Recombinant Mouse Double-stranded RNA-specific editase 1 (Adarb1)

Code CSB-YP821035MO
MSDS
Size Pls inquire
Source Yeast
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-EP821035MO
MSDS
Size Pls inquire
Source E.coli
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-EP821035MO-B
MSDS
Size Pls inquire
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.
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-BP821035MO
MSDS
Size Pls inquire
Source Baculovirus
Have Questions? Leave a Message or Start an on-line Chat
Code CSB-MP821035MO
MSDS
Size Pls inquire
Source Mammalian cell
Have Questions? Leave a Message or Start an on-line Chat

Product Details

Purity
>85% (SDS-PAGE)
Target Names
Adarb1
Uniprot No.
Alternative Names
Adarb1; Adar2; Red1; Double-stranded RNA-specific editase 1; EC 3.5.4.37; RNA-editing deaminase 1; RNA-editing enzyme 1; dsRNA adenosine deaminase
Species
Mus musculus (Mouse)
Expression Region
1-711
Target Protein Sequence
MDIEDEENMS SSSTDIKENR NLDNMPPKDS STPGPGEGIP LSNGGGGSTS RKRPLEEGSN GHSKYRLKKR RKTPGPVLPK NALMQLNEIK PGLQYMLLSQ TGPVHAPLFV MSVEVNGQVF EGSGPTKKKA KLHAAEKALR SFVQFPNASE AHLAMGRTLS VNTDFTSDQA DFPDTLFNGF ETPDKSEPPF YVGSNGDDSF SSSGDVSLSA SPVPASLTQP PLPIPPPFPP PSGKNPVMIL NELRPGLKYD FLSESGESHA KSFVMSVVVD GQFFEGSGRN KKLAKARAAQ SALATVFNLH LDQTPSRQPV LSEGLQLHLP QVLADAVSRL VLGKFSDLTD NFSSPHARRK VLSGVVMTTG TDVKDAKVIS VSTGTKCING EYMSDRGLAL NDCHAEIISR RSLLRFLYAQ LELYLNNKED QKKSIFQKSE RGGFRLKDTV QFHLYISTSP CGDARIFSPH EPVLEGMTPD SHQLTEPADR HPNRKARGQL RTKIESGEGT IPVRSNASIQ TWDGVLQGER LLTMSCSDKI ARWNVVGIQG SLLSIFVEPI YFSSIILGSL YHGDHLSRAM YQRISNIEDL PPLYTLNKPL LSGISNAEAR QPGKAPNFSV NWTVGDATIE VINATTGKDE LGRPSRLCKH ALYCRWMRVH GKVPPHLLRT KITKPTTYHE SKLAAREYQA AKARLFTAFI KAGLGAWVEK PTEQDQFSFT 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

 Customer Reviews

There are currently no reviews for this product.

Submit a Review here

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 inhibit cell proliferation and migration and can stimulate exocytosis.
Gene References into Functions
  1. FMRP inhibits ADAR2 activity, absence of FMRP results in defects of RNA editing of neuronal mRNAs in the mouse model of Fragile X Syndrome. PMID: 28640668
  2. ADARB1 mediates adenosine to inosine RNA editing in the testis, and these editing events are dispensable for male fertility in an inbred mouse strain in the lab. PMID: 28395340
  3. that ADAR2 is a mediator of injury-induced tactile allodynia and thus a potential therapeutic target for the treatment of neuropathic pain PMID: 28126736
  4. Results show that ADAR2 is important in site-specific changes of protein coding sequences but has relatively modest effects on gene expression and splicing in the adult mouse frontal cortex. PMID: 26669816
  5. Thus, Adarb1 and Adarb2 have nearly exclusive expression within brain tissue, while Adar has more appreciable expression across multiple tissues. PMID: 26768488
  6. After fear conditioning protocol, mRNA expression of ADAR2 increased in amygdala and hippocampus, and those mice had a learning-dependent increase in the alternatively spliced inactive form of ADAR2 in the amygdala. PMID: 26383032
  7. ADAR2 is a key factor for maintaining edited-miRNA population and balancing the expression of several essential miRNAs involved in cancer. PMID: 25582055
  8. This study clearly demonstrates that ADAR2 influences miRNA abundance and targeting at several levels in the mouse brain. PMID: 25260591
  9. chronically elevated intraocular pressure in adult mice reduces expression of the ADAR2 enzyme. PMID: 24608178
  10. Analysis of editing in the filamin A encoding mRNA shows very high editing levels outside the nervous system; further shows FLNA editing is mainly achieved by ADAR2 but that in some cases ADAR1 can efficiently compensate for ADAR2. PMID: 24025532
  11. Results suggest that ADAR2-reduction is associated with progressive deterioration of nuclear architecture, resulting in vacuolated nuclei due to a Ca2+-permeable AMPA receptor-mediated mechanism PMID: 24440630
  12. 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
  13. Goal-oriented overeating behavior of ADAR2 transgenic mice is associated with altered feeding, reward-related mRNAs and hyperactive brain mesolimbic region. PMID: 23323881
  14. The JNK1 pathway may be functionally linked to the nutrient-sensing actions of ADAR2-mediated RNA editing in professional secretory cells. PMID: 23139803
  15. Study show co-occurrence of TDP-43 mislocalization with reduced activity of an RNA editing enzyme, ADAR2, in aged mouse motor neurons. PMID: 22916266
  16. miRNA abundance and miRNA processing are mainly influenced by ADARB1; an additional loss of ADAR has only a minor effect on expression of mature miRNAs. PMID: 22310477
  17. Through these gene knockout animal models we demonstrated for the first time that ADAR1 is an essential molecule for skin integrity. PMID: 21788117
  18. These results altogether suggest that altered 5HT(2C) R function could be contributing to enhanced depression-like behavior of ADAR2 transgenic mice and further implicate ADAR2 as a contributing factor in cases of affective disorder. PMID: 21615684
  19. ADAR2 protein levels and catalytic activity are coordinately regulated in a positive manner by Pin1 and negatively by WWP2 and this may have downstream effects on the function of glutamate receptor 2. PMID: 21847096
  20. These results provide evidence that ADAR1, and not ADAR2, is the deaminase responsible for protection against virus-induced cytopathic effects, and that ADAR de fi ciency does not adversely affect PyV growth. PMID: 21632755
  21. Requirement of the RNA-editing enzyme ADAR2 for normal physiology in mice. PMID: 21467037
  22. The loss of ADAR2 activity causes AMPA receptor-mediated death of motor neurons in mice disease model(ALS). PMID: 20826656
  23. Activation of phospholipase C and alternative splicing of pre-mRNA encoding the editing enzymes ADAR1 and ADAR2 have both overlapping and specific roles in modulating 5-HT2CR editing phenotypes. PMID: 20651031
  24. the nucleolar localization of ADAR2 represents an important mechanism by which RNA editing can be modulated by the sequestration of enzymatic activity from potential RNA substrates in the nucleoplasm PMID: 14612560
  25. Through the subcellular targeting of minigenes that contain natural editing sites, we show that ADAR2- but not ADAR1-mediated RNA editing occurs in the nucleolus. PMID: 15939761
  26. mature miRNA-142 expression levels increased substantially in ADAR1 null or ADAR2 null mice PMID: 16369484
  27. ADAR2 autoediting is a key regulator of ADAR2 protein expression and activity in vivo. PMID: 16382140
  28. RNA editing by ADAR2 in pancreatic islets and beta-cells is metabolically regulated by nutritional and energy status PMID: 16956888
  29. ADAR2 may possess additional biological activities beyond those required for the site-selective deamination of adenosine or may interfere with the actions of other double-stranded RNA-specific binding proteins in the cell PMID: 17567573
  30. Possible target preferences of ADAR1 and ADAR2 were examined by determining the editing status of transcripts derived from mice deficient in either enzyme. PMID: 18430892
  31. 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
  32. ADAR1 and ADAR2 are broadly distributed in most regions of the mouse forebrain by P0. PMID: 19325227
  33. ADAR2 transgenic mice represent a novel rodent model of endogenous behavioral despair and anxiety accompanied by elevated hypothalamo-pituitary adrenal axis activity. PMID: 19361536

Show More

Hide All

Subcellular Location
Nucleus. Nucleus, nucleolus.
Database Links
icon of phone
Call us
301-363-4651 (Available 9 a.m. to 5 p.m. CST from Monday to Friday)
icon of address
Address
7505 Fannin St., Ste 610, Room 7 (CUBIO Innovation Center), Houston, TX 77054, USA
icon of social media
Join us with

Subscribe newsletter

Leave a message

* To protect against spam, please pass the CAPTCHA test below.
CAPTCHA verification
© 2007-2024 CUSABIO TECHNOLOGY LLC All rights reserved. 鄂ICP备15011166号-1