Recombinant Escherichia coli Peptide chain release factor 2 (prfB)

In Stock
Code CSB-EP362014ENV
Abbreviation Recombinant E.coli prfB protein
MSDS
Size $388
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Product Details

Purity
Greater than 95% as determined by SDS-PAGE.
Activity
Not Test
Target Names
prfB
Uniprot No.
Research Area
Others
Alternative Names
RF-2
Species
Escherichia coli (strain K12)
Source
E.coli
Expression Region
1-365aa
Target Protein Sequence
MFEINPVNNRIQDLTERSDVLRGYLDYDAKKERLEEVNAELEQPDVWNEPERAQALGKERSSLEAVVDTLDQMKQGLEDVSGLLELAVEADDEETFNEAVAELDALEEKLAQLEFRRMFSGEYDSADCYLDIQAGSGGTEAQDWASMLERMYLRWAESRGFKTEIIEESEGEVAGIKSVTIKISGDYAYGWLRTETGVHRLVRKSPFDSGGRRHTSFSSAFVYPEVDDDIDIEINPADLRIDVYRTSGAGGQHVNRTESAVRITHIPTGIVTQCQNDRSQHKNKDQAMKQMKAKLYELEMQKKNAEKQAMEDNKSDIGWGSQIRSYVLDDSRIKDLRTGVETRNTQAVLDGSLDQFIEASLKAGL
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.
Mol. Weight
48.2 kDa
Protein Length
Full Length
Tag Info
C-terminal 6xHis-tagged
Form
Liquid or 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
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose.
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°C/-80°C. 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
3-7 business days
Datasheet & COA
Please contact us to get it.

Customer Reviews and Q&A

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Target Background

Function
Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA. Acts as a peptidyl-tRNA hydrolase. In the presence of truncated mRNA in the 70S ribosome, ArfA and RF2 interact such that the GGQ peptide hydrolysis motif of RF2 rises into the peptidyl-transferase center and releases the ribosome. Recruited by ArfA to rescue stalled ribosomes in the absence of a normal stop codon.
Gene References into Functions
  1. both RF1 binding and RF2 binding are sufficient to shift the population of posthydrolysis ribosome complexes from primarily the rotated to the nonrotated state only when a cognate stop codon is present in the A-site. PMID: 29499110
  2. The structures demonstrate how ArfA 'senses' the vacant mRNA tunnel and activates RF2 to mediate peptide release without a stop codon, allowing stalled ribosomes to be recycled. PMID: 28300532
  3. The authors characterized the ArfA pathway of non-productive translation complexe resolution in vitro and identified RF2 as a factor that cooperates with ArfA to hydrolyse peptidyl-tRNAs located in the P-site of the stalled ribosome. PMID: 22857598
  4. RF2 binds to stalled ribosomes only in the presence of ArfA, demonstrating that ArfA recruits RF2 into the A site of the ribosome to facilitate peptidyl-tRNA hydrolysis. PMID: 22922063
  5. Mutations at the two positions on 23S rRNA did not affect aminoacyl-tRNA (aa-tRNA) accommodation, peptide bond formation, or the fidelity of aa-tRNA selection, but impaired RF2-catalyzed peptide release. PMID: 20668033
  6. prfB encoding RF2 is a new member of the polyamine modulon PMID: 16476727
  7. L11 mutations located on the surface of two domains of L11 affect the interaction of L11 with RF1 and RF2 thereby leading to an altered translation termination. PMID: 16556224
  8. All cognate ribosomal E-site duplex interactions are adequate for any translational role, including effects on reading frame maintenance during RF-2 programmed frameshifting. PMID: 17660276
  9. RF1 and RF2 are methylated on the Gln residue of a universally conserved tripeptide motif GGQ, which interacts with the peptidyl transferase center of the large ribosomal subunit, triggering hydrolysis of the ester bond in peptidyl-tRNA PMID: 17932046
  10. analysis of the direct relationship between cumulative signal phase and reading frame of prfB in E. coli PMID: 17946637

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Subcellular Location
Cytoplasm.
Protein Families
Prokaryotic/mitochondrial release factor family
Database Links
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