ADARB1 Antibody

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Description

Research Applications

ADARB1 antibodies are widely used to investigate the protein’s expression and function in diverse biological contexts:

Cancer Biology

  • Lung Adenocarcinoma (LUAD): Low ADARB1 expression correlates with poor prognosis, shorter survival, and increased metastasis. Studies using ADARB1 antibodies in Western blot and RT-PCR confirmed its tumor-suppressive role in LUAD cell lines (e.g., H358, A549) .

  • Mechanistic Insights: Knockdown of ADARB1 via siRNA enhances LUAD cell migration, as demonstrated in wound healing assays .

Neurological Research

  • ADARB1 edits the Q/R site of the GluA2 subunit of AMPA receptors, critical for regulating calcium permeability in neurons. Antibodies help validate ADARB1 expression in brain tissues and cell models .

Immune Regulation

  • While ADARB1’s role is less defined than ADAR1 in immune signaling, its antibodies aid in studying potential cross-talk with innate immune pathways .

Table: ADARB1 Antibody in Published Studies

Study FocusMethodologyKey OutcomeCitation
LUAD MetastasisWB, siRNA, Wound HealingADARB1 suppression increases metastasis
AMPA Receptor EditingIP, RIPConfirmed ADARB1’s role in RNA editing
Splice Variant DetectionWBIdentified isoforms at 50 kDa and 75 kDa

Technical Considerations

  • Band Discrepancies: Western blot often shows a strong ~50 kDa band alongside the predicted 75 kDa band, likely due to splice variants or post-translational modifications .

  • Methylation Link: DNA methylation inhibitors (e.g., 5-aza-2-deoxycytidine) upregulate ADARB1, suggesting epigenetic regulation in cancer .

Product Specs

Form
Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
Lead Time
Typically, we can ship the products within 1-3 business days after receiving your orders. Delivery times may vary depending on the purchasing method or location. For specific delivery times, please consult your local distributors.
Synonyms
tibody; ADARB1 antibody; 1700057H01Rik antibody; ADAR2 antibody; ADAR2a antibody; ADAR2a L1 antibody; ADAR2a L2 antibody; ADAR2a L3 antibody; ADAR2b antibody; ADAR2c antibody; ADAR2d antibody; ADAR2g antibody; Adarb1 antibody; Adenosine deaminase; RNA specific; 2 antibody; Adenosine deaminase; RNA specific; B1 (homolog of rat RED1) antibody; Adenosine deaminase; RNA specific; B1 (RED1 homolog rat) antibody; Adenosine deaminase; RNA specific; B1 antibody; AW124433 antibody; AW558573 antibody; BB220382 antibody; D10Bwg0447e antibody; Double stranded RNA specific editase 1 antibody; Double-stranded RNA-specific editase 1 antibody; DRABA2 antibody; DRADA2 antibody; dsRNA adenosine deaminase antibody; EC 3.5.-.- antibody; Human dsRNA adenosine deaminase DRADA2 antibody; Human dsRNA adenosine deaminase DRADA2b; EC 3.5 antibody; OTTHUMP00000115341 antibody; OTTHUMP00000115342 antibody; RED 1 antibody; RED1_HUMAN antibody; RNA editase antibody; RNA editase 1 antibody; RNA editing deaminase 1 antibody; RNA editing enzyme 1 antibody; RNA editing enzyme 1; rat; homolog of antibody; RNA specific adenosine deaminase B1 antibody; RNA-editing deaminase 1 antibody; RNA-editing enzyme 1 antibody
Target Names
ADARB1
Uniprot No.

Target Background

Function
ADARB1 (Adenosine Deaminase Acting on RNA 1), also known as ADAR1, is an enzyme that catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA). This process, known as A-to-I RNA editing, can significantly impact gene expression and function through several mechanisms, including: altering mRNA translation by modifying codons and consequently the amino acid sequence of proteins, influencing pre-mRNA splicing by modifying splice site recognition sequences, affecting RNA stability by changing sequences involved in nuclease recognition, contributing to genetic stability in RNA virus genomes by modifying sequences during viral RNA replication, and impacting RNA structure-dependent activities such as microRNA production, targeting, or protein-RNA interactions. ADARB1 can edit both viral and cellular RNAs, and it can edit RNAs at multiple sites (hyper-editing) or at specific sites (site-specific editing). Cellular RNA substrates for ADARB1 include: bladder cancer-associated protein (BLCAP), neurotransmitter receptors for glutamate (GRIA2 and GRIK2) and serotonin (HTR2C), GABA receptor (GABRA3), and potassium voltage-gated channel (KCNA1). Site-specific RNA editing of transcripts encoding these proteins results in amino acid substitutions, leading to alterations in their functional activities. ADARB1 edits GRIA2 at both the Q/R and R/G sites efficiently but converts the adenosine in hotspot1 much less efficiently. ADARB1 can exert a proviral effect towards human immunodeficiency virus type 1 (HIV-1), enhancing its replication via both an editing-dependent and editing-independent mechanism. The former involves editing of adenosines in the 5'UTR, while the latter occurs via suppression of EIF2AK2/PKR activation and function. ADARB1 can inhibit cell proliferation and migration and can stimulate exocytosis. It has a lower catalytic activity than isoform 2 and a higher catalytic activity than isoform 1.
Gene References Into Functions
  1. Adenosine-to-inosine editing in human miRNAs is enriched in seed sequence, influenced by sequence contexts, and significantly hypoedited in glioblastoma multiforme. This hypoediting correlates with downregulation of ADAR2. PMID: 28550310
  2. The deaminase domain-RNA contact surfaces are reviewed, and models of how full-length ADARs, bearing double-stranded RNA-binding domains (dsRBDs) and deaminase domains, could process naturally occurring substrate RNAs are presented. PMID: 28217931
  3. A two-way interaction between TPH2 rs4290270 and general traumas revealed that individuals with TT homozygotes and a history of general traumas had an increased risk for suicide attempts. A three-way interaction of general traumas, TPH2 rs4290270, and ADARB1 rs4819035 indicated that the highest predisposition to suicide attempts was observed in individuals who experienced general traumas and were TT homozygotes for both rs4290270 and rs4819035. PMID: 28084537
  4. Four crystal structures of the human ADAR2 deaminase domain bound to RNA duplexes bearing a mimic of the deamination reaction intermediate have been determined. PMID: 27065196
  5. The importance of specific amino acids at 19 different positions in the ADAR2 5' binding loop was determined, revealing six residues that provide essential structural elements supporting the fold of the loop and key RNA-binding functional groups. This research provided new insights into RNA recognition by ADAR2 and established a new tool for defining structure-function relationships in ADAR reactions. PMID: 27614075
  6. Data indicate that ADAR2 suppresses tumor growth and induces apoptosis by editing and stabilizing IGFBP7 in esophageal squamous cell carcinoma. PMID: 28035363
  7. These findings suggest that adenosine deaminase acting on RNA 2 is subject to different regulations by DNA methyltransferase and histone deacetylase enzymes in neuronal SH-SY5Y cells. PMID: 26485095
  8. These data suggest that, similar to ADAR2, underlying sequences in dsRNA may influence how NF90 recognizes its target RNAs. PMID: 26712564
  9. Detailed structural analysis indicates that the minor groove width of dsRNA and the global shape of RNA may play a crucial role in the specific reading mechanism of ADAR2. PMID: 26252972
  10. The research concludes that this aberrant alternative splicing pattern of ADAR2 downregulates A-to-I editing in glioma. PMID: 25873329
  11. ADARB1 rs9983925 and rs4819035 and HTR2C rs6318 were associated with suicide attempt risk. PMID: 25732952
  12. ADAR2 is a key factor for maintaining edited-miRNA population and balancing the expression of several essential miRNAs involved in cancer. PMID: 25582055
  13. The ADAR2 alternative splicing variants may be correlated with the invasiveness of gliomas. PMID: 24509948
  14. Characterization of the ADAR2 catalytic domain-RNA interaction. PMID: 25564529
  15. ADAR2-mediated editing of the complementary antisense transcripts is a novel mechanism for regulating the biogenesis of specific miRNAs during hepatocarcinogenesis. PMID: 24386085
  16. Altered RNA editing efficiency of AMPA receptors due to down-regulation of ADAR2 may play a role in the pathophysiology of mental disorders. PMID: 24443933
  17. The results represent the first evidence that the ADAR1 p150 isoform is the determinant of DSH and may provide insights into the currently unknown mechanisms involved in the development of DSH. PMID: 23621630
  18. Findings demonstrate that post-transcriptional A-to-I RNA editing might be crucial for glioblastoma pathogenesis, identify ADAR2-editing enzyme as a candidate tumor suppressor gene, and provide proof that ADAR2 may represent a suitable target. PMID: 22525274
  19. ADAR2 activity does not consistently change due to the overexpression or knockdown of TDP-43 or the expression of abnormal TDP-43 in amyotrophic lateral sclerosis (ALS) motor neurons. PMID: 22414730
  20. ADAR2 activity at the GluA2 pre-mRNA Q/R site correlates with the ADAR2 mRNA level relative to the GluA2 pre-mRNA in different cultured cell lines. PMID: 22366356
  21. These results indicated that ADAR2 downregulation is a profound pathological change relevant to the death of motor neurons in ALS. PMID: 22226999
  22. The strong functional similarity of human ADAR2 and Drosophila Adar suggests that these are true orthologs. PMID: 21622951
  23. The authors found that, analogously to ADAR1, ADAR2 enhances the release of progeny virions by an editing-dependent mechanism. PMID: 21289159
  24. Elucidation of the molecular mechanism underlying the co-occurrence of reduced ADAR2 activity and abnormal TDP-43 pathology in the same motor neurons may provide a clue to the neurodegenerative process of sporadic amyotrophic lateral sclerosis. PMID: 20372915
  25. The high conservation of the novel ADAR2 alternative exon in mammals indicates a physiological importance for this exon. PMID: 20215858
  26. Overexpression inhibits HDV RNA replication and compromises virus viability. PMID: 11907222
  27. Adenosine to inosine RNA editing requires formation of a ternary complex on the GluR-B R/G site. PMID: 12163487
  28. Short inhibitory RNA-mediated knockdown of host ADAR1 expression, but not that of ADAR2, led to decreased HDV amber/W editing and virus production. PMID: 12414985
  29. The Q/R site of GluRs editing is regulated in a regional manner, and the GluR2 Q/R site editing is critically regulated by ADAR2 in the human brain. PMID: 12859334
  30. Enzymatic activity of N-terminal deletion constructs of hADAR2 was assayed to determine the role of the double-stranded RNA binding motifs and the intervening linker peptide. PMID: 15383678
  31. Inositol hexakisphosphate is buried within the catalytic domain of ADAR2 and is required for editing of transfer RNA. PMID: 16141067
  32. Results show that bipolar affective disorder may not be caused by mutations in ADARB1. PMID: 16733555
  33. Serum adenosine deaminase (ADA) activity of active Behcet's disease (BD) was higher than that of inactive BD (P < 0.01), but erythrocyte ADA activity was found to be lower in active BD than inactive BD (P < 0.01). PMID: 16961545
  34. CD26 and cell surface adenosine deaminase are selectively expressed on ALK-positive, but not on ALK-negative, anaplastic large cell lymphoma and Hodgkin's lymphoma. PMID: 17071493
  35. The CTD of POLR2A and ADAR2 function together to enforce the order of events that allows editing to precede splicing, and they furthermore suggest a new role for the CTD as a coordinator of two interdependent pre-mRNA processing events. PMID: 17525170
  36. Reference values of serum adenosine deaminase (ADA) in normal pregnancy may provide important database for making clinical decisions in pregnancies complicated by conditions where cellular immunity has been altered. PMID: 17728516
  37. Analysis of a splice variant that extends the open reading frame of ADAR2 by 49 amino acids through the utilization of an exon located 18 kilobases upstream of the previously annotated first coding exon and driven by a candidate alternative promoter. PMID: 19156214
  38. Our understanding of the importance of functional groups found in the edited nucleotide and the role of specific active site residues of ADAR2. PMID: 19642681

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Database Links

HGNC: 226

OMIM: 601218

KEGG: hsa:104

STRING: 9606.ENSP00000353920

UniGene: Hs.474018

Subcellular Location
Nucleus. Nucleus, nucleolus.; [Isoform 1]: Nucleus. Nucleus, nucleolus.; [Isoform 2]: Nucleus. Nucleus, nucleolus.
Tissue Specificity
Highly expressed in brain and heart and at lower levels in placenta. Fair expression in lung, liver and kidney. Detected in brain, heart, kidney, lung and liver (at protein level).; [Isoform 5]: Highly expressed in hippocampus and colon. Expressed in pedi

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