추천 제품
일반 설명
Pyrophosphatase from E coli (E-PPase) has a broader pH optimum and contains four divalent cations per subunit. It comprises 175 amino acids with additional aspartate residue in the active site cavity. Structurally E-PPase is a homohexamer with six identical 20 kDa subunits. Magnesium is a cofactor for E-PPase.
애플리케이션
Inorganic pyrophosphatase (PPase) is a ubiquitous enzyme catalyzing the reaction PPi + H2O → 2Pi.
It plays an important role in protein, RNA, and DNA synthesis.
It plays an important role in protein, RNA, and DNA synthesis.
Pyrophosphatase, Inorganic from Escherichia coli has been used as a component of transcription buffer.
Pyrophosphatase, inorganic from Escherichia coli has been used in assay for conjugation of ubiquitin and ubiquitin-like proteins. It has been used for one-pot three-enzyme system for synthesis of Lewis x and sialyl Lewis x antigens.
생화학적/생리학적 작용
Pyrophosphatase from E coli (E-PPase) is an essential enzyme in yeast and bacteria The active site residues are crucial for binding to magnesium.
기타 정보
A homohexameric protein containing 175 amino acid residues per subunit, its activity is Mg2+ dependent. It is a relatively thermostable protein.
단위 정의
One unit will release 1.0 μmole of inorganic orthophosphate per minute at pH 9 at 25 °C.
물리적 형태
Lyophilized powder in Tris-buffered salts containing protease inhibitors
신호어
Warning
유해 및 위험 성명서
Hazard Classifications
Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3
표적 기관
Respiratory system
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
개인 보호 장비
Eyeshields, Gloves, type N95 (US)
시험 성적서(COA)
제품의 로트/배치 번호를 입력하여 시험 성적서(COA)을 검색하십시오. 로트 및 배치 번호는 제품 라벨에 있는 ‘로트’ 또는 ‘배치’라는 용어 뒤에서 찾을 수 있습니다.
이미 열람한 고객
Ngoc Truongvan et al.
Nature communications, 13(1), 4789-4789 (2022-08-16)
The covalent modification of target proteins with ubiquitin or ubiquitin-like modifiers is initiated by E1 activating enzymes, which typically transfer a single modifier onto cognate conjugating enzymes. UBA6 is an unusual E1 since it activates two highly distinct modifiers, ubiquitin
Christopher E Berndsen et al.
Analytical biochemistry, 418(1), 102-110 (2011-07-21)
Ubiquitination is a widely studied regulatory modification involved in protein degradation, DNA damage repair, and the immune response. Ubiquitin is conjugated to a substrate lysine in an enzymatic cascade involving an E1 ubiquitin-activating enzyme, an E2 ubiquitin-conjugating enzyme, and an
Hai Yu et al.
Current protocols in chemical biology, 4, 233-247 (2012-09-01)
L-Fucose has been found abundantly in human milk oligosaccharides, bacterial lipopolysaccharides, glycolipids, and many
The structure of E. coli soluble inorganic pyrophosphatase at 2.7
Kankare J, et al.
Protein engineering, design & selection : PEDS, 7(7), 823-830 (1994)
Rahul Sadavarte et al.
Biotechnology progress, 33(1), 133-139 (2016-11-01)
Heterologous overexpression of genes in Escherichia coli has made it possible to obtain high titers of recombinant proteins. However, this can result in the formation of aggregated protein particles known as 'inclusion bodies'. Protein sequestered as inclusion body is inactive
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