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Merck
모든 사진(2)

주요 문서

N9914

Sigma-Aldrich

Polynucleotide phosphorylase from Synechocystis sp.

recombinant, expressed in E. coli

동의어(들):

PNPase, Polyribonucleotide Nucleotidyltransferase

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크기 선택

100 μG
₩670,306

₩670,306


구입 가능 여부는 고객센터에 문의하십시오.

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크기 선택

보기 변경
100 μG
₩670,306

About This Item

효소 위원회 번호:
MDL number:
UNSPSC 코드:
12352204
NACRES:
NA.54

₩670,306


구입 가능 여부는 고객센터에 문의하십시오.

벌크 견적 요청

생물학적 소스

bacterial (Synechocystis sp.)

Quality Level

재조합

expressed in E. coli

설명

Histidine tagged

분석

90% (SDS-PAGE)

양식

solution

특이 활성도

≥500 units/mg protein

분자량

85 kDa

기술

cell based assay: suitable

적합성

suitable for molecular biology

응용 분야

cell analysis

배송 상태

dry ice

저장 온도

−70°C

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일반 설명

Polynuclotide phosphorlyase in spinach chloroplasts acts as a exonuclease and a poly(A) polymerase. [1]

애플리케이션

Polynucleotide phosphorylase has been used in a study to discover that a major function of PNPase is the synthesis of CDP. [2] It has also been used in a study to investigate the enzyme responsible for RNA 3′-tail synthesis in S. coelicolor. [3]

생화학적/생리학적 작용

Polynucleotide phosphorylase (PNPase) is a bifunctional enzyme with a phosphorolytic 3′ to 5′ exoribonuclease activity and a 3′-terminal oligonucleotide polymerase activity.
Polynucleotide phosphorylase localizes to the intermembrane space of mitochondria and has a critical function in regulating mitochondrial homeostasis in human cells. [4]

단위 정의

One unit will polymerize 1.0 μmole of ADP, releasing 1.0 μmole of inorganic phosphate in 15 minutes, at pH 9.1 at 37 °C.
Supplied as a solution in 20 mM Hepes buffer pH 7.9, 0.1 mM EDTA, 2 mM DTT, 12.5 mM MgCl2, 60 mM KCl, 20% (w/v) Glycerol

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable


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문서 라이브러리 방문

Patricia Bralley et al.
Microbiology (Reading, England), 152(Pt 3), 627-636 (2006-03-04)
As in other bacteria, 3'-tails are added post-transcriptionally to Streptomyces coelicolor RNA. These tails are heteropolymeric, and although there are several candidates, the enzyme responsible for their synthesis has not been definitively identified. This paper reports on three candidates for
Ruth Rott et al.
The Journal of biological chemistry, 278(18), 15771-15777 (2003-02-26)
The mechanism of RNA degradation in Escherichia coli involves endonucleolytic cleavage, polyadenylation of the cleavage product by poly(A) polymerase, and exonucleolytic degradation by the exoribonucleases, polynucleotide phosphorylase (PNPase) and RNase II. The poly(A) tails are homogenous, containing only adenosines in
G G Liou et al.
Proceedings of the National Academy of Sciences of the United States of America, 98(1), 63-68 (2001-01-03)
RNase E isolated from Escherichia coli is contained in a multicomponent "degradosome" complex with other proteins implicated in RNA decay. Earlier work has shown that the C-terminal region of RNase E is a scaffold for the binding of degradosome components
A Danchin
DNA research : an international journal for rapid publication of reports on genes and genomes, 4(1), 9-18 (1997-02-28)
Genome comparison permits identification of chromosome regions conserved during evolution. Bacillus subtilis and Escherichia coli are so distant that there exists very few conserved landmarks in their genome organisation. Analysis of the conserved cmk rpsA cluster pinpointed the importance of
Steven W Hardwick et al.
Open biology, 2(4), 120028-120028 (2012-06-23)
Polynucleotide phosphorylase (PNPase) is an exoribonuclease that cleaves single-stranded RNA substrates with 3'-5' directionality and processive behaviour. Its ring-like, trimeric architecture creates a central channel where phosphorolytic active sites reside. One face of the ring is decorated with RNA-binding K-homology

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