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B0681

Sigma-Aldrich

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

enhanced validation

affinity isolated antibody, buffered aqueous solution

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Synonym(s):
Anti-β-Site APP Cleaving Enzyme
MDL number:

biological source

rabbit

Quality Level

conjugate

unconjugated

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

technique(s)

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

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... BACE1(23621)

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SAB2100200MAB5308G0290
Quality Level

200

Quality Level

100

Quality Level

100

Quality Level

200

antibody form

affinity isolated antibody

antibody form

affinity isolated antibody

antibody form

purified immunoglobulin

antibody form

affinity isolated antibody

conjugate

unconjugated

conjugate

unconjugated

conjugate

-

conjugate

unconjugated

UniProt accession no.

P56817

UniProt accession no.

P56817

UniProt accession no.

P56817

UniProt accession no.

P15976

Gene Information

human ... BACE1(23621)

Gene Information

human ... BACE1(23621)

Gene Information

human ... BACE1(23621)

Gene Information

human ... GATA1(2623)

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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.

Storage Class

10 - Combustible liquids

wgk_germany

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable


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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
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
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)
Maturation and pro-peptide cleavage of beta-secretase
Capell A, et al.
Test, 275(40), 30849-30854 (2000)
L Devi et al.
Translational psychiatry, 5, e562-e562 (2015-05-06)
Accumulating evidence shows that brain-derived neurotrophic factor (BDNF) and its receptor tropomyosin-related kinase B (TrkB) significantly decrease early in Alzheimer's disease (AD). However, it remains unclear whether BDNF/TrkB reductions may be mechanistically involved in the pathogenesis of AD. To address

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