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AB5940

Sigma-Aldrich

Anti-BACE Antibody, CT

Chemicon®, from rabbit

Synonyme(s) :

ASP2, BACE1, Beta Secretase, beta-Site APP Cleaving Enzyme

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About This Item

Code UNSPSC :
12352203
eCl@ss :
32160702
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Niveau de qualité

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Produit purifié par

affinity chromatography

Espèces réactives

human

Fabricant/nom de marque

Chemicon®

Technique(s)

immunohistochemistry: suitable
western blot: suitable

Numéro d'accès UniProt

Conditions d'expédition

wet ice

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... BACE1(23621)

Description générale

Alzheimer′s disease (AD) is characterized by the progressive formation in the brain of insoluble amyloid plaques and vascular deposits consisting of the 4-kD amyloid b-peptide (Ab). Ab generation is initiated by proteolytic cleavage of the amyloid precursor protein (APP) at the N-terminal of Ab by b-secretase. The Ab peptide is then released by proteolytic cleavage at its C-terminus by g-secretase. Because both these proteases are prime candidates for therapeutic intervention, an intense search has been underway to identify these two enzymes.A human transmembrane aspartic-protease (Asp2), referred to as BACE, has been characterized and shown to have all the properties of b-secretase. Four groups in all have now confirmed that BACE (or Asp2) is a convincing candidate for b-secretase.

BACE is an N-glycosylated integral membrane aspartyl protease with Mr=70 kDa. Mature BACE is produced from the immature form through a series of post-translational proteolytic cleavages and glycosylation. Sequence analysis has revealed that the immature form of BACE contains an N-terminal signal sequence (residues 1-21) followed by a large catalytic domain, a single transmembrane domain (residues 461-477), and a short cytoplasmic domain (residues 478-501). The signal sequence (1-21) is cleaved from the immature form by a signal peptidase located in the endoplasmic reticulum (ER), yielding the proBACE protein (Mr=75 kDa) which starts at residue 22. The proBACE protein is modified by cleavage of 24 N-terminal residues (aa 22-45), producing the mature BACE protein.

Spécificité

BACE (beta-site APP Cleaving Enzyme).

Application

This Anti-BACE Antibody, C-terminus is validated for use in WB, IH for the detection of BACE.
Western blot on COS7 transfected cells. The antibody recognizes a band of ~70-75 kDa. It also recognizes a band at ~45 kDa.

Immunohistochemistry on rat and monkey.

Optimal working dilutions must be determined by end user.

Description de la cible

70 kDa

Remarque sur l'analyse

Control
Tested on human brain tissue lysate.

Informations légales

CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany

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Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

Ju-Fang Huang et al.
BMC complementary and alternative medicine, 12, 189-189 (2012-10-23)
Our previous studies indicated that oxidative stress up-regulated the expression of β-amyloid precursor protein cleavage enzyme-1 (BACE1) in rat retina. Pharmacological reports have shown Timosaponin-BII, a purified extract originating from Chinese medical herb Rhizoma Anemarrhenae, is characterized as an antioxidant.
Shengliang Li et al.
Molecular therapy. Nucleic acids, 1, e20-e20 (2013-01-25)
The fluorescent quantum dots (QDs) delivered small interfering RNAs (siRNAs) targeting β-secretase (BACE1) to achieve high transfection efficiency of siRNAs and reduction of β-amyloid (Aβ) in nerve cells. The CdSe/ZnS QDs with the conjugation of amino-polyethylene glycol (PEG) were synthesized.
Michela Guglielmotto et al.
Journal of Alzheimer's disease : JAD, 71(3), 907-920 (2019-08-28)
Neuroinflammation is involved in the pathogenesis of Alzheimer's disease, and the transcription factor NF-κB is a player in this event. We found here that the ischemic damage alone or in association with Aβ1-42 activates the NF-κB pathway, induces an increase
Experimental traumatic brain injury induces rapid aggregation and oligomerization of amyloid-beta in an Alzheimer's disease mouse model.
Washington, PM; Morffy, N; Parsadanian, M; Zapple, DN; Burns, MP
Journal of Neurotrauma null
Ruishan Wang et al.
The Journal of biological chemistry, 290(37), 22532-22542 (2015-08-05)
Insulin resistance and neuroinflammation have emerged as two likely key contributors in the pathogenesis of Alzheimer disease (AD), especially in those sporadic AD cases compromised by diabetes or cardiovascular disease. Amyloid-β (Aβ) deposition and its associated inflammatory response are hallmarks

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