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
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| Size/SKU | Availability | Price |
|---|---|---|
2500 units | Available to ship TODAYfromMILWAUKEE | $460.00 |
About This Item
NACRES:
NA.54
UNSPSC Code:
12352202
Form:
aqueous solution
Assay:
≥90% (SDS-PAGE)
Recombinant:
expressed in E. coli
Mol wt:
27 kDa
recombinant
expressed in E. coli
Quality Segment
assay
≥90% (SDS-PAGE)
form
aqueous solution
mol wt
27 kDa
concentration
≥25,000 units/mL
shipped in
dry ice
storage temp.
−20°C
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.
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).
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.
1 of 1
This Item | |||
|---|---|---|---|
| assay ≥90% (SDS-PAGE) | assay ≥95% (SDS-PAGE) | assay ≥90% | assay - |
| recombinant expressed in E. coli | recombinant expressed in E. coli | recombinant expressed in E. coli | recombinant - |
| concentration ≥25,000 units/mL | concentration - | concentration 0.8-1.2 mg/mL | concentration - |
| mol wt 27 kDa | mol wt 27 kDa | mol wt 22 kDa | mol wt - |
| form aqueous solution | form lyophilized powder | form aqueous solution | form buffered aqueous solution |
| storage temp. −20°C | storage temp. −20°C | storage temp. −20°C | storage temp. −20°C |
Storage Class
10 - Combustible liquids
flash_point_f
Not applicable
flash_point_c
Not applicable
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