|Reactivity||Human, Mouse, Rabbit, Hamster, Monkey, Pig, Horse, Bovine, Guinea Pig, Dog|
|Dilution||IHC-P (2.5 µg/ml)|
|Other Names||Beta-secretase 1, 22.214.171.124, Aspartyl protease 2, ASP2, Asp 2, Beta-site amyloid precursor protein cleaving enzyme 1, Beta-site APP cleaving enzyme 1, Memapsin-2, Membrane-associated aspartic protease 2, BACE1, BACE, KIAA1149|
|Target/Specificity||Human BACE1. BLAST analysis of the peptide immunogen showed no homology with other human proteins.|
|Reconstitution & Storage||Long term: -70°C; Short term: +4°C|
|Precautions||BACE1 / BACE Antibody (Internal) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Responsible for the proteolytic processing of the amyloid precursor protein (APP). Cleaves at the N-terminus of the A-beta peptide sequence, between residues 671 and 672 of APP, leads to the generation and extracellular release of beta-cleaved soluble APP, and a corresponding cell-associated C-terminal fragment which is later released by gamma-secretase.|
|Cellular Location||Membrane; Single-pass type I membrane protein. Golgi apparatus, trans-Golgi network. Endoplasmic reticulum. Endosome. Cell surface. Cytoplasmic vesicle membrane Note=Predominantly localized to the later Golgi/trans-Golgi network (TGN) and minimally detectable in the early Golgi compartments. A small portion is also found in the endoplasmic reticulum, endosomes and on the cell surface|
|Tissue Location||Expressed at high levels in the brain and pancreas. In the brain, expression is highest in the substantia nigra, locus coruleus and medulla oblongata|
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Provided below are standard protocols that you may find useful for product applications.
Responsible for the proteolytic processing of the amyloid precursor protein (APP). Cleaves at the N-terminus of the A-beta peptide sequence, between residues 671 and 672 of APP, leads to the generation and extracellular release of beta-cleaved soluble APP, and a corresponding cell-associated C-terminal fragment which is later released by gamma-secretase.
Vassar R.,et al.Science 286:735-741(1999).
Sinha S.,et al.Nature 402:537-540(1999).
Yan R.,et al.Nature 402:533-537(1999).
Hussain I.,et al.Mol. Cell. Neurosci. 14:419-427(1999).
Michel B.,et al.Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
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