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Merck
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Key Documents

AV43534

Sigma-Aldrich

Anti-AADAT antibody produced in rabbit

IgG fraction of antiserum

Sinónimos:

Anti-kynurenine aminotransferase II, Anti-Aminoadipate aminotransferase, Anti-KAT2, Anti-KATII

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About This Item

Código UNSPSC:
12352203
NACRES:
NA.41

origen biológico

rabbit

conjugado

unconjugated

forma del anticuerpo

IgG fraction of antiserum

tipo de anticuerpo

primary antibodies

clon

polyclonal

formulario

buffered aqueous solution

mol peso

47 kDa

reactividad de especies

rabbit, human

concentración

0.5 mg - 1 mg/mL

técnicas

immunohistochemistry: suitable
western blot: suitable

Nº de acceso NCBI

Nº de acceso UniProt

Condiciones de envío

wet ice

temp. de almacenamiento

−20°C

modificación del objetivo postraduccional

unmodified

Información sobre el gen

human ... AADAT(51166)

Descripción general

KAT (kynurenine aminotransferase, AADAT) II, a pyridoxal 5′-phosphate-dependent enzyme, is the primary enzyme in the brain for catalyzing the transamination of kynurenine to KγNA (kynurenic acid) and the transmination of aminoadipate to α-oxoadipate. Kynurenic acid, a neuroprotective compound, is an endogenous antagonist of ionotropic excitatory amino acid receptors in the central nervous system.

Especificidad

Anti-AADAT polyclonal antibody (Anti-KAT-II) reacts with a sequence of the enzyme human aminoadipate aminotransferase (kynurenine aminotransferase II, hAADAT, KAT-II).

Inmunógeno

Synthetic peptide directed towards the N terminal region of human AADAT

Aplicación

Anti-kynurenine aminotransferase II (anti-Aminoadipate aminotransferase; anti-AADAT) is a rabbit IgG polyclonal antibody used to tag kynurenine aminotransferase protein for detection and quantitation by Western blotting and in tissues by immunohistochemical (IHC) techniques. Selective KAT II inhibition may be an important pharmacological tool, since it would reduce KγNA formation without causing complete depletion of this neuroprotector.

Acciones bioquímicas o fisiológicas

AADAT is a protein that is highly similar to mouse and rat kynurenine aminotransferase II. The rat protein is a homodimer with two transaminase activities. One activity is the transamination of alpha-aminoadipic acid, a final step in the saccaropine pathway which is the major pathway for L-lysine catabolism. The other activity involves the transamination of kynurenine to produce kynurenine acid, the precursor of kynurenic acid which has neuroprotective properties.This gene encodes a protein that is highly similar to mouse and rat kynurenine aminotransferase II. The rat protein is a homodimer with two transaminase activities. One activity is the transamination of alpha-aminoadipic acid, a final step in the saccaropine pathway which is the major pathway for L-lysine catabolism. The other activity involves the transamination of kynurenine to produce kynurenine acid, the precursor of kynurenic acid which has neuroprotective properties. Two alternative transcripts encoding the same isoform have been identified, however, additional alternative transcripts and isoforms may exist.

Secuencia

Synthetic peptide located within the following region: AVITVENGKTIQFGEEMMKRALQYSPSAGIPELLSWLKQLQIKLHNPPTI

Forma física

Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.

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

12 - Non Combustible Liquids

Clase de riesgo para el agua (WGK)

WGK 3

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable


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Christos Papadimitriou et al.
Developmental cell, 46(1), 85-101 (2018-07-06)
Neural stem cells (NSCs) constitute an endogenous reservoir for neurons that could potentially be harnessed for regenerative therapies in disease contexts such as neurodegeneration. However, in Alzheimer's disease (AD), NSCs lose plasticity and thus possible regenerative capacity. We investigate how

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