Product Details

Purity

>85% (SDS-PAGE)

Target Names

rnpA

Uniprot No.

P0A7Y8

Alternative Names

rnpA; b3704; JW3681; Ribonuclease P protein component; RNase P protein; RNaseP protein; EC 3.1.26.5; Protein C5

Species

Escherichia coli (strain K12)

Expression Region

1-119

Target Protein Sequence

MVKLAFPREL RLLTPSQFTF VFQQPQRAGT PQITILGRLN SLGHPRIGLT VAKKNVRRAH ERNRIKRLTR ESFRLRQHEL PAMDFVVVAK KGVADLDNRA LSEALEKLWR RHCRLARGS

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

Protein 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.

Target Background

Function

RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.

Gene References into Functions

The comparative biology of Escherichia coli RNase P and Arabidopsis thaliana PRORP isozymes has been reported. PMID: 28499021
The ability of RNase P to initiate tRNA processing at the 3' ends of long primary transcripts by endonucleolytically removing the Rho-independent transcription terminator represents a previously unidentified function for the enzyme. PMID: 25183518
Rules govern substrate recognition by C5, which reveal specificity that is hidden in cellular substrates for RNase P; nonspecific and specific RNA-binding modes may not differ fundamentally, but represent distinct parts of common affinity distributions. PMID: 24056935
C5 protein has evolved to compensate for tRNA variation at positions important for binding to P RNA, allowing for tRNA specialization PMID: 19917291
results showed the presence of a bulge at U69 in the P4 domain was important in the holo enzyme; the conserved bases G63 and G64 in the J3/4 domain were important for efficient ribozyme reactions; domains displayed different responses to metal ions PMID: 15215612
mutations in the P3 domain did not affect the cleavage site selection of the pre-tRNA substrate, but did affect the efficiency of cleavage of the substrate PMID: 15527768
data indicate that the conserved AGGA sequence was important for efficient ribozyme reactions, and suggested that the length mutations affected ribozyme activity through metal ion binding steps PMID: 15618639
RNase P from Escherichia coli cleaves the coenzyme B12 riboswitch from E. coli and a similar one from Bacillus subtilis. PMID: 16061811
RNase P stabilizes the global structure of RNase P RNA, and influences holoenzyme dimer formation and precursor tRNA. PMID: 16163391
RNAs in a T-shape structure can be substrates for the ribozyme reactions even at low concentrations of magnesium ions, and the RNA in a natural L-shape is the best substrate for both the ribozyme and the holo enzyme. PMID: 16244456
assembly of the E. coli RNase P holoenzyme involves RNA-dependent folding and stabilization of C5 protein PMID: 16750220
analysis of antisense inhibition of RNase P PMID: 16901906
Cognate protein subunit C5 enhances metal ion affinity in the active site of RNAase P, and thus is likely to contribute significantly to rate enhancement at physiological metal ion concentrations. PMID: 17652407
Description for the first time of a previously unidentified pathway for the maturation of tRNAs in polycistronic operons where the processing of the primary transcripts only involves RNase P. PMID: 17981836
These results demonstrate that the C5 protein metabolically stabilizes M1 RNA in the cell. PMID: 19114042

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Protein Families

RnpA family

Database Links

KEGG: ecj:JW3681

STRING: 316385.ECDH10B_3890

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Recombinant Escherichia coli Ribonuclease P protein component (rnpA)

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