SAE0101

SUMO Protease, Biotin tagged

Recombinant protein, aqueous solution, ≥25,000 units/mL

• Synonym(s): Small Ubiquitin-like Modifier Protease, ULP, Ubiquitin like protease, Ubiquitin-homology domain protein PIC1, Ubl-specific protease 1
• NACRES: NA.54
• UNSPSC Code: 12352202
• Form: aqueous solution
• Assay: ≥90% (SDS-PAGE)
• Recombinant: expressed in E. coli
• Mol wt: 27 kDa

Properties

• recombinant: expressed in E. coli
• Quality Segment: 200
• assay: ≥90% (SDS-PAGE)
• form: aqueous solution
• mol wt: 27 kDa
• concentration: ≥25,000 units/mL
• shipped in: dry ice
• storage temp.: −20°C

Description

General description

SUMO proteases are enzymes that specifically cleave the post-translational protein modification (PTM) known as small ubiquitin-related modifier (SUMO). SUMO falls into the PTM class of ubiquitin and/or ubiquitin-like proteins (UBL).SUMO protease is the Ubl-specific protease 1 (Ulp1) from Saccharomyces cerevisiae. This was the first of this class of enzymes to be isolated. SUMO protease cleaves specifically the SUMO moiety in a ‘scarless′ manner. After recognizing the tertiary structure of the Ubiquitin-like SUMO domain, SUMO protease hydrolyzes the peptide bond in the x–Gly–Gly–x sequence after the Gly-Gly bond, at the C-terminus of the SUMO domain. Besides the cleavage of natural SUMO-modified proteins, SUMO protease is used to cleave recombinant SUMO fusion proteins. The SUMO domain is a known solubility-enhancing fusion tag used in recombinant protein expression. Since this recombinant protease does not contain any coman protein purification tag it can be used for on-column cleavage of column bound SUMO fusion protein. Sumo protease with Biotin tag can be easily removed at the end of the digestion reaction.

Application

This biotin-tagged SUMO protease product is designed to be used for on-column cleavage of SUMO fusion proteins. This method specifically cleaves the protein of interest from a column-bound SUMO fusion protein, leaving the SUMO domain bound to the affinity column (e.g. Ni-NTA column) and eluting only the protein of interest. This method is advantageous to post-elution cleavage for several reasons:

Eliminates most of the impurities normally associated with purification on Ni-chelating columns.

• Allows much gentler elution conditions, with an added flexibility in the composition of the elution buffer.
• Assist preventing protein aggregation and inactivation.
• Following cleavage, the protease can be efficiently removed by using any avidin-conjugated or streptavidin-conjugated beads.

This biotin-tagged SUMO protease has been enzymatically biotinylated without affecting its proteolytic activity. It does not include any additional protein purification tag (e.g., histidine-tag or GST).

Other Notes

One enzyme unit is defined as the amount that will cut 90% of 100 pmol of SUMO-GST in 1 hour at 30°C.

Safety Information

• Storage Class: 10 - Combustible liquids
• wgk: WGK 1
• flash_point_f: Not applicable
• flash_point_c: Not applicable