EMD Millipore

Oncogene Research Products, Calbiochem, Novagen, Merck, Upstate Biotechnology, Chemicon, LINCO, Novabiochem, Guava

ELISA/assay

BACE Proteins Investigator Minipack

15-206

3 vials/Pk

15-206

Neuroscience

BACE Proteins Investigator Minipack

Antibodies

Q9Y5Z0;P56817

BACE Proteins Investigator Minipack

BACE Proteins Investigator Minipack

Pathway Investigator Antibody MiniPack: Each Pathway Explorer Antibody Minipack contains three related antibodies as part of a signaling cascade or a combination of total and phosphorylated forms of key signaling targets. Each of the three antibodies are 30% the original pack size. Full size versions of each of the Pathway Explorer antibodies are available for sale individually under the same catalog number with the removal of “SP” off of each one (e.g. 05-591SP can be ordered as 05-591). Anti-BACE: 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. Anti-BACE2: Cerebral deposition of amyloid beta peptide is an early and critical feature of Alzheimer’s disease and a frequent complication of Down syndrome. BACE2 proteolytically cleaves amyloid precursor protein, generating the amyloid beta peptide. BACE2 is a member of the peptidase A1 protein family, a type I integral membrane glycoprotein and aspartic protease. Anti-BACE, C-terminus, clone 61-3E7: 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. * See full size versions for corresponding references.

ASP2; BACE1; Beta Secretase; beta-Site APP Cleaving Enzyme;Aspartyl protease 2;Beta-site amyloid precursor protein cleaving enzyme 1 ;Membrane-associated aspartic protease 2;beta-site amyloid beta A4 precursor protein-cleaving enzyme ;beta-site amyloid precursor protein cleaving enzyme 2 transmembrane aspartic proteinase Asp2

3 vials/Pk