SUMO-interacting Motif (SIM) Peptide Agarose Protein, CF

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Product Details

Summary
Reactivity MultiSpecies Glossary
Applications Enzyme Activity
Format
Carrier-Free

Order Details

SUMO-interacting Motif (SIM) Peptide Agarose Protein, CF Summary

Details of Functionality
SUMO-interacting Motif (SIM) Peptide Agarose is ideal for the enrichment of known SIM Peptide-interacting proteins as well as the discovery of novel SIM Peptide-interacting proteins. We recommend equilibrating the resin by washing with 5-10 mL of your desired aqueous buffer.
Source
Chemically Synthesized
Protein/Peptide Type
Affinity Matrices

Packaging, Storage & Formulations

Storage
Do not freeze.
  • 3 months from date of receipt, 2 to 8 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after opening.
Buffer
0.25 ml SIM peptide agarose supplied in a 0.5 ml total volume of 50 mM Hepes pH 7.5, 250 mM NaCl.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for SUMO-interacting Motif (SIM) Peptide Agarose Protein, CF

  • Chromosome 5 Open Reading Frame 25
  • Oocyte Maturation Associated 1
  • OOMA1
  • Platform Element For Inhibition Of Autolytic Degradation
  • PLEIAD
  • SIMC1
  • SUMOinteracting Motif
  • SUMO-interacting Motif
  • SUMO-Interacting Motif-Containing Protein 1
  • SUMO-Interacting Motifs Containing 1

Background

Small Ubiquitin-like Modifiers (SUMOs) are a family of small, related proteins that are enzymatically attached to target proteins by a process termed SUMOylation. This post-translational modification regulates many cellular processes including DNA transcription and repair, cell cycle progression, protein intracellular trafficking, and nuclear receptor activities (1,2). SUMO binding and/or interaction with proteins is mediated by short amino acid consensus sequences termed SUMO-interacting motifs (SIMs) (2-5). To date, all SIMs appear to contain a hydrophobic core sequence that is either preceded or succeeded by an acidic region composed of either glutamate or aspartate residues or phosphorylated serine or threonine residues (3,6,7). The hydrophobic core of SIMs has been shown to interact with the alpha ‑helix and beta 2-strand surfaces on SUMO proteins while the negatively charged residues surrounding the hydrophobic core appear to influence binding affinities and dictate binding preferences for the various SUMO isoforms (2,5-9). SIMs have been identified in numerous types of proteins including SUMO ligases (E3), transcription factors, and transcriptional repressors (2,4,6,10-16). This affinity resin is derived from a PIAS sequence and can be used for the enrichment, isolation, and identification of SUMOylated proteins.

  1. Hilgarth, R.S. et al. (2004) J. Biol. Chem. 279:53899.
  2. Gareau, J.R. & C.D. Lima (2010) Nat. Rev. Mol. Cell Biol. 11:861.
  3. Minty, A. et al. (2000) J. Biol. Chem. 275:36316.
  4. Song, J. et al. (2004) Proc. Natl. Acad. Sci. USA 101:14373.
  5. Song, J. et al. (2005) J. Biol. Chem. 280:40122.
  6. Hecker, C.M. et al. (2006) J. Biol. Chem. 281:16117.
  7. Hickey, C.M. et al. (2012) Nat. Rev. Mol. Cell Biol. 13:755.
  8. Namanja, A.T. et al. (2012) J. Biol. Chem. 287:3231.
  9. Chang, C.C. et al. (2011) Mol. Cell 42:62.
  10. .Lin, D.Y. et al. (2006) Mol. Cell 24:341.
  11. Du, J.X. et al. (2010) J. Biol. Chem. 285:28298.
  12. .Liu, Y.C. et al. (2011) J. Biol. Chem. 286:42818.
  13. Saether, T. et al. (2011) Oncogene 30:212.
  14. Guzzo, C.M. et al. (2012) Sci. Signal. 5:ra88.
  15. Kolesar, P. et al. (2012) Nucleic Acids Res. 40:7831.
  16. Lukic, Z. et al. (2013) Retrovirology 10:10.

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