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GENIUS™Nuclease

CAT: 0716-BEE-N3116-10KUSize: 10 KUDry Ice: NoHazardous: No
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CAT#:0716-BEE-N3116-10KUSize:10 KU
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24/48H Stock Items & 2 to 6 Weeks non Stock Items.
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Background
Beta-secretase 1 (BACE1) is also known as beta-site APP cleaving enzyme 1 (beta-site amyloid precursor protein cleaving enzyme 1), memapsin-2 (membrane-associated aspartic protease 2), and aspartyl protease 2 (ASP2), β-Secretase , and is a member of the peptidase A1 protein family, BACE1 is a type I integral membrane glycoprotein and aspartic protease that is found mainly in the Golgi. BACE1 is an aspartic-acid protease important in the pathogenesis of Alzheimers disease, and in the formation of myelin sheaths in peripheral nerve cells. The transmembrane protein contains two active site aspartate residues in its extracellular protein domain and may function as a dimer. This protease is responsible for the proteolytic processing of the amyloid precursor protein (APP) . Generation of the 40 or 42 amino acid-long amyloid-β peptides that aggregate in the brain of Alzheimers patients requires two sequential cleavages of the APP. Extracellular cleavage of APP by BACE creates a soluble extracellular fragment and a cell membrane-bound fragment referred to as C99. The elevation of BACE1 levels can be induced by amyloid plaques surrounding neurons at early stages of pathology before neuron death occurs, and may drive a positive-feedback loop in AD.
Description
GENIUS™Nuclease is a recombinant form of Serratia marcescens extracellular endonuclease produced in Escherichia coli cells using a proprietary process at ACRObiosystems. GENIUS™Nuclease is a homodimer with monomer molecular masses about 30 kDa. Two disulfide bonds found in the nuclease are crucial to its activity and stability. The enzyme is a non-specific nuclease with high specific activity, which degrades both single- and double-stranded nucleic acids in any form (single stranded, double stranded, linear, circular and supercoiled) . It hydrolyzes internal phosphodiester bonds present between the nucleotides to 5‘- phosphorylated oligonucleotides of 3-5 bases in length.
Specifications
BenzNuclease is a recombinant form of Serratia macescens extracellular endonuclease produced in Escherichia coli cells using a proprietary process at ACRObiosystems. BenzNuclease is a homodimer with monomer molecular masses about 30 kDa. Two disulfide bonds found in the nuclease are crucial to its activity and stability. The enzyme is a non-specific nuclease with high specific activity, which degrades both single- and double-stranded nucleic acids in any form (single stranded, double stranded, linear, circular and supercoiled) . It hydrolyzes internal phosphodiester bonds present between the nucleotides to 5'-phosphorylated oligonucleotides of 3-8 bases in length.
Host
E. coli
Target
Nuclease
Conjugation
Unconjugated
Tag
Native
Source
Serratia marcescens
Applications
Its high intrinsic activity and broad substrate tolerance make the endonuclease an ideal tool in a variety of biotechnological and pharmaceutical applications: removal of nucleic acid from protein samples (Elimination of nucleic acids from recombinant proteins; Purification of protein fragments from inclusion bodies; Sample preparation in western blotting or two-dimensional gel electrophoresis) ; Viscosity reduction in protein extracts.
Stability
Avoid repeated freeze-thaw cycles. This product is stable after storage at: In lyophilized state for 1 year (-20oC) ; After reconstitution under sterile conditions for 3 months (-70oC) .
Endotoxin
1.0 EU per μg
Purity
95%
Format
Powder
Buffer
20mM Tris, 20mM NaCl, 2mM MgCl2, pH8.0
Molecular Weight
26.8 kDa
Additionnal Information
Please see 'Shipping-and-Payments' sheet. Website: https://www.acrobiosystems.com/support/shipping-and-payments
Shipping Conditions
RT
Storage Conditions
-20°C
Package Size
10KU*1
Host or Source
E. coli
Species
Serratia marcescens

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