B0681

Sigma-Aldrich

Anti-BACE 1, N-Terminus (46-62) antibody produced in rabbit

enhanced validation

affinity isolated antibody, buffered aqueous solution

Synonym(s):
Anti-β-Site APP Cleaving Enzyme
MDL number:
Pricing and availability is not currently available.

biological source

rabbit

Quality Level

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen 60-75 kDa

species reactivity

human

enhanced validation

recombinant expression
Learn more about Antibody Enhanced Validation

application(s)

western blot: 1:1,000 using a whole cell extract from the human kidney HEK293 cell line stably transfected with human BACE-1

conjugate

unconjugated

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

Gene Information

human ... BACE1(23621)

General description

The membrane-associated aspartic protease BACE-1 (β-site APP cleaving enzyme, Asp2 or memapsin 2) has been identified as β-secretase. BACE-1 constitutes the predominant β-secretase activity in human brain tissue. It is highly expressed in neurons, the major site of Aβ generation. BACE-1 is localized within the Golgi and endosomal compartments, among the several intracellular sites where Aβ is thought to be produced. BACE-1 is initially an inactive proenzyme and localized in endoplasmic reticulum.

Immunogen

synthetic peptide corresponding to the N-terminus of human BACE-1 (amino acids 46-62).

Application

Anti-BACE 1, N-Terminus (46-62) antibody produced in rabbit has been used in western blotting.

Biochem/physiol Actions

Overexpression of β-site APP cleaving enzyme, Asp2 or memapsin 2 (BACE-1) leads to increased β-secretase activity while displaying appropriate cleavage site specificity for APP. The N-glycosylation and phosphorylation of BACE-1 within its C-terminal domain regulated its intracellular trafficking.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% bovine serum albumin and 15 mM sodium azide.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

RIDADR

NONH for all modes of transport

WGK Germany

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis
Certificate of Origin
Jan H Verheijen et al.
Clinical chemistry, 52(6), 1168-1174 (2006-04-15)
Formation of deposits of the insoluble amyloid beta-peptide is believed to be causally related with neurodegeneration in Alzheimer disease (AD). The beta-peptide originates from a larger amyloid precursor protein (APP) by the action of proteolytic enzymes. The first proteolytic event...
L Devi et al.
Neuroscience, 307, 128-137 (2015-09-01)
β-Site APP-cleaving enzyme 1 (BACE1) initiates the generation of amyloid-β (Aβ), thus representing a prime therapeutic target for Alzheimer's disease (AD). Previous work including ours has used BACE1 haploinsufficiency (BACE1(+/-); i.e., 50% reduction) as a therapeutic relevant model to evaluate...
Activity-induced convergence of APP and BACE-1 in acidic microdomains via an endocytosis-dependent pathway
Das U, et al.
Neuron, 79(3), 447-460 (2013)
Latha Devi et al.
Current Alzheimer research, 12(1), 13-21 (2014-12-20)
The β-secretase enzyme BACE1, which initiates the cleavage of amyloid precursor protein (APP) into the amyloid-β (Aβ) peptide, is a prime therapeutic target for Alzheimer's disease (AD). However, recent investigations using genetic animal models raise concern that therapeutic BACE1 inhibition...
BACE1 SUMOylation increases its stability and escalates the protease activity in Alzheimer?s disease
Bao J, et al.
Proceedings of the National Academy of Sciences of the USA, 115(15), 3954-3959 (2018)
Articles
Alzheimer's disease (AD) is the most common cause of dementia in the elderly and is characterized by gradual loss of cognitive functions.
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