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)
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이미 열람한 고객
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)
Microbial inorganic pyrophosphatases.
R Lahti
Microbiological reviews, 47(2), 169-178 (1983-06-01)
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
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
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