B0681
Anti-BACE 1, N-Terminus (46-62) antibody produced in rabbit
affinity isolated antibody, buffered aqueous solution
동의어(들):
Anti-β-Site APP Cleaving Enzyme
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크기 선택
제품정보 (DICE 배송 시 비용 별도)
Conjugate:
unconjugated
Clone:
polyclonal
Application:
WB
Citations:
30
Quality Level
biological source
rabbit
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)
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.
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저장 등급
10 - Combustible liquids
wgk
nwg
flash_point_f
Not applicable
flash_point_c
Not applicable
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
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
BACE1 protein endocytosis and trafficking are differentially regulated by ubiquitination at lysine 501 and the Di-leucine motif in the carboxyl terminus
Kang EL, et al.
The Journal of Biological Chemistry, 287(51), 42867-42880 (2012)
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)
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)
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