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Poly-SUMO-2 chains ([SUMO-2]2-7)

BML-UW9670-0025 25 µg 233.00 USD
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Product Details

MW:~21.1kDa - ~73.8kDa
Source:Produced in E. coli. Poly-SUMO-2 chains were synthesized enzymatically using SUMO-2 and purified by size exclusion chromatography to remove SUMO-2 monomer.
UniProt ID:P55854
Formulation:Liquid. In 50mM TRIS, pH 7.5, containing 150mM sodium chloride and 1mM DTT.
Purity:≥95% (SDS-PAGE)
Application Notes:Suggested uses:
  1. DeSUMOylating enzyme (SENP) substrates.
  2. Investigation of polySUMO-2 chain recognition by and interaction with SUMO/polySUMO binding proteins.
  3. PolySUMOylation studies.
Shipping:Blue Ice
Long Term Storage:-20°C
Use/Stability:Stable for at least 1 year after receipt when stored at -20°C.
Handling:Avoid freeze/thaw cycles. After opening, prepare aliquots and store at -20°C.
Scientific Background:Small Ubiquitin-like Modifier (SUMO) is involved in diverse biological processes ranging from transcriptional regulation to defining sub-cellular localization. SUMO-2 and SUMO-3 each contain an acceptor lysine (K11) that allows the formation of polySUMO chains by canonical means. Under appropriate conditions, SUMO-1 may also form polySUMO chains at sites not comprising a recognised SUMOylation motif. A number of studies have implicated important biological functions for SUMO polymers including roles in chromosome segregation, recovery from checkpoint arrest, DNA damage response and meiosis. PolySUMO conjugates identified include HIF1α, PARP1, TOP2, PCNA and PML.
Technical Info/Product Notes:NOTE: There is confusion within the scientific literature (including NCBI and UniProt protein databases) concerning the nomenclature used for SUMO-2 and SUMO-3 paralogs. Please note that Enzo Life Sciences uses the nomenclature proposed by Saitoh and Hinchey for SUMO-2/SMT3A and SUMO-3/SMT3B and reports data accordingly.
Regulatory Status:RUO - Research Use Only

General Literature References

PARP-1 transcriptional activity is regulated by sumoylation upon heat shock: N. Martin, et al.; EMBO J. 28, 3534 (2009), Abstract;
Architecture and assembly of poly-SUMO chains on PCNA in Saccharomyces cerevisiae: H. Windecker & H.D. Ulrich; J. Mol. Biol. 376, 221 (2008), Abstract;
In vivo identification of human small ubiquitin-like modifier polymerization sites by high accuracy mass spectrometry and an in vitro to in vivo strategy: I. Matic, et al.; Mol. Cell Proteomics 7, 132 (2008), Abstract;
In vivo modeling of polysumoylation uncovers targeting of Topoisomerase II to the nucleolus via optimal level of SUMO modification: Y. Takahashi & A. Strunnikov; Chromosoma 117, 189 (2008), Abstract;
RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation: M.H. Tatham, et al.; Nat. Cell Biol. 10, 538 (2008), Abstract;
The fast-growing business of SUMO chains: H.D. Ulrich; Mol. Cell. 32, 301 (2008), Abstract;
The Ulp2 SUMO protease is required for cell division following termination of the DNA damage checkpoint: D.C. Schwartz, et al.; Mol. Cell Biol. 27, 6948 (2007), Abstract;
SUMO modifications control assembly of synaptonemal complex and polycomplex in meiosis of Saccharomyces cerevisiae: C.H. Cheng, et al.; Genes Dev. 20, 2067 (2006), Abstract;
Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9: M.H. Tatham, et al.; J. Biol. Chem. 276, 35368 (2001), Abstract; Full Text
SUMO, ubiquitin’s mysterious cousin: S. Muller, et al.; Nat. Rev. Mol. Cell Biol. 2, 202 (2001), Abstract;
Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3: H. Saitoh & J. Hinchey; J. Biol. Chem. 275, 6252 (2000), Abstract;

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