BACE1
BACE1 (beta-secretase 1, also known as Asp2 or BACE) is a transmembrane aspartic protease that carries out the first step in generating amyloid beta peptide from amyloid precursor protein (APP). It is also called beta-site APP-cleaving enzyme 1. Browse Assay Genie's current range of BACE1 research reagents below, or read on for the biology behind the target.
BACE1 is responsible for the proteolytic processing of amyloid precursor protein (APP). It cleaves at the N-terminus of the A-beta peptide sequence, between residues 671 and 672 of APP. This cleavage generates and releases extracellularly a beta-cleaved soluble APP fragment, and leaves a corresponding cell-associated C-terminal fragment, which is later released by gamma-secretase. BACE1 therefore catalyses the first step in the formation of amyloid beta peptide. The source annotation also lists CHL1 as a substrate of BACE1.
The BACE1 gene encodes a member of the peptidase A1 family of aspartic proteases, classified under EC 3.4.23.46. Alternative splicing gives rise to multiple transcript variants, and at least one of these encodes a preproprotein that is proteolytically processed to produce the mature protease. BACE1 is a transmembrane protein, and UniProt records it at many sites in the cell: the cell membrane and cell surface, the trans-Golgi network, the endoplasmic reticulum, membrane rafts, lysosomes, and early, late and recycling endosomes. It is also found in cytoplasmic vesicle membranes and in axons and dendrites. The mouse and rat orthologues are both named Bace1.
The enzyme was first described as beta-site APP-cleaving enzyme, and the symbols Asp2 and BACE are previous names for the gene. Amyloid beta peptides are the main constituent of the amyloid beta plaques that accumulate in the brains of people with Alzheimer's disease, which is why BACE1 is studied in neurodegeneration research. A related protein, BACE2, is covered on a separate page.
BACE1 catalyses the first step in amyloid beta formation, and amyloid beta peptides are the main constituent of plaques found in Alzheimer's disease brains.
BACE1 cleaves APP between residues 671 and 672, releasing soluble beta-cleaved APP and leaving a C-terminal fragment for gamma-secretase.
Besides APP, BACE1 is annotated as cleaving CHL1, making it a model aspartic protease for studying membrane protein substrate processing.
BACE1 localises to endosomes, the trans-Golgi network, axons and dendrites, so it is used to study protein trafficking in neurons.
BACE1 is a transmembrane aspartic protease that cleaves amyloid precursor protein at the N-terminus of the A-beta sequence. This releases soluble beta-cleaved APP and leaves a cell-associated C-terminal fragment that gamma-secretase later cleaves. It also cleaves CHL1.
BACE1 is the HGNC symbol for beta-secretase 1. Previous symbols are Asp2 and BACE, and previous names include beta-site APP-cleaving enzyme and beta-site APP-cleaving enzyme 1. Alternative splicing produces multiple transcript variants, and at least one encodes a preproprotein that is processed into the mature protease.
Yes. Mouse and rat both carry an orthologue named Bace1. The human protein belongs to the peptidase A1 family of aspartic proteases. Check the datasheet of any product for its validated reactivity.
A related beta-secretase and other targets relevant to amyloid precursor protein processing research.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P56817; product specifications from Assay Genie datasheets.