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Material Data Sheet
SUMO-1 Conjugation Kit
Price: $295.00
SUMO-1 Conjugation Kit
Price:
295
Quantity:
1 Kit
Data Sheet:
This kit is designed for the conjugation of the ubiquitin-like modifier SUMO-1 to protein substrates in vitro, which requires the activities of the heterodimeric human E1 activating enzyme (SAE1/SAE2) and the UbcH9 E2 enzyme.
NOTE: Kit contains reagents sufficient for 5-10 x 20 μl reactions.
Product Information
Western Blot Data:
Western Blot Data:
Supplied:
ProteinConcentrationQuantity10X E1 EnzymeX mg/ml (X μM)20 μL10X SUMO-1X mg/ml (X μM)20 μL10X UbcH9X mg/ml (X μM)20 μL 10X Mg-ATP Solution XmM 20 μL 10X Reaction Buffer X mM Hepes pH 8 20 μL X mM NaCl X mM DTT
Background:
The ubiquitin-like SUMO-1 is conjugated to a variety of proteins in the presence of UbcH9 and the SUMO E1 activating enzyme (SAE1/SAE2 in human, or Aos1/Uba2p in yeast). The heterodimeric SAE1/SAE2 complex (38 and 70 kDa respectively) uses ATP to adenylate the C-terminal glycine<br>residue of SUMO-1, forming a high-energy thiolester bond with the SAE2 subunit. The second step is the trans-esterification reaction whereby the activated SUMO-1 is transferred to Cys93 of UbcH9. UbcH9 is a member of the E2 family and is homologous to ubiquitin conjugating enzymes, but is<br>specific for the conjugation of SUMO to a variety of target proteins. This E2 is unusual in that it interacts directly with protein substrates that are modified by sumolyation, and may play a role in substrate recognition. Sumoylated substrates are primarily localized to thenucleus (RanGAP-1, RANBP2, PML, p53, Sp100, HIPK2) but there are also cytosolic substrates (IκBα, GLUT1, GLUT4). SUMO modification has been implicated in functions such as nuclear transport, chromosome segregation and transcriptional regulation, apoptosis and protein function and stability. Storage:
Store at -80°C. Avoid multiple freeze/thaw cycles.
Literature
References:
Desterro J.M., et al. (1997) FEBs. Lett. 417:297-300
Okama T., et al. (1999) Biochem. Biophys. Res. Comm. 254:693-698
Pichler A. et al. (2005) Nat. Struct. Mol. Biol. 12:264-269
Rodriguez M.S et al. (2001) J. Biol. Chem. 276:12654-59
Saitoh H. and Hinchey J. (2000) J. Biol. Chem. 275:6252-6258
Seeler J-S. and Dejean A. (2003) Nat. Rev. 4:690-699
Su H-L., et al. (2002) Gene 296:65-73
Tatham M.H., et al. (2001) J. Biol. Chem. 276:35368-35374
Yeh E.T.H., et al. (2000) Gene 248:1-14
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