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> home > Products > Peptides > Blocking Peptides > Adenosine Deaminase (ADAR) Antibody (N-term) Blocking peptide
Adenosine Deaminase (ADAR) Antibody (N-term) Blocking peptide
Synthetic peptide
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- BACKGROUND
| Primary Accession | P55265 |
|---|---|
| Clone Names | 70716004 |
| Gene ID | 103 |
|---|---|
| Other Names | Double-stranded RNA-specific adenosine deaminase, DRADA, 136 kDa double-stranded RNA-binding protein, p136, Interferon-inducible protein 4, IFI-4, K88DSRBP, ADAR, ADAR1, DSRAD, G1P1, IFI4 |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | ADAR |
|---|---|
| Synonyms | ADAR1, DSRAD, G1P1, IFI4 |
| Function | Catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA) referred to as A-to-I RNA editing (PubMed:7972084, PubMed:7565688, PubMed:12618436). This may affect gene expression and function in a number of ways that include mRNA translation by changing codons and hence the amino acid sequence of proteins since the translational machinery read the inosine as a guanosine; pre-mRNA splicing by altering splice site recognition sequences; RNA stability by changing sequences involved in nuclease recognition; genetic stability in the case of RNA virus genomes by changing sequences during viral RNA replication; and RNA structure- dependent activities such as microRNA production or targeting or protein-RNA interactions. Can edit both viral and cellular RNAs and can edit RNAs at multiple sites (hyper-editing) or at specific sites (site- specific editing). Its cellular RNA substrates include: bladder cancer- associated protein (BLCAP), neurotransmitter receptors for glutamate (GRIA2) and serotonin (HTR2C) and GABA receptor (GABRA3). Site-specific RNA editing of transcripts encoding these proteins results in amino acid substitutions which consequently alters their functional activities. Exhibits low-level editing at the GRIA2 Q/R site, but edits efficiently at the R/G site and HOTSPOT1. Its viral RNA substrates include: hepatitis C virus (HCV), vesicular stomatitis virus (VSV), measles virus (MV), hepatitis delta virus (HDV), and human immunodeficiency virus type 1 (HIV-1). Exhibits either a proviral (HDV, MV, VSV and HIV-1) or an antiviral effect (HCV) and this can be editing-dependent (HDV and HCV), editing-independent (VSV and MV) or both (HIV-1). Impairs HCV replication via RNA editing at multiple sites. Enhances the replication of MV, VSV and HIV-1 through an editing-independent mechanism via suppression of EIF2AK2/PKR activation and function. Stimulates both the release and infectivity of HIV-1 viral particles by an editing-dependent mechanism where it associates with viral RNAs and edits adenosines in the 5'UTR and the Rev and Tat coding sequence. Can enhance viral replication of HDV via A-to-I editing at a site designated as amber/W, thereby changing an UAG amber stop codon to an UIG tryptophan (W) codon that permits synthesis of the large delta antigen (L-HDAg) which has a key role in the assembly of viral particles. However, high levels of ADAR1 inhibit HDV replication. |
| Cellular Location | [Isoform 1]: Cytoplasm. Nucleus. Note=Shuttles between the cytoplasm and nucleus (PubMed:7565688, PubMed:24753571). Nuclear import is mediated by TNPO1 (PubMed:24753571). |
| Tissue Location | Ubiquitously expressed, highest levels were found in brain and lung (PubMed:7972084). Isoform 5 is expressed at higher levels in astrocytomas as compared to normal brain tissue and expression increases strikingly with the severity of the tumor, being higher in the most aggressive tumors. |
Research Areas
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Application Protocols
Provided below are standard protocols that you may find useful for product applications.
Background
ADAR is the enzyme responsible for RNA editing by site-specific deamination of adenosines. This enzyme destabilizes double stranded RNA through conversion of adenosine to inosine. Mutations have been associated with dyschromatosis symmetrica hereditaria.
References
Lykke-Andersen,S., RNA 13 (10), 1732-1744 (2007)Li,M., Arch. Dermatol. Res. 299 (5-6), 273-275 (2007)
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$ 277.78
Cat# BP1493a
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