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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

Sinónimos:

Anti-β-Site APP Cleaving Enzyme

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0.2 ML
$631.000

$631.000


Fecha estimada de envío03 de mayo de 2025


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0.2 ML
$631.000

About This Item

Número MDL:
Código UNSPSC:
12352203
NACRES:
NA.41

$631.000


Fecha estimada de envío03 de mayo de 2025


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origen biológico

rabbit

Nivel de calidad

conjugado

unconjugated

forma del anticuerpo

affinity isolated antibody

tipo de anticuerpo

primary antibodies

clon

polyclonal

Formulario

buffered aqueous solution

mol peso

antigen 60-75 kDa

reactividad de especies

human

validación mejorada

recombinant expression
Learn more about Antibody Enhanced Validation

técnicas

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

Nº de acceso UniProt

Condiciones de envío

dry ice

temp. de almacenamiento

−20°C

modificación del objetivo postraduccional

unmodified

Información sobre el gen

human ... BACE1(23621)

Descripción general

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.

Inmunógeno

synthetic peptide corresponding to the N-terminus of human BACE-1 (amino acids 46-62).

Aplicación

Anti-BACE 1, N-Terminus (46-62) antibody produced in rabbit has been used in western blotting.

Acciones bioquímicas o fisiológicas

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.

Forma física

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

Cláusula de descargo de responsabilidad

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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Código de clase de almacenamiento

10 - Combustible liquids

Clase de riesgo para el agua (WGK)

nwg

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°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
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
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)

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