modifier (SUMO) proteins to target substrates. SUMO1 (small ubiquitin-like modifier 1) is a member of the SUMO protein family, which also includes SUMO2. SUMO3. and SUMO4. Unlike ubiquitination, SUMOylation does not typically mark proteins for degradation but regulates diverse cellular processes such as nuclear-cytosolic transport, transcriptional regulation, DNA repair, and stress responses. SUMO1. in particular, is known for its role in modulating protein localization, stability, and interaction networks.

SUMO1 antibodies are designed to specifically detect endogenous or exogenous SUMO1-conjugated proteins in various experimental applications, including Western blotting, immunoprecipitation, immunofluorescence, and immunohistochemistry. These antibodies are critical for identifying SUMOylation substrates, studying dynamic SUMO1 modification under different physiological or pathological conditions (e.g., cancer, neurodegenerative diseases), and exploring mechanisms of SUMOylation enzymes (E1 activating, E2 conjugating, and E3 ligating enzymes).

Most SUMO1 antibodies are raised against recombinant SUMO1 proteins or synthetic peptides corresponding to unique regions of SUMO1. ensuring specificity and minimizing cross-reactivity with other SUMO paralogs. Validation often includes testing in SUMO1-knockout models or siRNA-mediated knockdown systems. Researchers must consider potential cross-reactivity with free SUMO1 versus conjugated forms, as well as tissue-specific expression patterns, when interpreting results. The development of high-affinity, modification-state-specific SUMO1 antibodies continues to advance research in cellular signaling and disease mechanisms.