Active • Host: E. coli • AA: 403-621 • Tag: N-terminal His • MW: 27.6 kDa
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Ubiquitin-like-specific Protease 1 (S. cerevisiae, recombinant)

Item No. 41844

Technical Information
Synonyms
  • His-Ulp1
  • SUMO Protease
  • Ubl-specific Protease 1
  • Ulp1
Purity
≥80% estimated by SDS-PAGE
Source
Active recombinant S. cerevisiae N-terminal His-tagged Ulp1 expressed in E. coli
Amino Acids
403-621
MW
27.6 kDa
50 mM Tris, pH 7.5, with 200 mM sodium chloride, 10% glycerol, and 1 mM DTT
Applications
SUMO tag cleavage from SUMO fusion proteins
UniProt Accession №
Q02724
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
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    Product Description

    Ubiquitin-like-specific protease 1 (Ulp1) is a small ubiquitin-related modifier (SUMO) protease and member of the cysteine protease superfamily.1 It is composed of an N-terminal regulatory domain and a C-terminal protease domain.2 Ulp1 processes Smt3, the yeast ortholog to human SUMO, into its mature form by cleavage of the alanine-threonine-tyrosine residues at the C-terminal end.1 It also deconjugates Smt3 from Smt3-protein conjugates, which is required for normal cell cycle progression in S. cerevisiae, and can cleave human SUMO-tagged proteins.3,2,1 A version of Ulp1 lacking the N-terminal regulatory domain does not localize to the nuclear pore complex and can desumoylate certain Ulp2 targets. Cayman’s Ubiquitin-like-specific Protease 1 (S. cerevisiae, recombinant) protein can be used for SUMO tag cleavage from SUMO fusion proteins.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Mossessova, E., and Lima, C.D. Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast. Mol. Cell 5(5), 865-876 (2000).

    2. Li, S.-J., and Hochstrasser, M. The Ulp1 SUMO isopeptidase: distinct domains required for viability, nuclear envelope localization, and substrate specificity. J. Cell. Biol. 160(7), 1069-1081 (2003).

    3. Li, S.-J., and Hochstrasser, M. A new protease required for cell-cycle progression in yeast. Nature 398(6724), 246-251 (1999).