GENIUS™Nuclease

Native, Unconjugated

RT

26.8 kDa

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.

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.

20mM Tris, 20mM NaCl, 2mM MgCl2, pH8.0