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Merck
모든 사진(1)

주요 문서

SAE0101

Sigma-Aldrich

SUMO Protease, Biotin tagged

Recombinant protein, aqueous solution, ≥25,000 units/mL

동의어(들):

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

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About This Item

UNSPSC 코드:
12352202
NACRES:
NA.54

재조합

expressed in E. coli

Quality Level

분석

≥90% (SDS-PAGE)

양식

aqueous solution

분자량

27 kDa

농도

≥25,000 units/mL

배송 상태

dry ice

저장 온도

−20°C

관련 카테고리

일반 설명

SUMO proteases are enzymes that specifically cleave the post-translational protein modification (PTM) known as small ubiquitin-related modifier (SUMO). SUMO falls into the PTM class of ubiquitin and/or ubiquitin-like proteins (UBL).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 cleaves specifically the SUMO moiety in a ‘scarless′ manner. After recognizing the tertiary structure of the Ubiquitin-like SUMO domain, SUMO protease hydrolyzes the peptide bond in the x–Gly–Gly–x sequence after the Gly-Gly bond, at the C-terminus of the SUMO domain. Besides the 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. Since this recombinant protease does not contain any coman protein purification tag it can be used for on-column cleavage of column bound SUMO fusion protein. Sumo protease with Biotin tag can be easily removed at the end of the digestion reaction.

애플리케이션

This biotin-tagged SUMO protease product is designed to be used for on-column cleavage of SUMO fusion proteins. This method specifically cleaves the protein of interest from a column-bound SUMO fusion protein, leaving the SUMO domain bound to the affinity column (e.g. Ni-NTA column) and eluting only the protein of interest. This method is advantageous to post-elution cleavage for several reasons:

Eliminates most of the impurities normally associated with purification on Ni-chelating columns.

  • Allows much gentler elution conditions, with an added flexibility in the composition of the elution buffer.
  • Assist preventing protein aggregation and inactivation.
  • Following cleavage, the protease can be efficiently removed by using any avidin-conjugated or streptavidin-conjugated beads.

This biotin-tagged SUMO protease has been enzymatically biotinylated without affecting its proteolytic activity. It does not include any additional protein purification tag (e.g., histidine-tag or GST).

단위 정의

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 Code

10 - Combustible liquids

WGK

WGK 1

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable


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