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SAB4200142

Sigma-Aldrich

Anti-ADAR2 antibody, Mouse monoclonal

clone ADAR2-8, purified from hybridoma cell culture

Synonym(s):

Anti-ADARB1, Anti-Adenosine Deaminase, RNA-specific B1, Anti-DRABA2, Anti-DRADA2, Anti-RED1, Anti-RNA Editase 1, Anti-RNA-editing enzyme 1

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

conjugate

unconjugated

antibody form

purified from hybridoma cell culture

antibody product type

primary antibodies

clone

ADAR2-8, monoclonal

mol wt

antigen ~81 kDa

species reactivity

human

packaging

antibody small pack of 25 μL

concentration

~1 mg/mL

technique(s)

western blot: 1-2 μg/mL using HL-60 total cell extract

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... ADARB1(104)

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General description

Adenosine deaminase acting on RNA type 2 (ADAR2) is localized predominantly in the nucleus.
Adenosine deaminase acting on RNA type 2 (ADAR2), also known as adenosine deaminase, RNA specific B1 (ADARB1), is encoded by the gene mapped to human chromosome 21q22.3. ADARB1 is characterized with two double-stranded RNA-binding domains and a deaminase domain involved in editing action.

Application

Monoclonal Anti-ADAR2 antibody produced in mouse has been used in immunoblotting.

Biochem/physiol Actions

Adenosine deaminase acting on RNA type 2 (ADAR2) activity is directly involved in both cell cycle by slowing down cell growth rate at the S-G2 phase and in cell migration. Decrease in ADAR2 editing activity is linked to tumor malignancy (astrocytoma grade I-IV) in children.
Adenosine deaminase acting on RNA type 2 (ADAR2) enzyme plays a vital role in editing pre-mRNA of glutamate receptor B subunit. Combined effect of ADAR2 and HTR2C (5-hydroxytryptamine receptor 2C) variants contribute to the suicide attempt (SA) vulnerability in psychiatric patients. ADAR2 is a candidate gene for neurological diseases, such as bipolar affective disorder and epilepsy. Decrease in the activity of ADAR2 enzyme results in α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptor-mediated death of motor neurons in mice. ADAR2 enzyme is expressed consistently in carcinomas and sarcomas and it is upregulated in lymphomas and seminomas when compared to normal tissues.

Physical form

Solution in 0.01 M phosphate buffered saline pH 7.4, containing 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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Storage Class Code

12 - Non Combustible Liquids

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Dynamic association of RNA-editing enzymes with the nucleolus
Desterro JMP, et al.
Journal of Cell Science, 116(9), 1805-1818 (2003)
Sequence analysis of ADARB1 gene in patients with familial bipolar disorder.
Amore M
Journal of Affective Disorders, 81, 79-85 (2004)
Caterina Cenci et al.
The Journal of biological chemistry, 283(11), 7251-7260 (2008-01-08)
Since alterations in post-transcriptional events can contribute to the appearance and/or progression of cancer, we investigated whether RNA editing, catalyzed by the ADAR (adenosine deaminases that act on RNA) enzymes, is altered in pediatric astrocytomas. We find a decrease in
Genomics screen in transformed stem cells reveals RNASEH2A, PPAP2C, and ADARB1 as putative anticancer drug targets.
Flanagan JM
Molecular Cancer Therapeutics, 8, 249-260 (2009)
Cloning of a human RNA editing deaminase (ADARB1) of glutamate receptors that maps to chromosome 21q22.3.
Mittaz L
Genomics, 41, 210-217 (1997)

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