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SUMO Protease

SUMO Protease
1 of 1 reviewers received a sample product or took part in a promotion

His tagged recombinant protein, lyophilized powder

Synonyme(s) :

Small Ubiquitin-like Modifier Protease, ULP, Ubiquitin like protease, Ubiquitin-homology domain protein PIC1, Ubl-specific protease 1

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2500 UNITS
610,00 $

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2500 UNITS
610,00 $

About This Item

Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

610,00 $


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Produit recombinant

expressed in E. coli

Niveau de qualité

Essai

≥95% (SDS-PAGE)

Forme

lyophilized powder

Poids mol.

27 kDa

Conditions d'expédition

ambient

Température de stockage

−20°C

Description générale

SUMO proteases are a general class of enzymes that specifically remove the post-translational protein modification (PTM) known as small ubiquitin-related modifier (SUMO), which falls into the PTM class of ubiquitin and/or ubiquitin-like proteins (UBL). The enzyme commonly referred to as ‘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 specifically cleaves the SUMO moiety in a ‘scarless′ manner. SUMO protease recognizes the tertiary structure of the Ubiquitin-like SUMO domain and hydrolyzes the peptide bond in the x–Gly–Gly–x sequence after the Gly-Gly bond, at the C-terminus of the SUMO domain. In addition to 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. A histidine tag can also be added at the N-terminus of the SUMO domain as a purification tag. This SUMO protease product carries a 6x histidine tag. Thus it can be easily removed together with the cleaved SUMO domain, following the digestion reaction
SUMO protease is active over a wide range of temperatures (2–30 °C), ionic strengths (0–400 mM NaCl), and pH ranges (6–8.5). However, its activity may vary depending on the substrate and conditions. Researchers will need to optimize their specific reaction conditions. As an initial suggestion, 20 units of SUMO protease can be used per mg of target protein for 1 hour at 30 °C, or overnight at 2–8 °C. The cleavage efficiency can then be estimated by SDS-PAGE. If necessary, the amount of SUMO protease can then be adjusted. SUMO protease works better in the presence of reducing agents, e.g., 0.5–2 mM DTT. DTT in the reaction mixture can significantly enhance cleavage efficiency, especially during longer incubations
Store the reconstituted product at –20 °C. It is recommended to reconstitute the enzyme in 100 μL of either water or 50% glycerol (v/v), supplemented with 1 mM DTT. Solutions in water/DTT should be stored in frozen aliquots to avoid freeze-thaw cycles, which can adversely affect the protease activity.

Définition de l'unité

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

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 2

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


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Camille Le Gall et al.
Journal for immunotherapy of cancer, 10(4) (2022-04-17)
Type 1 conventional dendritic cells (cDC1s) are characterized by their ability to induce potent CD8+ T cell responses. In efforts to generate novel vaccination strategies, notably against cancer, human cDC1s emerge as an ideal target to deliver antigens. cDC1s uniquely
Chuanwu Xia et al.
iScience, 24(10), 103153-103153 (2021-10-15)
The dual function protein ACAD9 catalyzes α,β-dehydrogenation of fatty acyl-CoA thioesters in fatty acid β-oxidation and is an essential chaperone for mitochondrial respiratory complex I (CI) assembly. ACAD9, ECSIT, and NDUFAF1 interact to form the core mitochondrial CI assembly complex.
Lin Liu et al.
Advanced healthcare materials, 10(20), e2100956-e2100956 (2021-08-10)
Novel methods that enable sensitive, accurate and rapid detection of RNA would not only benefit fundamental biological studies but also serve as diagnostic tools for various pathological conditions, including bacterial and viral infections and cancer. Although highly sensitive, existing methods
Sho W Suzuki et al.
eLife, 10 (2021-09-16)
Membrane protein recycling systems are essential for maintenance of the endosome-lysosome system. In yeast, retromer and Snx4 coat complexes are recruited to the endosomal surface, where they recognize cargos. They sort cargo and deform the membrane into recycling tubules that
Matthijs P Hoelscher et al.
Nature communications, 13(1), 5856-5856 (2022-10-05)
Antimicrobial peptides (AMPs) kill microbes or inhibit their growth and are promising next-generation antibiotics. Harnessing their full potential as antimicrobial agents will require methods for cost-effective large-scale production and purification. Here, we explore the possibility to exploit the high protein

Articles

Proteases for biotinylated tag removal for protein purification workflows with related reagents and technical resources.

Questions

  1. Please state if this protease is specific to cleave off Human SUMO (there are various SUMO proteins used in expression studies).

    1 answer
    1. SUMO protease recognizes the tertiary structure of the Ubiquitin-like SUMO domain, hydrolyzing the peptide bond in the x–Gly–Gly–x sequence after the Gly-Gly bond, at the C-terminus of the SUMO domain. This protease will work with whichever species such a situation appears. While this product is not tested specifically for this application, product S0439, a recombinant SUMO-1 product, has been recommended for use as a positive control substrate. This enzyme is expected to be suitable for use in Human SUMO studies.

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1 of 1 reviewers received a sample product or took part in a promotion

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