Recombinant Human SUMO2 Protein, CF

Catalog # Availability Size / Price Qty
UL-752-500
Product Details
Citations (5)
FAQs
Reviews

Recombinant Human SUMO2 Protein, CF Summary

Purity
>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain
Activity
Recombinant Human SUMO2 can be conjugated to substrate proteins via the subsequent actions of an SUMO-activating (E1) enzyme, an SUMO-conjugating (E2) enzyme, and an SUMO ligase (E3). Reaction conditions will need to be optimized for each specific application. We recommend an initial Recombinant Human SUMO2 concentration of 10-50 μM.
Source
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.

UL-752

Formulation Supplied as a solution in HEPES, NaCl, DTT and Glycerol.
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.
Reconstitution Calculator

Reconstitution Calculator

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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).

SUMOylation can occur without the requirement of a specific E3 ligase activity, where SUMO is transferred directly from UbcH9 to specific substrates. SUMOylated substrates are primarily localized to the nucleus (RanGAP-1, RANBP2, PML, p53, Sp100, HIPK2), but there are also cytosolic substrates (I kappa B alpha, GLUT1, GLUT4). SUMO modification has been implicated in functions such as nuclear transport, chromosome segregation, transcriptional regulation, apoptosis, and protein stability.

References
  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 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.

5 Citations: Showing 1 - 5
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  1. Super Resolution Microscopy of SUMO Proteins in Neurons
    Authors: L Colnaghi, L Russo, C Natale, E Restelli, A Cagnotto, M Salmona, R Chiesa, L Fioriti
    Front Cell Neurosci, 2019;13(0):486.
    Species: Human
    Sample Types: Antibody
    Applications: Neutralization
  2. SUMOylation determines the voltage required to activate cardiac IKs channels
    Authors: D Xiong, T Li, H Dai, AF Arena, LD Plant, SAN Goldstein
    Proc. Natl. Acad. Sci. U.S.A., 2017;0(0):.
    Species: Hamster
    Sample Types: Whole Cells
    Applications: Bioassay
  3. Functional Insights into ANP32A-Dependent Influenza A Virus Polymerase Host Restriction
    Authors: P Domingues, BG Hale
    Cell Rep, 2017;20(11):2538-2546.
    Species: Human
    Sample Types: Protein
    Applications: Bioassay
  4. Functional Insights into ANP32A-Dependent Influenza A Virus Polymerase Host Restriction
    Authors: P Domingues, BG Hale
    Cell Rep, 2017;20(11):2538-2546.
    Species: Human
    Sample Types: Cell Lysates
    Applications: Bioassay
  5. HSP70-Hrd1 axis precludes the oncorepressor potential of N-terminal misfolded Blimp-1s in lymphoma cells
    Authors: WF Wang, L Yan, Z Liu, LX Liu, J Lin, ZY Liu, XP Chen, W Zhang, ZZ Xu, T Shi, JM Li, YL Zhao, G Meng, Y Xia, JY Li, J Zhu
    Nat Commun, 2017;8(1):363.
    Applications: Bioassay

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