08-143 | SUMO2 Protein

08-143
100 µg  
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      Overview

      Replacement Information
      Description
      Catalogue Number08-143
      Brand Family Upstate
      Trade Name
      • Upstate
      DescriptionSUMO2 Protein
      References
      Product Information
      Presentation100 µg of concentration 1.0 mg/mL in 20mM HEPES, pH8.0, 50mM NaCl, 1mM DTT.
      Applications
      Application NotesMature SUMO-2 suitable for in vitro SUMOylation using the SUMO Activating Enzyme Complex (Cat. no. 14-858) and SUMO conjugating enzyme UbcH9 (Cat. no. 14-815). In The presence of these enzymes with ATP, Mg2+, and DTT, mature SUMO-2 may be conjugated to soluble proteins. The protein is N-terminally His6-tagged within a leader sequence. Typical in vitro concentration for non-rate limiting conjugate formation is 200μM to 1mM depending upon conditions.
      Biological Information
      Concentration1.0 mg/mL
      Purity≥95%
      Entrez Gene Number
      Entrez Gene SummarySUMO proteins, such as SUMO3, and ubiquitin (see MIM 191339) posttranslationally modify numerous cellular proteins and affect their metabolism and function. However, unlike ubiquitination, which targets proteins for degradation, sumoylation participates in a number of cellular processes, such as nuclear transport, transcriptional regulation, apoptosis, and protein stability (Su and Li, 2002 [PubMed 12383504]).[supplied by OMIM]
      Gene Symbol
      • SUMO3
      • SUMO-2
      • SMT3H1
      • SMT3A
      • SUMO-3
      UniProt Number
      UniProt SummaryFUNCTION: SwissProt: P55854 # Ubiquitin-like protein which can be covalently attached to target lysines either as a monomer or as a lysine-linked polymer. Does not seem to be involved in protein degradation and may function as an antagonist of ubiquitin in the degradation process. Plays a role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Covalent attachment to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase such as PIAS1-4, RANBP2 or CBX4.
      SIZE: 103 amino acids; 11637 Da
      SUBUNIT: Interacts with SAE2 and UBE2I. Covalently attached to a number of proteins (By similarity).
      SUBCELLULAR LOCATION: Cytoplasm.
      TISSUE SPECIFICITY: Expressed predominantly in liver.
      PTM: Polymeric chains can be formed through Lys-11 cross-linking. & Cleavage of precursor form by SENP1, SENP2 or SENP5 is necessary for function.
      SIMILARITY: SwissProt: P55854 ## Belongs to the ubiquitin family. SUMO subfamily. & Contains 1 ubiquitin-like domain.
      Molecular Weight15 kDa
      Physicochemical Information
      Dimensions
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Usage Statement
      • Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
      Storage and Shipping Information
      Storage ConditionsStable 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.
      Packaging Information
      Material Size100 µg
      Transport Information
      Supplemental Information
      Specifications

      Documentation

      Certificates of Analysis

      TitleLot Number
      SUMO2 Protein - 0611045520 0611045520

      References

      Reference overviewPub 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

      Show Abstract
      11451954 11451954
      Structure determination of the small ubiquitin-related modifier SUMO-1
      Bayer, P, et al
      J Mol Biol, 280:275-86 (1998)  1998

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