|Calculated MW||56180 Da|
|Purification||Antisera to human BACE2 were raised by repeated immunisation of rabbits with highly purified antigen. Purified IgG was prepared from whole serum by affinity chromatography.|
|Immunogen||Synthetic peptide corresponding to amino acids 44-59 of human BACE2.|
|Shelf Life||18 months from date of despatch.|
|Other Names||Beta-secretase 2, 188.8.131.52, Aspartic-like protease 56 kDa, Aspartyl protease 1, ASP1, Asp 1, Beta-site amyloid precursor protein cleaving enzyme 2, Beta-site APP cleaving enzyme 2, Down region aspartic protease, DRAP, Memapsin-1, Membrane-associated aspartic protease 1, Theta-secretase, BACE2, AEPLC, ALP56, ASP21|
|Target/Specificity||Rabbit anti-Human BACE2 antibody recognizes human Beta-secretase 2, also known as BACE2, Aspartic-like protease 56 kDa, Aspartyl protease 1, Beta-site amyloid precursor protein cleaving enzyme 2, Down region aspartic protease, Memapsin-1, Membrane-associated aspartic protease 1 or Theta-secretase. BACE2 is a 456 amino acid ~56 kDa single pass type 1 transmembrane glycoprotein bearing a 20 amino acid N-terminal signal peptide and an adjacent 42 amino acid pro-peptide region. Rabbit anti-Human BACE2 antibody recognizes an epitope within the N-terminal region of BACE2, a homologue of the beta-site APP cleaving enzyme (BACE). BACE2 has been reported to cleave the beta-amyloid precursor protein (APP) at the beta-site, producing amyloid-beta protein (Yanet al.1999). Accumulation of amyloid beta plaques in the cerebral cortex play an important role in the pathogenesis of Alzheimer's disease, particularly in individuals bearing the Flemish mutation (Farzanet al.2000).|
|Preservative & Stabilisers||0.02% Sodium Azide|
|Storage||Store at +4℃ or at -20 ℃.|
|Precautions||Anti-Human BACE2 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
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2. Koryakina A et al. (2009) Regulation of secretases by all-trans-retinoic acid.FEBS J. 276 (9): 2645-55.1. Farzan, M. et al. (2000) BACE2, a beta -secretase homolog, cleaves at the beta site and within the amyloid-beta region of the amyloid-beta precursor protein.Proc. Natl. Acad. Sci. 97:9712-7.
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