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AB202628

Recombinant Human PNPT1 protein

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(1 Publication)

Recombinant Human PNPT1 protein is a Human Full Length protein, in the 46 to 783 aa range, expressed in Escherichia coli, with >85%, suitable for SDS-PAGE.

View Alternative Names

PNPASE, PNPT1, 3'-5' RNA exonuclease OLD35, PNPase old-35, Polynucleotide phosphorylase 1, Polynucleotide phosphorylase-like protein, PNPase 1

1 Images
SDS-PAGE - Recombinant Human PNPT1 protein (AB202628)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human PNPT1 protein (AB202628)

15% SDS-PAGE analysis of ab202628 (3μg).

Key facts

Purity

>85% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

Q8TCS8

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.4 Constituents: PBS, 10% Glycerol (glycerin, glycerine), 0.02% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMGSAVAVDLGNRKLEISSGKLARFADGSAVVQSGDTAVMVTAVSKTKPSPSQFMPLVVDYRQKAAAAGRIPTNYLRREIGTSDKEILTSRIIDRSIRPLFPAGYFYDTQVLCNLLAVDGVNEPDVLAINGASVALSLSDIPWNGPVGAVRIGIIDGEYVVNPTRKEMSSSTLNLVVAGAPKSQIVMLEASAENILQQDFCHAIKVGVKYTQQIIQGIQQLVKETGVTKRTPQKLFTPSPEIVKYTHKLAMERLYAVFTDYEHDKVSRDEAVNKIRLDTEEQLKEKFPEADPYEIIESFNVVAKEVFRSIVLNEYKRCDGRDLTSLRNVSCEVDMFKTLHGSALFQRGQTQVLCTVTFDSLESGIKSDQVITAINGIKDKNFMLHYEFPPYATNEIGKVTGLNRRELGHGALAEKALYPVIPRDFPFTIRVTSEVLESNGSSSMASACGGSLALMDSGVPISSAVAGVAIGLVTKTDPEKGEIEDYRLLTDILGIEDYNGDMDFKIAGTNKGITALQADIKLPGIPIKIVMEAIQQASVAKKEILQIMNKTISKPRASRKENGPVVETVQVPLSKRAKFVGPGGYNLKKLQAETGVTISQVDEETFSVFAPTPSAMHEARDFITEICKDDQEQQLEFGAVYTATITEIRDTGVMVKLYPNMTAVLLHNTQLDQRKIKHPTALGLEVGQEIQVKYFGRDPADGRMRLSRKVLQSPATTVVRTLNDRSSIVMGEPISQSSSNSQ","proteinLength":"Full Length","predictedMolecularWeight":"83.3 kDa","actualMolecularWeight":null,"aminoAcidEnd":783,"aminoAcidStart":46,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"Q8TCS8","tags":[{"tag":"His","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

PNPT1 also known as polyribonucleotide nucleotidyltransferase 1 or mitochondrial RNA polymerase is an enzyme with a molecular weight of approximately 85 kDa. The protein is widely expressed in cellular mitochondria and cytoplasm where it performs its essential functions in RNA processing. It aids in the degradation and processing of mitochondrial RNA reflecting its significant role in mitochondrial function. The protein's activity relies heavily on its conserved domains that are necessary for effective RNA binding and hydrolysis.
Biological function summary

PNPT1 plays a critical role in maintaining mitochondrial gene expression and is a component of the RNA-degrading exosome complex. This complex is involved in the surveillance and breakdown of defective RNA molecules thereby ensuring the integrity and balance of the mitochondrial transcriptome. By participating in these processes PNPT1 helps to enhance the overall mitochondrial function which is vital for energy production and cell metabolism.

Pathways

PNPT1 significantly contributes to the mitochondrial RNA decay pathway and the broader RNA processing pathways related to mitochondrial maintenance. It interacts with other proteins such as polynucleotide phosphorylase domain-containing proteins which are involved in similar RNA processing functions. This integration highlights the coordinated network of proteins that cooperate to ensure proper mitochondrial RNA metabolism affecting both the quality and quantity of the RNA molecules available for translation.

Mutations or dysregulations in PNPT1 are linked to mitochondrial disorders such as autosomal recessive combined oxidative phosphorylation deficiency. These disorders often exhibit symptoms like muscle weakness developmental delays and other systemic issues due to compromised energy production. Additionally studies indicate a possible connection between PNPT1 dysfunction and neurodegenerative disorders where its interaction with proteins like TYMP (thymidine phosphorylase) can lead to mitochondrial dysfunction and subsequent disease progression.

Specifications

Form

Liquid

Additional notes

ab202628 was purified by conventional chromatography techniques.

General info

Function

RNA-binding protein implicated in numerous RNA metabolic processes. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'-to-5' direction. Mitochondrial intermembrane factor with RNA-processing exoribonulease activity. Component of the mitochondrial degradosome (mtEXO) complex, that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. Involved in the degradation of non-coding mitochondrial transcripts (MT-ncRNA) and tRNA-like molecules (PubMed : 29967381). Required for correct processing and polyadenylation of mitochondrial mRNAs. Plays a role as a cytoplasmic RNA import factor that mediates the translocation of small RNA components, like the 5S RNA, the RNA subunit of ribonuclease P and the mitochondrial RNA-processing (MRP) RNA, into the mitochondrial matrix. Plays a role in mitochondrial morphogenesis and respiration; regulates the expression of the electron transport chain (ETC) components at the mRNA and protein levels. In the cytoplasm, shows a 3'-to-5' exoribonuclease mediating mRNA degradation activity; degrades c-myc mRNA upon treatment with IFNB1/IFN-beta, resulting in a growth arrest in melanoma cells. Regulates the stability of specific mature miRNAs in melanoma cells; specifically and selectively degrades miR-221, preferentially. Also plays a role in RNA cell surveillance by cleaning up oxidized RNAs. Binds to the RNA subunit of ribonuclease P, MRP RNA and miR-221 microRNA.

Sequence similarities

Belongs to the polyribonucleotide nucleotidyltransferase family.

Subcellular localisation

Mitochondrion matrix

Product protocols

Target data

RNA-binding protein implicated in numerous RNA metabolic processes. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'-to-5' direction. Mitochondrial intermembrane factor with RNA-processing exoribonulease activity. Component of the mitochondrial degradosome (mtEXO) complex, that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. Involved in the degradation of non-coding mitochondrial transcripts (MT-ncRNA) and tRNA-like molecules (PubMed : 29967381). Required for correct processing and polyadenylation of mitochondrial mRNAs. Plays a role as a cytoplasmic RNA import factor that mediates the translocation of small RNA components, like the 5S RNA, the RNA subunit of ribonuclease P and the mitochondrial RNA-processing (MRP) RNA, into the mitochondrial matrix. Plays a role in mitochondrial morphogenesis and respiration; regulates the expression of the electron transport chain (ETC) components at the mRNA and protein levels. In the cytoplasm, shows a 3'-to-5' exoribonuclease mediating mRNA degradation activity; degrades c-myc mRNA upon treatment with IFNB1/IFN-beta, resulting in a growth arrest in melanoma cells. Regulates the stability of specific mature miRNAs in melanoma cells; specifically and selectively degrades miR-221, preferentially. Also plays a role in RNA cell surveillance by cleaning up oxidized RNAs. Binds to the RNA subunit of ribonuclease P, MRP RNA and miR-221 microRNA.
See full target information PNPT1

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

Nucleic acids research 48:7027-7040 PubMed32542340

2020

3'-Terminal 2'-O-methylation of lung cancer miR-21-5p enhances its stability and association with Argonaute 2.

Applications

Unspecified application

Species

Unspecified reactive species

Hongwei Liang,Zichen Jiao,Weiwei Rong,Shuang Qu,Zhicong Liao,Xinlei Sun,Yao Wei,Quan Zhao,Jun Wang,Yuan Liu,Xi Chen,Tao Wang,Chen-Yu Zhang,Ke Zen
View all publications

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