Saltar al contenido
Merck

SAE0067

Sigma-Aldrich

SUMO Protease

His tagged recombinant protein, lyophilized powder

Sinónimos:

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

Iniciar sesiónpara Ver la Fijación de precios por contrato y de la organización


About This Item

UNSPSC Code:
12352204
NACRES:
NA.54

recombinant

expressed in E. coli

Quality Level

assay

≥95% (SDS-PAGE)

form

lyophilized powder

mol wt

27 kDa

shipped in

ambient

storage temp.

−20°C

General description

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.

Unit Definition

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

Storage Class

11 - Combustible Solids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

¿Ya tiene este producto?

Encuentre la documentación para los productos que ha comprado recientemente en la Biblioteca de documentos.

Visite la Librería de documentos

Los clientes también vieron

Slide 1 of 1

1 of 1

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.
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
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
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

Artículos

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

Nuestro equipo de científicos tiene experiencia en todas las áreas de investigación: Ciencias de la vida, Ciencia de los materiales, Síntesis química, Cromatografía, Analítica y muchas otras.

Póngase en contacto con el Servicio técnico