AB5940
Anti-BACE Antibody, CT
Chemicon®, from rabbit
Synonym(e):
ASP2, BACE1, Beta Secretase, beta-Site APP Cleaving Enzyme
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Alle Fotos(2)
About This Item
UNSPSC-Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Empfohlene Produkte
Biologische Quelle
rabbit
Qualitätsniveau
Antikörperform
affinity isolated antibody
Antikörper-Produkttyp
primary antibodies
Klon
polyclonal
Aufgereinigt durch
affinity chromatography
Speziesreaktivität
human
Hersteller/Markenname
Chemicon®
Methode(n)
immunohistochemistry: suitable
western blot: suitable
NCBI-Hinterlegungsnummer
UniProt-Hinterlegungsnummer
Versandbedingung
wet ice
Posttranslationale Modifikation Target
unmodified
Angaben zum Gen
human ... BACE1(23621)
Allgemeine Beschreibung
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.
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.
Spezifität
BACE (beta-site APP Cleaving Enzyme).
Anwendung
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.
Immunohistochemistry on rat and monkey.
Optimal working dilutions must be determined by end user.
Zielbeschreibung
70 kDa
Hinweis zur Analyse
Control
Tested on human brain tissue lysate.
Tested on human brain tissue lysate.
Rechtliche Hinweise
CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany
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Lagerklassenschlüssel
12 - Non Combustible Liquids
WGK
WGK 1
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
Analysenzertifikate (COA)
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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 neurochemistry, 108(4), 1045-1056 (2009-02-07)
While it is well established that stroke and cerebral hypoperfusion are both significant risk factors for Alzheimer's disease, the molecular link between ischemia and amyloid precursor protein processing has only been recently established. Specifically, hypoxia significantly increases beta-site APP cleaving
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.
Human apoB overexpression and a high-cholesterol diet differently modify the brain APP metabolism in the transgenic mouse model of atherosclerosis.
Bjelik, Annamaria, et al.
Neurochemistry International, 49, 393-400 (2006)
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
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