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SUMO Protease

No Product Name Cat.# Conc Size Price(₩) Add
1 SUMO Protease PR001S 1 unit/μl 250 units ₩ 300,000 추가
2 SUMO Protease PR001M 1 unit/μl 500 units ₩ 540,000 추가
3 SUMO Protease PR001L 1 unit/μl 1,250 units ₩ 1,200,000 추가
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Product description
SUMO Protease (Ulp1, Ubl-specific protease 1) from yeast is expressed and purified from E. coli to near homogeneity, SUMO Protease cleaves in a highly specific manner, recognizing the tertiary structure of the ubiquitin-like (UBL) protein, SUMO rather than an amino acid sequence. The protease can be used to cleave SUMO from recombinant fusion proteins, it cleaves a peptide bond located after the C-terminal diglycine residues of SUMO. The optimal temperature for cleavage is 30oC; however, the enzyme is active over wide ranges of temperature and pH (pH 7.0-9.0).

Characteristics
- Molecular weight : 25 kDa
- Reaction temperature : 2-37℃ (30℃ is optimal)
- Optimal pH range : pH 5.5-9.5

Applications
- Removal of fusion tag from recombinant proteins

Quality control
- Purity : >99% on SDS-PAGE
- Endonuclease-free
- Exonuclease-free
- RNase-free

Unit definition
One unit of SUMO Protease is the amount of enzyme required to cleaves 100 μg of SUMO-MetGFP substrate in 1X SUMO Protease buffer at 30°C for 1 hr.

Storage buffer
50 mM Tris-HCl (pH 8.0), 150 mM NaCl, 5 mM DTT, 4% trehalose, 50% glycerol

10X SUMO Protease buffer
- Salt plus buffer : 500 mM Tris-HCl, pH 8.0, 2% Igepal (NP-40), 1.5 M NaCl, 10 mM DTT
- Salt free buffer : 500 mM Tris-HCl, pH 8.0, 2% Igepal (NP-40), 10 mM DTT

Standard reaction conditions

10X SUMO Protease buffer +/-salt

20 μl

SUMO protease (1 units/μl)

10 μl

Fusion protein (substrate, 1 μg/μl)

20 μl

Distilled water

up to 200 μl

→ Incubate the reaction mixture at 30.

→ Withdraw 20 μl aliquots at 1, 2, 4, and 6 hr after incubation.

→ Add 20 μl of 2X SDS sample buffer to the aliquots, boil the mixture, and analyze by SDS-PAGE

 to check.

→ Keep the rest of the reaction mixture at -20 until analysis is completed


Cautions
- Avoid repeated cycles of freezing-thawing.

- This enzyme is active in NaCl from 100 mM to 300 mM (150 mM is optimum).
- Keep the imidazole concentration lower than 150 mM. Concentrations higher than 150 mM can inhibit the

  activity of this protease.

  
        

Figure 1. Removal of SUMO from SUMO-fusion proteins by SUMO protease.
A SUMO-fusion protein (20 μg), in which SUMO is fused to its Nterminus, was incubated at 4, 16, 21, or 30℃ for 1 hr with 10 unit of SUMO proteases from Enzynomics (Cat.# PR001) or other company (Supplier A). At all temperatures tested, SUMO was released from the substrates by SUMO proteases of both companies. The optimal temperature for SUMO proteases is 30℃ In excess of enzymes, however, all substrates can be cleaved over a wide range of temperatures. Mw, molecular weight marker. Lane 9, substrate only control. The protein substrate used, cleavage products, and SUMO released by digestion are indicated by arrows.



● Material Safety Data Sheet

- Enzynomics_MSDS_PR001_SUMO Protease_E

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