T4330
Endonucléase from Serratia marcescens
recombinant, expressed in E. coli
Synonyme(s) :
Endonuclease from Serratia marcescens
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About This Item
Numéro CAS:
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54
Produits recommandés
Source biologique
Serratia marcescens
Niveau de qualité
Produit recombinant
expressed in E. coli
Forme
liquid
Concentration
≥200,000 units/mL
Technique(s)
DNA purification: suitable
Adéquation
suitable for cell lysis
Application(s)
life science and biopharma
Température de stockage
−20°C
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Description générale
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.
Application
Turbonuclease from Serratia marcescens has been used for cell lysis during proximity biotinylation assay (BioID) and affinity-purification. It has also been used as a component of lysis buffer for protein extraction from cell lines for affinity purification studies.
Turbonuclease has been used in a study to assess the TY3 gag3 spacer effect on intracellular condensation and uncoating.
Pour l'élimination des acides nucléiques présents dans les échantillons protéiques.
Actions biochimiques/physiologiques
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.
Turbonuclease provides a nuclease treatment by reducing viscosity and degrading RNA, genomic DNA, baculovirus DNA, and unencapsidated vector DNA.
Digère l′ADN et l′ARN endogènes ou dénaturés par voie thermique.
Définition de l'unité
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.
Forme physique
Supplied as a solution in 50 mM Tris-HCl, pH 8.0 and 50 mM NaCl
Code de la classe de stockage
10 - Combustible liquids
Classe de danger pour l'eau (WGK)
WGK 2
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
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Les clients ont également consulté
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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