|Presentation||100 µg of concentration 1.0 mg/mL in 20mM HEPES, pH8.0, 50mM NaCl, 1mM DTT.|
|Safety Information according to GHS|
|Storage and Shipping Information|
|Storage Conditions||Stable for 1 year at -80°C from date of shipment for up to 12 months. Avoid multiple freeze/thaw cycles. After initial defrost, aliquot into individual tubes and refreeze at -80ºC.|
|Material Size||100 µg|
|SUMO2 Protein - 0611045520||0611045520|
|Reference overview||Pub Med ID|
|Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9.|
Tatham, M H, et al.
J. Biol. Chem., 276: 35368-74 (2001) 2001
Conjugation of the small ubiquitin-like modifier SUMO-1/SMT3C/Sentrin-1 to proteins in vitro is dependent on a heterodimeric E1 (SAE1/SAE2) and an E2 (Ubc9). Although SUMO-2/SMT3A/Sentrin-3 and SUMO-3/SMT3B/Sentrin-2 share 50% sequence identity with SUMO-1, they are functionally distinct. Inspection of the SUMO-2 and SUMO-3 sequences indicates that they both contain the sequence psiKXE, which represents the consensus SUMO modification site. As a consequence SAE1/SAE2 and Ubc9 catalyze the formation of polymeric chains of SUMO-2 and SUMO-3 on protein substrates in vitro, and SUMO-2 chains are detected in vivo. The ability to form polymeric chains is not shared by SUMO-1, and although all SUMO species use the same conjugation machinery, modification by SUMO-1 and SUMO-2/-3 may have distinct functional consequences.
|Structure determination of the small ubiquitin-related modifier SUMO-1|
Bayer, P, et al
J Mol Biol, 280:275-86 (1998) 1998