This enzyme is a homodimer comprised of 27 kDa subunits.
T4330
Endonuclease
recombinant, expressed in E. coli
Sinônimo(s):
Endonuclease from Serratia marcescens
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50000 UNITS
R$ 2.702,00
R$ 2.702,00
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50000 UNITS
R$ 2.702,00
About This Item
Número CAS:
Número MDL:
Código UNSPSC:
12352204
NACRES:
NA.54
R$ 2.702,00
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fonte biológica
Serratia marcescens
Nível de qualidade
recombinante
expressed in E. coli
Formulário
liquid
concentração
≥200,000 units/mL
técnica(s)
DNA purification: suitable
adequação
suitable for cell lysis
aplicação(ões)
life science and biopharma
temperatura de armazenamento
−20°C
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Descrição geral
Endonuclease from Serratia marcescens is a dimer containing two identical monomeric units with distinct protein folds. The core contains a six-stranded antiparallel β-sheet flanked by α-helices on either side. Each monomer bears one active site. This enzyme is a magnesium-dependent nucleases.[1]
Aplicação
Usado para remoção de ácidos nucleicos de amostras proteicas.
Turbonuclease from Serratia marcescens has been used for cell lysis during proximity biotinylation assay (BioID) and affinity-purification[2]. It has also been used as a component of lysis buffer for protein extraction from cell lines for affinity purification studies.[3]
Turbonuclease has been used in a study to assess the TY3 gag3 spacer effect on intracellular condensation and uncoating. [4]
Ações bioquímicas/fisiológicas
Digere DNA e RNA nativos ou desnaturados por calor.
Endonuclease from Serratia marcescens is effective against both single- and double-stranded DNA and RNA. It mediates the digestion of the 3′ O—P bond resulting in oligonucleotides ending with 5′ monophosphate. The activity of this enzyme is known to be less affected by the reducing and chaotropic agents. It is highly stable at room temperature. This endonuclease eliminates the undesired nucleic acids in downstream processing.[1]
Turbonuclease provides a nuclease treatment by reducing viscosity and degrading RNA, genomic DNA, baculovirus DNA, and unencapsidated vector DNA.[5]
Definição da unidade
One unit will digest sonicated salmon sperm DNA to acid-soluble oligonucleotides equivalent to a ΔA260 of 1.0 in 30 min at pH 8.0 at 37 °C.
forma física
Supplied as a solution in 50 mM Tris-HCl, pH 8.0 and 50 mM NaCl
Código de classe de armazenamento
10 - Combustible liquids
Classe de risco de água (WGK)
WGK 2
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
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M D Miller et al.
Journal of molecular biology, 288(5), 975-987 (1999-05-18)
Serratia endonuclease is an important member of a class of magnesium dependent nucleases that are widely distributed in nature. Here, we describe the location and geometry of a magnesium-water cluster within the active site of this enzyme. The sole protein
Kristina Clemens et al.
Journal of virology, 85(7), 3055-3066 (2011-01-29)
Cells expressing the yeast retrotransposon Ty3 form concentrated foci of Ty3 proteins and RNA within which virus-like particle (VLP) assembly occurs. Gag3, the major structural protein of the Ty3 retrotransposon, is composed of capsid (CA), spacer (SP), and nucleocapsid (NC)
Sylvain Cecchini et al.
Human gene therapy, 22(8), 1021-1030 (2011-03-09)
The large amounts of recombinant adeno-associated virus (rAAV) vector needed for clinical trials and eventual commercialization require robust, economical, reproducible, and scalable production processes compatible with current good manufacturing practice. rAAV produced using baculovirus and insect cells satisfies these conditions;
Madhuri Gade et al.
JACS Au, 1(12), 2349-2360 (2022-01-04)
Protein conformational changes can facilitate the binding of noncognate substrates and underlying promiscuous activities. However, the contribution of substrate conformational dynamics to this process is comparatively poorly understood. Here, we analyze human (hMAT2A) and Escherichia coli (eMAT) methionine adenosyltransferases that
Marion Schuller et al.
Science advances, 7(16) (2021-04-16)
The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) macrodomain within the nonstructural protein 3 counteracts host-mediated antiviral adenosine diphosphate-ribosylation signaling. This enzyme is a promising antiviral target because catalytic mutations render viruses nonpathogenic. Here, we report a massive crystallographic screening
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