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        <h1 class="post-title" style="">SUMO-tag protease</h1>
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                            <span>Last updated on 2026-10-12</span>
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<p class="wp-block-paragraph"><strong>SUMO Protease</strong></p>


<p class="wp-block-paragraph"><strong>1. Product Information</strong></p>


<figure class="wp-block-table"><table class="has-fixed-layout"><tbody><tr><td>Product Name</td><td>Catalog No.</td><td>Size</td></tr><tr><td rowspan="3">SUMO Protease</td><td><strong>ZS00021ES25</strong></td><td><strong>25 KU</strong></td></tr><tr><td><strong>ZS0002ES50</strong></td><td><strong>50 KU</strong></td></tr><tr><td><strong>ZS0002ES100</strong></td><td><strong>100 KU</strong></td></tr></tbody></table></figure>


<p class="wp-block-paragraph"><strong>2. Product Description</strong></p>


<p class="wp-block-paragraph"><strong>SUMO Protease</strong> (also known as Ulp) is a recombinant fragment of ULP1 (Ubl-specific protease 1) from <em>Saccharomyces cerevisiae</em>. It exhibits high specificity toward SUMO protein fusions by recognizing the tertiary structure of SUMO rather than amino acid sequences. SUMO protease recognizes the full-length 100-amino-acid SUMO (Small Ubiquitin-like Modifier) tag and efficiently cleaves SUMO from fusion proteins. Compared with recognition sites of proteases such as EK and TEV, SUMO protease delivers superior cleavage specificity due to its long recognition sequence. It maintains high activity over a wide range of reaction conditions, including temperature (4–30℃) and pH (5.5–9.5). SUMO protease carries a poly-His tag, enabling removal of SUMO protease via affinity chromatography for target protein purification.</p>


<p class="wp-block-paragraph"><strong>3. Product Properties</strong></p>


<figure class="wp-block-table"><table class="has-fixed-layout"><tbody><tr><td>Source</td><td><em>E.coli</em></td></tr><tr><td>Molecular Weight</td><td>26.55 kDa</td></tr><tr><td>Purity</td><td>≥90%, ≥95%</td></tr><tr><td>Enzyme Activity</td><td>200–250 U/μL</td></tr><tr><td>Specific Activity</td><td>≥1.5×10<sup>6</sup> U/mg protein</td></tr><tr><td>Storage Buffer</td><td>500 mM Tris-HCl, pH 8.0, 2% Igepal (NP-40), 1.5 M NaCl, 10 mM DTT</td></tr><tr><td>Unit Definition</td><td>One unit (1 U) is defined as the amount of SUMO Protease required to cleave ≥85% of 2 μg fusion protein containing the cleavage site within 1 hour at 30℃.</td></tr></tbody></table></figure>


<p class="wp-block-paragraph"><strong>4. Protocol</strong></p>


<p class="wp-block-paragraph">4.1. Prepare the recommended reaction system in EP tube</p>


<p class="wp-block-paragraph"><strong>Component &nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;Volume</strong></p>


<p class="wp-block-paragraph">Fusion protein &nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;20 μg</p>


<p class="wp-block-paragraph">10X SUMO Protease Buffer &nbsp;&nbsp;&nbsp;&nbsp;20 μL</p>


<p class="wp-block-paragraph">ddH<sub>2</sub>O &nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;to 190 μL</p>


<p class="wp-block-paragraph">SUMO Protease &nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;10 μL</p>


<p class="wp-block-paragraph">Total volume &nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;200 μL</p>


<p class="wp-block-paragraph">4.2. Incubate at 30℃. Transfer 30 μL aliquots of the reaction mixture into separate EP tubes at 0.5 h, 1 h, 2 h and 3 h.</p>


<p class="wp-block-paragraph">4.3. Add 30 μL 2×SDS Loading Buffer to each aliquot and store at -20℃.</p>


<p class="wp-block-paragraph">4.4. Once all time-point sampling is finished, boil samples for 5 min and analyze by SDS-PAGE to determine optimal incubation time.</p>


<p class="wp-block-paragraph">【Note】If the fusion protein requires low-temperature treatment, overnight incubation at 4℃ with increased SUMO protease dosage is recommended to guarantee cleavage efficiency.</p>


<p class="wp-block-paragraph">4.5. SUMO protease can be removed from the reaction mixture after cleavage by affinity chromatography using His-tag purification resin.</p>


<p class="wp-block-paragraph"><strong>5. Storage Conditions</strong></p>


<p class="wp-block-paragraph">Long-term storage at -80℃; or store at -20℃ after thawing.</p>


<p class="wp-block-paragraph"><strong>6. Product Advantages</strong></p>


<p class="wp-block-paragraph">Animal-origin free: recombinantly produced, free of exogenous viral contaminants; no animal-derived raw materials used in production.</p>


<p class="wp-block-paragraph">Consistent quality: mass production enables stable continuous batch supply with negligible batch-to-batch variation.</p>


<p class="wp-block-paragraph">High purity: high specific activity; host cell protein residue below bioproduct limits.</p>


<p class="wp-block-paragraph"><strong>Precautions:</strong></p>


<p class="wp-block-paragraph">1. For optimal cleavage performance, the recombinant protein should be partially or fully purified;</p>


<p class="wp-block-paragraph">2. For most fusion proteins, the optimal NaCl concentration in reaction buffer is 150 mM. Adjust NaCl between 100 mM–300 mM for best results according to practical conditions. Take the salt concentration carried by fusion protein into account in experiments;</p>



<p class="wp-block-paragraph">3. Imidazole concentration should be kept below 150 mM; higher concentration will inhibit SUMO protease activity.</p>


<p class="wp-block-paragraph">4. This product is for research use only. Not for pharmaceutical, clinical therapeutic, food or cosmetic applications.</p>

