Anti-BACE Antibody, CT

70 kDa

Alzheimer′s disease (AD) is characterized by the progressive formation in the brain of insoluble amyloid plaques and vascular deposits consisting of the 4-kD amyloid b-peptide (Ab). Ab generation is initiated by proteolytic cleavage of the amyloid precursor protein (APP) at the N-terminal of Ab by b-secretase. The Ab peptide is then released by proteolytic cleavage at its C-terminus by g-secretase. Because both these proteases are prime candidates for therapeutic intervention, an intense search has been underway to identify these two enzymes.A human transmembrane aspartic-protease (Asp2), referred to as BACE, has been characterized and shown to have all the properties of b-secretase. Four groups in all have now confirmed that BACE (or Asp2) is a convincing candidate for b-secretase.

BACE is an N-glycosylated integral membrane aspartyl protease with Mr=70 kDa. Mature BACE is produced from the immature form through a series of post-translational proteolytic cleavages and glycosylation. Sequence analysis has revealed that the immature form of BACE contains an N-terminal signal sequence (residues 1-21) followed by a large catalytic domain, a single transmembrane domain (residues 461-477), and a short cytoplasmic domain (residues 478-501). The signal sequence (1-21) is cleaved from the immature form by a signal peptidase located in the endoplasmic reticulum (ER), yielding the proBACE protein (Mr=75 kDa) which starts at residue 22. The proBACE protein is modified by cleavage of 24 N-terminal residues (aa 22-45), producing the mature BACE protein.

This Anti-BACE Antibody, C-terminus is validated for use in WB, IH for the detection of BACE.

Western blot on COS7 transfected cells. The antibody recognizes a band of ~70-75 kDa. It also recognizes a band at ~45 kDa.

Immunohistochemistry on rat and monkey.

Optimal working dilutions must be determined by end user.

BACE (beta-site APP Cleaving Enzyme).

Control
Tested on human brain tissue lysate.

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