Pular para o conteúdo
Merck
Todas as fotos(2)

Documentos Principais

N9914

Sigma-Aldrich

Polynucleotide phosphorylase from Synechocystis sp.

recombinant, expressed in E. coli

Sinônimo(s):

PNPase, Polyribonucleotide Nucleotidyltransferase

Faça loginpara ver os preços organizacionais e de contrato

Selecione um tamanho

100 μG
R$ 3.072,00

R$ 3.072,00


Check Cart for Availability

Solicite uma grande encomenda

Selecione um tamanho

Alterar visualização
100 μG
R$ 3.072,00

About This Item

Número da licença da enzima:
Número MDL:
Código UNSPSC:
12352204
NACRES:
NA.54

R$ 3.072,00


Check Cart for Availability

Solicite uma grande encomenda

fonte biológica

bacterial (Synechocystis sp.)

Nível de qualidade

recombinante

expressed in E. coli

descrição

Histidine tagged

Ensaio

90% (SDS-PAGE)

Formulário

solution

atividade específica

≥500 units/mg protein

peso molecular

85 kDa

técnica(s)

cell based assay: suitable

adequação

suitable for molecular biology

aplicação(ões)

cell analysis

Condições de expedição

dry ice

temperatura de armazenamento

−70°C

Procurando produtos similares? Visita Guia de comparação de produtos

Descrição geral

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

Aplicação

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]

Ações bioquímicas/fisiológicas

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]

Definição da unidade

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

Código de classe de armazenamento

12 - Non Combustible Liquids

Classe de risco de água (WGK)

WGK 1

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable


Escolha uma das versões mais recentes:

Certificados de análise (COA)

Lot/Batch Number

Não está vendo a versão correta?

Se precisar de uma versão específica, você pode procurar um certificado específico pelo número do lote ou da remessa.

Já possui este produto?

Encontre a documentação dos produtos que você adquiriu recentemente na biblioteca de documentos.

Visite a Biblioteca de Documentos

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
Yu-Chuan Wang et al.
Acta crystallographica. Section F, Structural biology and crystallization communications, 68(Pt 10), 1247-1250 (2012-10-03)
Bacterial polynucleotide phosphorylase (PNPase) is a 3'-5' processive exoribonuclease that participates in mRNA turnover and quality control of rRNA precursors in many bacterial species. It also associates with the RNase E scaffold and other components to form a multi-enzyme RNA

Questions

Reviews

No rating value

Active Filters

Nossa equipe de cientistas tem experiência em todas as áreas de pesquisa, incluindo Life Sciences, ciência de materiais, síntese química, cromatografia, química analítica e muitas outras.

Entre em contato com a assistência técnica