Recombinant Human ADAR1 Protein Standard (His tag)
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Recombinant Human ADAR1 Protein Standard (His tag) is a Human Fragment protein, expressed in Escherichia coli, with >80%, suitable for sELISA, SDS-PAGE.
View Alternative Names
ADAR1, DSRAD, G1P1, IFI4, ADAR, Double-stranded RNA-specific adenosine deaminase, DRADA, 136 kDa double-stranded RNA-binding protein, Interferon-inducible protein 4, K88DSRBP, p136, IFI-4
- sELISA
Supplier Data
Sandwich ELISA - Recombinant Human ADAR1 Protein Standard (His tag) (AB323090)
Sandwich ELISA with the capture antibody dilution at 2 µg/mL and detector antibody dilution at 0.5 µg/mL.
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human ADAR1 Protein Standard (His tag) (AB323090)
SDS-PAGE analysis of ab323090 under reducing conditions for 2ug protein.
Reactivity data
Product details
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Specifications
Form
Liquid
General info
Function
Catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA) referred to as A-to-I RNA editing (PubMed : 12618436, PubMed : 7565688, PubMed : 7972084). 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.
Post-translational modifications
Sumoylation reduces RNA-editing activity.
Subcellular localisation
Nucleus
Target data
Product promise
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