Recombinant Human Poly-SUMO2 Wild-type Chains (3-8), CF

Discontinued Product

ULC-220 has been discontinued.
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Recombinant Human Poly-SUMO2 Wild-type Chains (3-8), CF Summary

Product Specifications

Purity
>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain
Activity
The function of SUMO chains is an area of intense research. K11-linked Poly-SUMO2 WT Chains (3-8) are ideal for investigating SUMO-binding proteins and as substrates for SUMO-specific proteases. Reaction conditions will need to be optimized for each specific application.
Source
E. coli-derived human Poly-SUMO2 protein
Accession #

Product Datasheets

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ULC-220

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

ULC-220

Formulation Supplied as a solution in HEPES, NaCl and DTT.
Shipping The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -70 °C as supplied.
  • 3 months, -70 °C under sterile conditions after opening.
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Background: Poly-SUMO2

Human Small Ubiquitin-like Modifier 2 (SUMO2), also known as Sentrin2 and SMT3B is synthesized as a 95 amino acid (aa), propeptide with a predicted 11 kDa. SUMO2 contains a two aa C-terminal prosegment and an 18 aa N-terminal protein interacting region between aa 33-50. Poly-SUMO2 represents chains of wild-type recombinant human SUMO2 molecules linked via Lys11, which is the point of attachment for the C-terminal glycine residue of the preceding SUMO2 (1). SUMO2 monomers and dimers (Di-SUMO2) have been removed from the chain mixture. Human SUMO2 shares 100% aa sequence identity with mouse SUMO2. Poly-SUMO2 can be used as a substrate for SUMO-specific isopeptidases (SENPs) and DeSumoylating Isopeptidase 1 that cleave the isopeptide linkage between two SUMO2 molecules (2). It can also be used to investigate mechanisms of binding and recognition by SUMO-activating (E1) enzymes, SUMO-conjugating (E2) enzymes, SUMO ligases (E3s), and other proteins that contain SUMO binding domains. SUMOs are a family of small, related proteins that can be enzymatically attached to a target protein by a post-translational modification process termed SUMOylation (3-5). Unlike SUMO1 which is usually conjugated to proteins as a monomer, SUMO2 and SUMO3 form high molecular weight polymers on proteins. All SUMO proteins share a conserved Ubiquitin domain and a C-terminal diglycine cleavage/attachment site. Following prosegment cleavage, the C-terminal glycine residue of SUMO2 is enzymatically attached to a lysine residue on a target protein. In humans, SUMO2 is conjugated to a variety of molecules in the presence of the SAE1/UBA2 SUMO-activating (E1) enzyme and the UBE2I/Ubc9 SUMO-conjugating (E2) enzyme (6,7). In yeast, the SUMO-activating (E1) enzyme is Aos1/Uba2p (8).

Poly-SUMO-2 chains can be used to investigate mechanisms of chain recognition, binding and hydrolysis by SUMO-specific isopeptidases (SENPs), SUMO-specific E3 ligases or other proteins that contain SUMO-2 binding domains. This product is formed enzymatically with wildtype Human Recombinant SUMO-2 linked via lysine 11 which is the point of attachment for the C-terminal glycine of the preceding SUMO-2. Mono- and di-SUMO-2 have been removed from the chain mixture.

References
  1. Bylebyl, G.R. et al. (2003) J. Biol. Chem. 278:44113.
  2. Shin, E.J. et al. (2012) EMBO Report 13:339.
  3. Desterro, J.M. et al. (1997) FEBs. Lett. 417:297.
  4. Bettermann, K. et al. (2012) Cancer Lett. 316:113.
  5. Praefcke, G.J. et al. (2012) Trends Biochem. Sci. 37:23.
  6. Okuma, T. et al. (1999) Biochem. Biophys. Res.  Commun. 254:693.
  7. Tatham, M.H. et al. (2001) J. Biol. Chem. 276:35368.
  8. Johnson, E.S. et al. (1997) EMBO J. 16:5509.
Entrez Gene IDs
6613 (Human)
Alternate Names
PolySUMO2; Poly-SUMO2

Citations for Recombinant Human Poly-SUMO2 Wild-type Chains (3-8), CF

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

3 Citations: Showing 1 - 3
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  1. A Virally Encoded DeSUMOylase Activity Is Required for Cytomegalovirus Reactivation from Latency
    Authors: EL Poole, VG Kew, JCH Lau, MJ Murray, T Stamminger, JH Sinclair, MB Reeves
    Cell Rep, 2018-07-17;24(3):594-606.
    Applications: Bioassay
  2. USP7 is a SUMO deubiquitinase essential for DNA replication
    Authors: E Lecona, S Rodriguez-, J Specks, AJ Lopez-Cont, I Ruppen, M Murga, J Muñoz, J Mendez, O Fernandez-
    Nat Struct Mol Biol, 2016-03-07;23(4):270-7.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Bioassay
  3. Rap80 Protein Recruitment to DNA Double-strand Breaks Requires Binding to Both Small Ubiquitin-like Modifier (SUMO) and Ubiquitin Conjugates.
    Authors: Hu X, Paul A, Wang B
    J. Biol. Chem., 2012-06-11;287(30):25510-9.
    Applications: Binding Assay

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