Technical Data
BACE, Asp2, CT, Blocking Peptide (Beta-site APP Cleaving Enzyme, Aspartyl Protease 2)
Molecular Biology Storage: -20°CShipping: Blue Ice
Peptide corresponding to amino acids 485 to 501 of human BACE (1).
Accumulation of the amyloid-b (Ab) plaque in the cerebral cortex is a critical event in the pathogenesis of Alzheimer’s disease. Ab peptide is generated by proteolytic cleavage of the b-amyloid protein precursor (APP) at b-and g-sites by two proteases. APP is first cleaved by b-secretase, producing a soluble derivative of the protein and a membrane anchored 99-amino acid carboxy-terminal fragment (C99). The C99 fragment serves as substrate for g-secretase to generate the 4kD amyloid-b peptide, which is deposited in the brains of all suffers of Alzheimer’s disease. The long-sought b-secretase was recently identified by several groups independently and designated beta-site APP cleaving enzyme (BACE) and aspartyl protease 2 (Asp2) (1-4). BACE/Asp2 is a novel transmembrane aspartic protease and co-localizes with APP.
Source: Synthetic peptide
Purity: Purified 60-70%
Concentration: 0.2mg/ml
Form: Supplied as a lyophilized powder.

Important Note: This product is intended for research use only, not for use in human, therapeutic or diagnostic applications.
1. Vassar R, Bennett BD, Babu-Khan S, et al. Beta-secretase cleavage of Alzheimer’s amyloid precursor protein by the transmembrane aspartic protease BACE. Science 1999;286:735-41 2. Hussain I, Powell D, Howlett DR, et al. Identification of a novel aspartic protease (Asp 2) as beta-secretase. Mol Cell Neurosci 1999;14:419-27 3. Yan R, Bienkowski MJ, Shuck ME, et al. Membrane-anchored aspartyl protease with Alzheimer’s disease beta-secretase activity. Nature 1999;402:533-7 4. Sinha S, Anderson JP, Barbour R, et al. Purification and cloning of amyloid precursor protein beta-secretase from human brain. Nature 1999;402:537-40

Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.