Recombinant Escherichia coli Ribonuclease R (rnr), partial

Code CSB-YP321970ENV
MSDS
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Source Yeast
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Code CSB-EP321970ENV
MSDS
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Source E.coli
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Code CSB-EP321970ENV-B
MSDS
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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-BP321970ENV
MSDS
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Source Baculovirus
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Code CSB-MP321970ENV
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
rnr
Uniprot No.
Alternative Names
rnr; vacB; yjeC; b4179; JW5741; Ribonuclease R; RNase R; EC 3.1.13.1; Protein VacB
Species
Escherichia coli (strain K12)
Protein Length
Partial
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.

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Target Background

Function
3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs (rRNAs, tRNAs and SsrA/tmRNA). In stationary phase, involved in the post-transcriptional regulation of ompA mRNA stability. Shortens RNA processively to di- and trinucleotides. In vitro, exhibits helicase activity, which is independent of its RNase activity. RNases 2 and R (rnb and this entry) contribute to rRNA degradation during starvation, while RNase R and PNPase (this entry and pnp) are the major contributors to quality control of rRNA during steady state growth. Required for the expression of virulence genes in enteroinvasive strains of E.coli.
Gene References into Functions
  1. Data indicate that RNase R is a proficient enzyme, capable of concurrently binding, unwinding and degrading structured RNA in a highly processive manner during RNA decay. PMID: 29036353
  2. These findings indicate that the intrinsic helicase activity of RNase R is required for its proper functioning in vivo and for effective RNA metabolism PMID: 27022019
  3. The frequency downshifts of the ring and CO bands are consistent with charge transfer from YO. to W or another residue of RNR. PMID: 26627888
  4. These findings indicate that the helicase activity plays an essential role in the catalytic efficiency of RNase R. PMID: 25931119
  5. This study leads the authors to conclude that RNase R can interact with ribosomal proteins and that this interaction may be a result of this enzyme involvement in the ribosome quality control. PMID: 24517631
  6. RNase R binding to ribosomes is dependent on transfer-messenger RNA (tmRNA)-SmpB, nonstop mRNA, and the modified form of ribosomal protein S12. PMID: 24133211
  7. We show that RNR101 is stabilized in the presence of rifampicin at 42C. PMID: 21527473
  8. analysis of growth stage-dependent modification of RNase R PMID: 21981926
  9. The results presented here show that in fact the RNB domain from RNase R is the one responsible for the degradation of double-stranded substrates. PMID: 21465561
  10. The authors carried out a domain analysis of RNase R and showed that this protein has two distinct activities, RNase and helicase, which are independent of each other and are due to different domains. PMID: 20023028
  11. Data demonstrate that RNase R, which is widespread in prokaryotes and eukaryotes, is an important participant in mRNA decay. PMID: 15664199
  12. RNAse R is dramatically increased under multiple stress conditions, which suggests extensive remodeling of structured RNA in response to the altered environment PMID: 16135521
  13. induced in stationary phase cells and is involved in the post-transcriptional regulation of ompA mRNA. PMID: 16556233
  14. Using a variety of specifically designed substrates, a model shows how RNase R interacts with its substrates and degrades RNA. PMID: 16893880

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Subcellular Location
Cytoplasm.
Protein Families
RNR ribonuclease family, RNase R subfamily
Database Links
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