Recombinant E.Coli Ribonuclease E (RNE) Protein (His)

Beta LifeScience SKU/CAT #: BLC-06801P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant E.Coli Ribonuclease E (RNE) Protein (His)

Beta LifeScience SKU/CAT #: BLC-06801P
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Product Overview

Description Recombinant E.Coli Ribonuclease E (RNE) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb P21513
Target Symbol RNE
Species Escherichia coli (strain K12)
Expression System E.coli
Tag N-6His
Target Protein Sequence EQKKANIYKGKITRIEPSLEAAFVDYGAERHGFLPLKEIAREYFPANYSAHGRPNIKDVLREGQEVIVQIDKEERGNKGAALTTFISLAGS
Expression Range 35-125aa
Protein Length Partial
Mol. Weight 16.1 kDa
Research Area Others
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function Endoribonuclease that plays a central role in RNA processing and decay. Required for the maturation of 5S and 16S rRNAs and the majority of tRNAs. Also involved in the degradation of most mRNAs. Can also process other RNA species, such as RNAI, a molecule that controls the replication of ColE1 plasmid, and the cell division inhibitor DicF-RNA. It initiates the decay of RNAs by cutting them internally near their 5'-end. It is able to remove poly(A) tails by an endonucleolytic process. Required to initiate rRNA degradation during both starvation and quality control; acts after RNase PH (rph) exonucleolytically digests the 3'-end of the 16S rRNA. Degradation of 16S rRNA leads to 23S rRNA degradation. Processes the 3 tRNA(Pro) precursors immediately after the 3'-CCA to generate the mature ends.; Prefers 5'-monophosphorylated substrates over 5'-triphosphorylated substrates. 5'-monophosphate-assisted cleavage requires at least 2 and preferably 3 or more unpaired 5'-terminal nucleotides. The optimal spacing between the 5' end and the scissile phosphate appears to be 8 nucleotides. Any sequence of unpaired nucleotides at the 5'-end is tolerated.
Subcellular Location Cytoplasm. Cell inner membrane; Peripheral membrane protein; Cytoplasmic side.
Protein Families RNase E/G family, RNase E subfamily
Database References

Gene Functions References

  1. This study suggests that, rather than its role in the processing of any one particular substrate, its distributed functions on all the different substrates (mRNA, rRNA, and tRNA) are responsible for the essentiality of RNase E in E. coli. PMID: 28167522
  2. Small RNAs processing and Hfq binding determinants for RNase E: RNase E cleaves any RNA fused to the 3' end. PMID: 26531825
  3. bacteria producing RNase E, have nutritional requirements different from those of cells supplied with only the N-terminal catalytic region of RNase E and mitigation of RNase E deficiency by overexpression of RNase G, is also affected by carbon source. PMID: 23275245
  4. Electrostatic potentials of were found to be conserved, highly positive, and spread over a large surface area encompassing four putative membrane-binding regions identified in the "large" domain. PMID: 22509045
  5. Strains harbouring rne alleles that express variants of RNase E in which 5' sensing or direct entry are inactivated, are viable. PMID: 22074454
  6. Increased abundance of R-loops in the rho and nusG mutants contributes to rescue the lethality associated with loss of the two RNase E cleavage pathways. PMID: 22026368
  7. demonstrated that CsdA, whose expression is induced by cold shock, interacts physically and functionally with RNase E PMID: 15554978
  8. The RNase E tetramer has two nonequivalent subunit interfaces, one of which is mediated by a single, tetrathiol-zinc complex; one or both interfaces organize the active site, which is distinct from the primary site of RNA binding. PMID: 15779893
  9. Observed role of RNase E in sodB mRNA turnover. PMID: 15781494
  10. crystal structures of the catalytic domain of RNase E as trapped allosteric intermediates with RNA substrates PMID: 16237448
  11. RNase E is required for induction of the glutamate-dependent acid resistance system in a RpoS-independent manner PMID: 17213667
  12. RNaseE and the other constituents of the RNA degradosome are components of the bacterial cytoskeleton PMID: 17242352
  13. This paper demonstrated that RNase E, a key endonuclease responsible for mRNA degradation in E. coli, regulates cspE transcript stability, possibly through the assembly of a degradosome. PMID: 18177308
  14. RNaseE and RNA helicase B play central roles in the cytoskeletal organization of the RNA degradosome PMID: 18337249
  15. RraA and RraB have a conserved property to directly act on RNAse E-related enzymes and inhibit their ribonucleolytic activity. PMID: 18510556
  16. Study shows that the arginine-rich RNA binding domain (ARRBD) of RNase E is important for the initial endoribonucleolytic cleavage of RNAI but dispensable for the endoribonucleolytic cleavages of the Rep mRNA. PMID: 19426759

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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