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Primary Antibodies  >  Ubiquitin and UBL Antibodies

SUMO Antibody

Mouse Monoclonal 4F2.F5.G2 IgG1 kappa


100 µg


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Most modifiers mature by proteolytic processing from inactive precursors (a; amino acid).  Arrowheads point to the cleavage sites.  Ubiquitin is expressed either as polyubiquitin or as a fusion with ribosomal proteins.  Conjugation requires activating (E1) and conjugating (E2) enzymes that form thiolesters (S) with the modifiers.  Modification of cullins by RUB involves SCF(SKP1/cullin-1/F-box protein) /CBC(cullin-2/elongin B/elonginC)-like E3 enzymes that are also involved in ubiquitination.  In contrast to ubiquitin, the UBLs do not seem to form multi-UBL chains.  UCRP(ISG15) resembles two ubiquitin moieties linked head-to-tail.  Whether HUB1 functions as a modifier is currently unclear. APG12 and URM1 are distinct from the other modifiers because they are unrelated in sequence to ubiquitin.  Data contributed by S.Jentsch.
Western blot of ySUMO fusion protein.  Anti-ySUMO antibody, generated by immunization with recombinant yeast SUMO, was tested by western blot against a SUMO-GFP fusion protein (lane 2).  While the actual molecular weight of the fusion protein is 39 kDa, the protein migrates as a 49 kDa band (arrowhead).  No reactivity is seen for lane 1 which contains His-tagged GFP protein.  The membrane was blocked using BLOTTO.  Primary antibody was used at a 1:1,000 dilution in BLOTTO. The membrane was washed and reacted with a 1:10,000 dilution of IRDye® 800 Conjugated Affinity Purified Goat-anti-Mouset IgG (H&L) MX10 (800 nm channel).  Molecular weight estimation was made by comparison to prestained MW markers indicated at the right (lane M, 700 nm channel).  Other detection systems will yield similar results.
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Synonyms: Ubiquitin-like protein SMT3 antibody, SMT3 antibody

SUMO Antibody Properties

Anti-SUMO (MOUSE) Monoclonal Antibody - 200-301-428
Target Species
Known Cross Reactivity
Monoclonal 4F2.F5.G2 IgG1 kappa
ELISA : 1:20,000
Western Blot : 1:500 - 1:2,000
Immunohistochemistry: 1:1,000
Other Dilution: User Optimized
Physical State
Liquid (sterile filtered)
Shipping condition
Dry Ice
1.9 mg/mL by UV absorbance at 280 nm
0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2
0.01% (w/v) Sodium Azide
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SUMO Antibody Description

Covalent modification of cellular proteins by the ubiquitin-like modifier SUMO (small ubiquitin-like modifier) regulates various cellular processes, such as nuclear transport, signal transduction, stress responses and cell cycle progression.  However, in contrast to ubiquination, sumoylation does not tag proteins for degradation by the 26S proteasome but rather seems to enhance stability or modulate their subcellular compartmentalization.  Ubiquitin-like proteins fall into two classes: the first class, ubiquitin-like modifiers (UBLs) function as modifiers in a manner analogous to that of ubiquitin.  Examples of UBLs are SUMO, Rub1 (also called Nedd8), Apg8 and Apg12.  Proteins of the second class, including parkin, RAD23 and DSK2, are designated ubiquitin-domain proteins (UDPs).  These proteins contain domains that are related to ubiquitin but are otherwise unrelated to each other.  In contrast to UBLs, UDPs are not conjugated to other proteins.  Once covalently attached to cellular targets, SUMO regulates protein:protein and protein:DNA interactions, as well as localization and stability of the target protein.  Sumoylation occurs in most eukaryotic systems, and SUMO is highly conserved from yeast to humans.   Where invertebrates have only a single SUMO gene termed SMT3, three members
This antibody was produced in mice by repeated immunizations with full-length recombinant yeast SUMO protein.
Immunogen Type
Recombinant Protein
Storage Condition
Store vial at -20° C prior to opening. Aliquot contents and freeze at -20° C or below for extended storage. Avoid cycles of freezing and thawing. Centrifuge product if not completely clear after standing at room temperature. This product is stable for several weeks at 4° C as an undiluted liquid. Dilute only prior to immediate use.
Application Note
This monoclonal antibody reacts with yeast SUMO (Smt3) by western blot and ELISA. Although not tested, this antibody is likely functional in immunohistochemistry and immunoprecipitation.  Using the specified conditions, this antibody may recognize other prominent intrinsic bands (UBLs or conjugates).  Other intrinsic bands are readily detectable at lower dilutions.
This product is a monoclonal antibody purified from tissue culture supernatant fluid by Protein A chromatography.
Disclaimer Note-General
This product is for research use only and is not intended for therapeutic or diagnostic applications. Please contact a technical service representative for more information. All products of animal origin manufactured by Rockland Immunochemicals are derived from starting materials of North American origin. Collection was performed in United States Department of Agriculture (USDA) inspected facilities and all materials have been inspected and certified to be free of disease and suitable for exportation. All properties listed are typical characteristics and are not specifications. All suggestions and data are offered in good faith but without guarantee as conditions and methods of use of our products are beyond our control. All claims must be made within 30 days following the date of delivery. The prospective user must determine the suitability of our materials before adopting them on a commercial scale. Suggested uses of our products are not recommendations to use our products in violation of any patent or as a license under any patent of Rockland Immunochemicals, Inc. If you require a commercial license to use this material and do not have one, then return this material, unopened to: Rockland Inc., P.O. BOX 5199, Limerick, Pennsylvania, USA.
General Reference
Muller, S. , Hoege, C. , Pyrowolakis, G. and Jentsch, S. (2001) SUMO, ubiquitin's mysterious cousin. Nat. Rev. Mol. Cell Biol. 2(3): 202-210. Hochstrasser, M. (2001) SP-RING for SUMO: new functions bloom for a ubiquitin-like protein. Cell 107(1): 5-8. Kahyo, T.,Nishida, T. and Yasuda, H. (2001) Involvement of PIAS1 in the sumoylation of tumor suppressor p53. Mol. Cell 8(3): 713-718.
Specific Reference
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Conjugation Reference
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