Recombinant Human Double-stranded RNA-specific editase 1 (ADARB1)

Code CSB-YP001325HU
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Source Yeast
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Code CSB-EP001325HU
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Source E.coli
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Code CSB-EP001325HU-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP001325HU
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Source Baculovirus
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Code CSB-MP001325HU
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
ADARB1
Uniprot No.
Alternative Names
DARB 1; ADARB1; 1700057H01Rik; ADAR2; ADAR2a ; ADAR2a L1 ; ADAR2a L2 ; ADAR2a L3; ADAR2b; ADAR2c ; ADAR2d ; ADAR2g ; Adarb1; Adenosine deaminase; RNA specific; 2; Adenosine deaminase; RNA specific; B1 (homolog of rat RED1) ; Adenosine deaminase; RNA specific; B1 (RED1 homolog rat); Adenosine deaminase; RNA specific; B1; AW124433; AW558573; BB220382; D10Bwg0447e; Double stranded RNA specific editase 1; Double-stranded RNA-specific editase 1; DRABA2; DRADA2; dsRNA adenosine deaminase; EC 3.5.-.- ; Human dsRNA adenosine deaminase DRADA2 ; Human dsRNA adenosine deaminase DRADA2b; EC 3.5; OTTHUMP00000115341 ; OTTHUMP00000115342 ; RED 1; RED1_HUMAN; RNA editase ; RNA editase 1; RNA editing deaminase 1; RNA editing enzyme 1; RNA editing enzyme 1; rat; homolog of; RNA specific adenosine deaminase B1 ; RNA-editing deaminase 1; RNA-editing enzyme 1
Species
Homo sapiens (Human)
Expression Region
1-741
Target Protein Sequence
MDIEDEENMS SSSTDVKENR NLDNVSPKDG STPGPGEGSQ LSNGGGGGPG RKRPLEEGSN GHSKYRLKKR RKTPGPVLPK NALMQLNEIK PGLQYTLLSQ TGPVHAPLFV MSVEVNGQVF EGSGPTKKKA KLHAAEKALR SFVQFPNASE AHLAMGRTLS VNTDFTSDQA DFPDTLFNGF ETPDKAEPPF YVGSNGDDSF SSSGDLSLSA SPVPASLAQP PLPVLPPFPP PSGKNPVMIL NELRPGLKYD FLSESGESHA KSFVMSVVVD GQFFEGSGRN KKLAKARAAQ SALAAIFNLH LDQTPSRQPI PSEGLQLHLP QVLADAVSRL VLGKFGDLTD NFSSPHARRK VLAGVVMTTG TDVKDAKVIS VSTGTKCING EYMSDRGLAL NDCHAEIISR RSLLRFLYTQ LELYLNNKDD QKRSIFQKSE RGGFRLKENV QFHLYISTSP CGDARIFSPH EPILEGSRSY TQAGVQWCNH GSLQPRPPGL LSDPSTSTFQ GAGTTEPADR HPNRKARGQL RTKIESGEGT IPVRSNASIQ TWDGVLQGER LLTMSCSDKI ARWNVVGIQG SLLSIFVEPI YFSSIILGSL YHGDHLSRAM YQRISNIEDL PPLYTLNKPL LSGISNAEAR QPGKAPNFSV NWTVGDSAIE VINATTGKDE LGRASRLCKH ALYCRWMRVH GKVPSHLLRS KITKPNVYHE SKLAAKEYQA AKARLFTAFI KAGLGAWVEK PTEQDQFSLT P
Protein Length
Full length protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

Customer Reviews and Q&A

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Target Background

Function
Catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA) referred to as A-to-I RNA editing. 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; 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 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 which consequently alter their functional activities. Edits GRIA2 at both the Q/R and R/G sites efficiently but converts the adenosine in hotspot1 much less efficiently. Can exert a proviral effect towards human immunodeficiency virus type 1 (HIV-1) and enhances 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. Can inhibit cell proliferation and migration and can stimulate exocytosis.; Has a lower catalytic activity than isoform 2.; Has 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, which correlated 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. 2-way interaction between TPH2 rs4290270 and general traumas revealed that TT homozygotes with history of general traumas had an increased risk for suicide attempt. 3-way interaction of general traumas, TPH2 rs4290270 and ADARB1 rs4819035 indicated that highest predisposition to suicide attempt was observed in individuals who experienced general traumas and were TT homozygote for rs4290270 and TT homozygote for 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. PMID: 27065196
  5. we determined the importance of specific amino acids at 19 different positions in the ADAR2 5' binding loop and revealed six residues that provide essential structural elements supporting the fold of the loop and key RNA-binding functional groups. This work provided new insight 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, like 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 global shape of RNA may play an important role in the specific reading mechanism of ADAR2. PMID: 26252972
  10. we conclude 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 has a possible 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 give insight 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 death of motor neurons in ALS. PMID: 22226999
  22. The strong functional similarity of human ADAR2 and Drosophila Adar suggests rather 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 human brain PMID: 12859334
  30. assayed enzymatic activity of N-terminal deletion constructs of hADAR2 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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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
Database Links

HGNC: 226

OMIM: 601218

KEGG: hsa:104

STRING: 9606.ENSP00000353920

UniGene: Hs.474018

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