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SUMO Protease Protein, S. cerevisiae, Recombinant (His)
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Catalog No. TMPS-00130 Copy Product Info
SUMO protease, also known as Ulp, is a highly specific enzyme that removes small ubiquitin-like modifier (SUMO) from recombinant SUMO fusion proteins. Unlike proteases such as enterokinase or TEV, which recognize linear amino acid sequences, SUMO protease recognizes the native tertiary structure of SUMO, allowing precise cleavage without leaving extra residues at the cleavage site.
This recombinant SUMO protease is derived from Saccharomyces cerevisiae, expressed in E. coli, and purified to obtain high yields of active enzyme under animal-free conditions. It is well suited for applications in drug and vaccine development, protein manufacturing, and other research uses. A C-terminal 6×His tag is included to enable easy removal of the protease following cleavage via Ni²⁺ affinity purification.
This recombinant SUMO protease is derived from Saccharomyces cerevisiae, expressed in E. coli, and purified to obtain high yields of active enzyme under animal-free conditions. It is well suited for applications in drug and vaccine development, protein manufacturing, and other research uses. A C-terminal 6×His tag is included to enable easy removal of the protease following cleavage via Ni²⁺ affinity purification.
| Pack Size | Price | USA Stock | Global Stock | Quantity |
|---|---|---|---|---|
| 250 U | $113 | 7-10 days | 7-10 days | |
| 1000 U | $339 | 7-10 days | 7-10 days |
For In stock only · Estimated delivery: USA Stock (1-2 days) Global Stock (5-7 days)
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For research use only—not for human use. No sales to individuals. Use as intended only.
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Purity:≥ 95% as analyzed by SDS-PAGE
Appearance:Liquid
Color:Transparent
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Product Introduction
Bioactivity
Chemical Properties
Storage & Solubility Information
| Bioactivity | 10 U/μl Unit definition: One unit of SUMO Protease cleaves ≥ 85% of 2 μg control substrate in 1 h at 30℃ |
| Description | SUMO protease, also known as Ulp, is a highly specific enzyme that removes small ubiquitin-like modifier (SUMO) from recombinant SUMO fusion proteins. Unlike proteases such as enterokinase or TEV, which recognize linear amino acid sequences, SUMO protease recognizes the native tertiary structure of SUMO, allowing precise cleavage without leaving extra residues at the cleavage site.
This recombinant SUMO protease is derived from Saccharomyces cerevisiae, expressed in E. coli, and purified to obtain high yields of active enzyme under animal-free conditions. It is well suited for applications in drug and vaccine development, protein manufacturing, and other research uses. A C-terminal 6×His tag is included to enable easy removal of the protease following cleavage via Ni²⁺ affinity purification. |
| Species | Saccharomyces cerevisiae |
| Tag | His |
| Protein Purity | ≥ 95% as determined by SDS-PAGE |
| Endotoxin | < 0.2 EU/μg of protein as determined by the LAL method. |
| Stability & Storage | Upon receiving, the product remains stable for up to 6 months at -20 °C. This product is stable for up to 1 week at 37 °C. Avoid repeated freeze-thaw cycles by making single-use aliquots before the solution is stored at -20 °C. |
| Shipping | In general, lyophilized powders are shipped with blue ice, while solutions are shipped with dry ice. |
| Research Background |
| Molecular Weight | 27 kDa (Predicted) |
| Storage | Lyophilized powder: -20~-80°C for 1 year | Solution: -80°C for 6 months |
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Please see Inhibitor Handling Instructions for more frequently ask questions. Topics include: how to prepare stock solutions, how to store products, and cautions on cell-based assays & animal experiments, etc
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Related Tags: SUMO Protease Protein, S. cerevisiae, Recombinant (His) chemical structure | SUMO Protease Protein, S. cerevisiae, Recombinant (His) molecular weight
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