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Merck
CN

AV43534

Anti-AADAT antibody produced in rabbit

IgG fraction of antiserum

别名:

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

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关于此项目

NACRES:
NA.41
UNSPSC Code:
12352203
Conjugate:
unconjugated
Clone:
polyclonal
Application:
IHC, WB
Citations:
1
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biological source

rabbit

conjugate

unconjugated

antibody form

IgG fraction of antiserum

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

47 kDa

species reactivity

rabbit, human

concentration

0.5 mg - 1 mg/mL

technique(s)

immunohistochemistry: suitable, western blot: suitable

NCBI accession no.

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... AADAT(51166)

General description

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.

Immunogen

Synthetic peptide directed towards the N terminal region of human AADAT

Application

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.

Biochem/physiol Actions

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

Physical form

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

Other Notes

Synthetic peptide located within the following region: AVITVENGKTIQFGEEMMKRALQYSPSAGIPELLSWLKQLQIKLHNPPTI

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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存储类别

12 - Non Combustible Liquids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

法规信息

低风险生物材料
常规特殊物品
此项目有

历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

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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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