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Key Documents

B0681

Sigma-Aldrich

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

enhanced validation

affinity isolated antibody, buffered aqueous solution

Synonyme(s) :

Anti-β-Site APP Cleaving Enzyme

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About This Item

Numéro MDL:
MFCD03454775
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Conjugué

unconjugated

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Poids mol.

antigen 60-75 kDa

Espèces réactives

human

Validation améliorée

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

Numéro d'accès UniProt

P56817

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... BACE1(23621)

Catégories apparentées

Description générale

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.

Immunogène

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.

Actions biochimiques/physiologiques

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.

Forme physique

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

Clause de non-responsabilité

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.

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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

nwg

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

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)
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)
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
BACE-1 is expressed in the blood-brain barrier endothelium and is upregulated in a murine model of Alzheimer?s disease
Devraj K, et al.
Journal of Cerebral Blood Flow and Metabolism, 36(7), 1281-1294 (2016)
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