70664
Benzonase® Nuclease
Purity > 99%, Effective viscosity reduction and removal of nucleic acids from protein solutions
동의어(들):
Endonuclease from Serratia marcescens
제품 이름
Benzonase® Nuclease, Purity > 99%, Effective viscosity reduction and removal of nucleic acids from protein solutions
생물학적 소스
Serratia marcescens
Quality Level
재조합
expressed in E. coli
분석
>99% (SDS-PAGE)
양식
buffered aqueous glycerol solution
제조업체/상표
Novagen®
저장 조건
OK to freeze
농도
25-29 units/μL
불순물
<0.25 EU/kU Total endotoxin
응용 분야
research use
배송 상태
wet ice
저장 온도
−20°C
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일반 설명
Benzonase® Nuclease is a genetically engineered endonuclease from Serratia marcescens. It degrades all forms of DNA and RNA (single stranded, double stranded, linear and circular) while having no proteolytic activity. It is effective over a wide range of conditions and possesses an exceptionally high specific activity. The enzyme completely digests nucleic acids to 5′-monophosphateterminated oligonucleotides 2 to 5 bases in length (below the hybridization limit), which is ideal for removal of nucleic acids from recombinant proteins, enabling compliance with FDA guidelines for nucleic acid contamination. The ability of Benzonase to rapidly hydrolyze nucleic acids makes the enzyme an excellent choice for viscosity reduction to reduce processing time and increase yields of protein. For example, the enzyme is compatible with BugBuster and PopCulture Protein Extraction Reagents and can therefore be added along with these reagents to eliminate viscosity and remove nucleic acids from E. coli extracts.
The enzyme consists of two subunits of30 kDa each. It is functional between pH 6 and 10 and from 0-42°C and requires1-2 mM Mg2+ for activation. The enzyme is also active in the presence of ionic and non-ionic detergents, reducing agents, PMSF(1 mM), EDTA (1 mM) and urea (relative activity depends on specific conditions).Activity is inhibited by > 150 mM monovalent cations, > 100 mM phosphate, > 100 mMammonium sulfate, or > 100 mM guanidine HCl.
Benzonase Nuclease is available in ultrapure (> 99% by SDS-PAGE) and pure (> 90%) grades at a standard concentration of 25-29 U/µl and at a high concentration (HC) of 250 U/µl. Both preparations are free of detectable protease and have specific activity> 1 × 106 U/mg protein. The > 99% purity grade is tested for endotoxins and contains< 0.25 EU/1000 units. The product is supplied in 50% glycerol. Store at -20°C.

Total endotoxin:< 0.25 EU/1,000 units. Purity: > 99% by SDS-PAGE.
The enzyme consists of two subunits of30 kDa each. It is functional between pH 6 and 10 and from 0-42°C and requires1-2 mM Mg2+ for activation. The enzyme is also active in the presence of ionic and non-ionic detergents, reducing agents, PMSF(1 mM), EDTA (1 mM) and urea (relative activity depends on specific conditions).Activity is inhibited by > 150 mM monovalent cations, > 100 mM phosphate, > 100 mMammonium sulfate, or > 100 mM guanidine HCl.
Benzonase Nuclease is available in ultrapure (> 99% by SDS-PAGE) and pure (> 90%) grades at a standard concentration of 25-29 U/µl and at a high concentration (HC) of 250 U/µl. Both preparations are free of detectable protease and have specific activity> 1 × 106 U/mg protein. The > 99% purity grade is tested for endotoxins and contains< 0.25 EU/1000 units. The product is supplied in 50% glycerol. Store at -20°C.

Total endotoxin:< 0.25 EU/1,000 units. Purity: > 99% by SDS-PAGE.
Effective viscosity reduction and removal of nucleic acids from protein solutions
애플리케이션
Used for the removal of nucleic acid from protein samples.
생화학적/생리학적 작용
Digests native or heat-denatured DNA and RNA.
기타 정보
One unit is defined as the amount of enzyme that causes a ΔA₂₆₀ of 1.0 in 30 minutes, which corresponds to complete digestion of 37 µg DNA.
법적 정보
Benzonase is a registered trademark of Merck KGaA, Darmstadt, Germany
NOVAGEN is a registered trademark of Merck KGaA, Darmstadt, Germany
면책조항
Toxicity: Standard Handling (A)
Storage Class Code
10 - Combustible liquids
WGK
WGK 2
시험 성적서(COA)
제품의 로트/배치 번호를 입력하여 시험 성적서(COA)을 검색하십시오. 로트 및 배치 번호는 제품 라벨에 있는 ‘로트’ 또는 ‘배치’라는 용어 뒤에서 찾을 수 있습니다.
Hannah Schneider et al.
Journal of neurochemistry, 140(1), 170-182 (2016-10-28)
Targeting the vascular endothelial growth factor signaling axis in glioblastoma inevitably leads to tumor recurrence and a more aggressive phenotype. Therefore, other angiogenic pathways, like the angiopoietin/tunica interna endothelial cell kinase (TIE) signaling axis, have become additional targets for therapeutic
Xuemei Nan et al.
Physiological genomics, 46(7), 268-275 (2014-01-30)
This study was conducted to determine the optimum ratio of lysine and methionine (Lys:Met) to enhance milk protein concentration in vitro, focusing on the regulation of genes related to the JAK2-STAT5 and the mammalian target of rapamycin (mTOR) signaling pathways.
Enmanuel J Perez et al.
The Journal of clinical investigation, 127(8), 3114-3125 (2017-07-18)
After traumatic brain injury (TBI), glial cells have both beneficial and deleterious roles in injury progression and recovery. However, few studies have examined the influence of reactive astrocytes in the tripartite synapse following TBI. Here, we have demonstrated that hippocampal
Timothy N Audam et al.
American journal of physiology. Heart and circulatory physiology, 319(1), H109-H122 (2020-05-23)
Although cell therapy-mediated cardiac repair offers promise for treatment/management of heart failure, lack of fundamental understanding of how cell therapy works limits its translational potential. In particular, whether reparative cells from failing hearts differ from cells derived from nonfailing hearts
Georg E Winter et al.
Molecular cell, 67(1), 5-18 (2017-07-05)
Processive elongation of RNA Polymerase II from a proximal promoter paused state is a rate-limiting event in human gene control. A small number of regulatory factors influence transcription elongation on a global scale. Prior research using small-molecule BET bromodomain inhibitors
문서
Benzonase®endonuclease efficiently removes nucleic acid contaminants from viral production, crucial for cell and gene therapies and vaccines.
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