BACE1 Rabbit mAb

BACE1 Rabbit mAb recognizes endogenous levels of total BACE1 protein.

BACE1 (β-site APP-cleaving enzyme 1), also known as β-secretase, is a membrane-associated aspartyl protease crucial for the initiation of amyloid-β (Aβ) peptide production, a hallmark of Alzheimer's disease (AD) pathology. It cleaves amyloid precursor protein (APP) at the β-site to generate a C-terminal fragment (C99), which is subsequently processed by γ-secretase to produce Aβ peptides, particularly the pathogenic Aβ42 variant. Structurally, BACE1 is a type I transmembrane protein with a luminal catalytic domain containing two conserved aspartate residues (Asp32 and Asp228) essential for its enzymatic activity, along with a transmembrane domain and a short cytoplasmic tail. It also contains characteristic motifs like the DTG and DSG sequences within its active site. BACE1 is predominantly expressed in neurons and localized in acidic compartments such as endosomes, where APP processing occurs. Beyond APP cleavage, BACE1 has physiological substrates including neuregulin-1, voltage-gated sodium channel β-subunits, and others involved in myelination, synaptic function, and axon guidance, indicating its broader role in neurodevelopment and function. Elevated BACE1 activity and expression are observed in AD brains, and its genetic deletion in animal models leads to reduced Aβ levels and amyloid plaque formation.