Recombinant Human SUMO2 AMC Protein, CF

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Product Details
Citations (3)

Recombinant Human SUMO2 AMC Protein, CF Summary

>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain.
SUMO2 AMC is a fluorogenic substrate for some SUMO-specific isopeptidases. Release of AMC fluorescence can be monitored with an excitation wavelength of 380 nM and an emission wavelength of 460 nM. Reaction conditions will need to be optimized for each specific application. We recommend an initial SUMO2 AMC concentration of 0.1-1 μM.
E. coli-derived human SUMO2 protein
Accession #
Predicted Molecular Mass
11 kDa

Product Datasheets

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.



X mg/ml (X µM) in 25 mM MOPS pH 6.5, 200 mM NaCl, 10% (v/v) Glycerol,  2 mM DTT

Shipping The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: Protect from light. Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -70 °C as supplied.
  • 3 months, -70 °C under sterile conditions after opening.
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Background: 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. Human SUMO2 shares 100% aa sequence identity with mouse SUMO2. SUMO2 also has very high aa sequence identity with SUMO3 and SUMO4, 86% and 85%, respectively. SUMO2 shares only 44% aa sequence identity with SUMO1. 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 (1-3). 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 (4,5). In yeast, the SUMO-activating (E1) enzyme is Aos1/Uba2p (6). Because of the high level of aa sequence identity most studies report effects of SUMO2/3. For example, post-translational addition of SUMO2/3 was shown to modulate the function of ARHGAP21, a RhoGAP protein known to be involved in cell migration (7). Other reports indicate that the SUMOylation with SUMO2/3, but not SUMO1, may represent an important mechanism to protect neurons during episodes of cerebral ischemia (8,9). However, studies suggest that SUMO2/3 expression is regulated in an isoform-specific manner since oxidative stress downregulated the transcription of SUMO3 but not SUMO2 (10).

Fluorogenic substrate for SUMO2 hydrolases based on the carboxy-terminus derivatization of SUMO2 with 7-amido-4-methylcoumarin (AMC). SUMO2 AMC is useful for studying SUMO2 hydrolases (SENPs) when detection sensitivity or continuous monitoring of activity is essential.

  1. Desterro, J.M. et al. (1997) FEBS. Lett. 417:297.
  2. Bettermann, K. et al. (2012) Cancer Lett. 316:113.
  3. Praefcke, G.J. et al. (2012) Trends Biochem. Sci. 37:23.
  4. Okuma, T. et al. (1999) Biochem. Biophys. Res. Commun. 254:693.
  5. Tatham, M.H. et al. (2001) J. Biol. Chem. 276:35368.
  6. Johnson, E.S. et al. (1997) EMBO J. 16:5509.
  7. Bigarella, C.L. et al. (2012) FEBS Lett. 586:3522.
  8. Datwyler, A.L. et al. (2012) J. Cereb. Blood Flow Metab. 31:2152.
  9. Wang, Z. et al. (2012) Protein Expr. Purif. 82:174.
  10. Sang, J. et al. (2012) Biochem. J. 435:489.
Long Name
Small Ubiquitin-like Modifier 2
Entrez Gene IDs
6613 (Human)
Alternate Names
HSMT3; MGC117191; sentrin 2; Sentrin-2; small ubiquitin-like modifier 2; small ubiquitin-related modifier 2; SMT3 (suppressor of mif two 3, yeast) homolog 2; SMT3 homolog 2; SMT3 suppressor of mif two 3 homolog 2 (S. cerevisiae); SMT3 suppressor of mif two 3 homolog 2 (yeast); SMT3A; SMT3B; SMT3H2; SUMO2; SUMO-2; SUMO3; SUMO-3; Ubiquitin-like protein SMT3A; ubiquitin-like protein SMT3B

Citations for Recombinant Human SUMO2 AMC Protein, 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 family of unconventional deubiquitinases with modular chain specificity determinants
    Authors: T Hermanns, C Pichlo, I Woiwode, K Klopffleis, KF Witting, H Ovaa, U Baumann, K Hofmann
    Nat Commun, 2018;9(1):799.
    Applications: Bioassay
  2. Shigella entry unveils a calcium/calpain-dependent mechanism for inhibiting sumoylation
    Authors: P Lapaquette, S Fritah, N Lhocine, A Andrieux, G Nigro, J Mounier, P Sansonetti, A Dejean
    Elife, 2017;6(0):.
    Applications: Bioassay
  3. Diverse mechanisms of metaeffector activity in an intracellular bacterial pathogen, Legionella pneumophila
    Authors: Malene L Urbanus
    Mol. Syst. Biol, 2016;12(12):893.
    Applications: Bioassay


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