Recombinant Human SUMO1 AMC Protein, CF

 

Discontinued Product

UL-551 has been discontinued.
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Recombinant Human SUMO1 AMC Protein, CF Summary

Product Specifications

Purity
>95%, by HPLC.
Activity
Recombinant Human SUMO1 AMC is a fluorogenic substrate for some SUMO-specific isopeptidases. Release of AMC fluorescence can be monitored with an excitation wavelength of 345 nM and an emission wavelength of 445 nM. Reaction conditions will need to be optimized for each specific application. We recommend an initial Recombinant Human SUMO1 AMC concentration of 0.1-1 μM.
Source
E. coli-derived human SUMO1 protein
Accession #
Predicted Molecular Mass
11 kDa

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UL-551

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-551

Formulation

1.13 mg/ml (100 µM) in 50 mM HEPES pH 7.5, 100 mM NaCl

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.
  • 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: SUMO1

Human Small Ubiquitin-like Modifier 1 (SUMO1), also known as Sentrin, UBL1, and SMT3C, is synthesized as a 101 amino acid (aa) propeptide with a predicted molecular weight of 11.5 kDa. Human SUMO1 is the most unique of the four identified SUMO proteins and shares only 44%, 47%, and 41% aa sequence identity with SUMO2, SUMO3, and SUMO4, respectively. In contrast, human SUMO1 shares 100% aa sequence identity with the mouse ortholog. 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 cleavage of a four aa C-terminal prosegment, the C-terminal glycine residue of SUMO1 is enzymatically attached to a lysine residue on a target protein. In humans, SUMO1 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). SUMOylation can occur without the requirement of a specific SUMO ligase (E3), where SUMO1 is transferred directly from UBE2I/Ubc9 to specific substrates. In Alzheimer's disease models SUMO1 has been shown to influence the generation of Amyloid-beta peptide by promoting the accumulation of BACE-1 (7). Covalent modification of Phosphatase and Tensin Homolog Deleted on Chromosome (PTEN) by SUMO1 is thought to regulate tumorigenesis by retaining PTEN at the plasma membrane, an effect that suppresses PI 3-Kinase/Akt-dependent tumor growth (8).

This fluorogenic substrate for SUMO1 hydrolases is based on the carboxy-terminus derivatization of SUMO1 with 7-amido-4-methylcoumarin (AMC). SUMO1 AMC is useful for studying SUMO1 hydrolases when detection sensitivity or continuous monitoring of activity is essential.

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. Yun, S.M. et al. (2013) Neurobiol Aging. 34:650.
  8. Huang, J. et al. (2012) Nat. Commun. 3:911.
Long Name
Small Ubiquitin-like Modifier 1
Entrez Gene IDs
7341 (Human); 22218 (Mouse); 301442 (Rat)
Alternate Names
DAP1; GAP modifying protein 1; GAP-modifying protein 1; GMP1SMT3CSMT3H3OFC10UBL1PIC1; PIC1; SENP2; Sentrin; small ubiquitin-related modifier 1; SMT3 homolog 3; SMT3 suppressor of mif two 3 homolog 1 (S. cerevisiae); SMT3 suppressor of mif two 3 homolog 1 (yeast); SMT3; SMT3C; SMT3H3; SUMO1; SUMO-1; Ubiquitin-homology domain protein PIC1; ubiquitin-like 1 (sentrin); Ubiquitin-like protein SMT3C; Ubiquitin-like protein UBL1; UBL1

Citations for Recombinant Human SUMO1 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.

6 Citations: Showing 1 - 6
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  1. Discovery of a Dual SENP1 and SENP2 Inhibitor
    Authors: M Brand, EB Bommeli, M Rütimann, U Lindenmann, R Riedl
    International Journal of Molecular Sciences, 2022-10-11;23(20):.
    Applications: Bioassay
  2. Crystal structure and activity-based labeling reveal the mechanisms for linkage-specific substrate recognition by deubiquitinase USP9X
    Authors: P Paudel, Q Zhang, C Leung, HC Greenberg, Y Guo, YH Chern, A Dong, Y Li, M Vedadi, Z Zhuang, Y Tong
    Proc. Natl. Acad. Sci. U.S.A., 2019-03-26;0(0):.
    Applications: Bioassay
  3. The SUMO protease SENP1 and the chromatin remodeller CHD3 interact and jointly affect chromatin accessibility and gene expression
    Authors: F Rodríguez-, RB Lemma, I Cuervo, M Bengtsen, LM Moen, M Ledsaak, R Eskeland, OS Gabrielsen
    J. Biol. Chem., 2018-08-06;0(0):.
  4. 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, 2017-12-12;6(0):.
    Applications: Bioassay
  5. Diverse mechanisms of metaeffector activity in an intracellular bacterial pathogen, Legionella pneumophila
    Authors: Malene L Urbanus
    Mol. Syst. Biol, 2016-12-16;12(12):893.
    Applications: Bioassay
  6. A selective USP1-UAF1 inhibitor links deubiquitination to DNA damage responses.
    Authors: Liang, Qin, Dexheimer, Thomas S, Zhang, Ping, Rosenthal, Andrew S, Villamil, Mark A, You, Changjun, Zhang, Qiuting, Chen, Junjun, Ott, Christin, Sun, Hongmao, Luci, Diane K, Yuan, Bifeng, Simeonov, Anton, Jadhav, Ajit, Xiao, Hui, Wang, Yinsheng, Maloney, David J, Zhuang, Zhihao
    Nat Chem Biol, 2014-02-16;10(4):298-304.
    Applications: Bioassay

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