Recombinant Human Poly (PARN) Protein (His)

Name: Recombinant Human Poly (PARN) Protein (His)
Brand: Beta LifeScience
SKU: BLC-09672P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Poly (PARN) Protein (His) is produced by our Yeast expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	O95453
Target Symbol	PARN
Synonyms	DAN; Deadenylating nuclease; Deadenylation nuclease; PARN; PARN_HUMAN; Poly A specific ribonuclease; Poly(A) specific ribonuclease; Poly(A)-specific ribonuclease PARN; Polyadenylate specific ribonuclease; Polyadenylate-specific ribonuclease
Species	Homo sapiens (Human)
Expression System	Yeast
Tag	N-6His
Target Protein Sequence	MEIIRSNFKSNLHKVYQAIEEADFFAIDGEFSGISDGPSVSALTNGFDTPEERYQKLKKHSMDFLLFQFGLCTFKYDYTDSKYITKSFNFYVFPKPFNRSSPDVKFVCQSSSIDFLASQGFDFNKVFRNGIPYLNQEEERQLREQYDEKRSQANGAGALSYVSPNTSKCPVTIPEDQKKFIDQVVEKIEDLLQSEENKNLDLEPCTGFQRKLIYQTLSWKYPKGIHVETLETEKKERYIVISKVDEEERKRREQQKHAKEQEELNDAVGFSRVIHAIANSGKLVIGHNMLLDVMHTVHQFYCPLPADLSEFKEMTTCVFPRLLDTKLMASTQPFKDIINNTSLAELEKRLKETPFNPPKVESAEGFPSYDTASEQLHEAGYDAYITGLCFISMANYLGSFLSPPKIHVSARSKLIEPFFNKLFLMRVMDIPYLNLEGPDLQPKRDHVLHVTFPKEWKTSDLYQLFSAFGNIQISWIDDTSAFVSLSQPEQVKIAVNTSKYAESYRIQTYAEYMGRKQEEKQIKRKWTEDSWKEADSKRLNPQCIPYTLQNHYYRNNSFTAPSTVGKRNLSPSQEEAGLEDGVSGEISDTELEQTDSCAEPLSEGRKKAKKLKRMKKELSPAGSISKNSPATLFEVPDTW
Expression Range	1-639aa
Protein Length	Full Length
Mol. Weight	75.5kDa
Research Area	Transcription
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	3'-exoribonuclease that has a preference for poly(A) tails of mRNAs, thereby efficiently degrading poly(A) tails. Exonucleolytic degradation of the poly(A) tail is often the first step in the decay of eukaryotic mRNAs and is also used to silence certain maternal mRNAs translationally during oocyte maturation and early embryonic development. Interacts with both the 3'-end poly(A) tail and the 5'-end cap structure during degradation, the interaction with the cap structure being required for an efficient degradation of poly(A) tails. Involved in nonsense-mediated mRNA decay, a critical process of selective degradation of mRNAs that contain premature stop codons. Also involved in degradation of inherently unstable mRNAs that contain AU-rich elements (AREs) in their 3'-UTR, possibly via its interaction with KHSRP. Probably mediates the removal of poly(A) tails of AREs mRNAs, which constitutes the first step of destabilization. Also able to recognize and trim poly(A) tails of microRNAs such as MIR21 and H/ACA box snoRNAs (small nucleolar RNAs) leading to microRNAs degradation or snoRNA increased stability.
Subcellular Location	Nucleus. Cytoplasm. Nucleus, nucleolus. Note=Some nuclear fraction is nucleolar.
Protein Families	CAF1 family
Database References	HGNC: 8609 OMIM: 604212 KEGG: hsa:5073 STRING: 9606.ENSP00000387911 UniGene: Hs.253197
Associated Diseases	Dyskeratosis congenita, autosomal recessive, 6 (DKCB6); Pulmonary fibrosis, and/or bone marrow failure, telomere-related, 4 (PFBMFT4)
Tissue Specificity	Ubiquitous.

Gene Functions References

Results show that PARN deadenylase activity is regulated by the phosphorylated form of Nucleolin. PMID: 29168431
Studies suggest that the effects of poly(A)-specific ribonuclease (PARN) mutations on telomere length are likely indirect and may lead to telomere shortening that less perfectly cosegregates with heterozygous mutations. PMID: 26908837
Pulmonary fibrosis patients with mutations in telomerase reverse transcriptase, telomerase RNA component, regulator of telomere elongation helicase 1 and poly(A)-specific ribonuclease were identified and clinical data were analysed. Genetic mutations in telomere related genes lead to a variety of interstitial lung disease diagnoses that are universally progressive. PMID: 27540018
PARN polyadenylates the 3' end of telomerase RNA component (known as TERC or hTR), which serves as the template for telomerase reverse transcriptase-mediated telomere replication. PMID: 28414520
PARN is a new component of the ribosome biogenesis machinery in human cells. PMID: 28402503
provide evidence that PARN can also deadenylate the U6 and RMRP RNAs without affecting their levels PMID: 28760775
poly(A)-specific ribonuclease (PARN) participates in steps leading to 18S pre-rRNA maturation in human cells PMID: 27899605
we found a polyadenylation-dependent 3' end maturation pathway for the human telomerase RNA that relies on the nuclear poly(A)-binding protein PABPN1 and the poly(A)-specific RNase PARN. PMID: 26628368
PARN increased telomerase RNA component levels by deadenylating telomerase RNA component, thereby limiting its degradation by EXOSC10. PMID: 26950371
Large monoallelic mutations of PARN can cause developmental/mental illness. Biallelic PARN mutations cause severe bone marrow failure and central hypomyelination. PMID: 26342108
results highlight the clinical significance of PARN and NOC on the survival in SCC diagnosed patients. PMID: 26541675
Mutations in the PARN gene cause dyskeratosis congenital. PMID: 26482878
The results indicate that the cellular level of miR-122 is determined by the balance between the opposing effects of GLD-2 and PARN/CUGBP1 on the metabolism of its 3'-terminus. PMID: 26130707
3 families with dyskeratosis congenita had key domain mutations in PARN shortening telomeres, reducing deadenylation, and downregulating TERC, DKC1, RTEL1, and TERF1. PMID: 25893599
PARN and RTEL1 mutation carriers had shortened leukocyte telomere lengths. PMID: 25848748
poly(A)-specific ribonuclease (PARN) was upregulated in gastric tumor tissues and gastric cancer cell lines MKN28 and AGS. PMID: 25499764
Both R3H and RRM domains were essential for the high affinity of long poly(A) substrate. PMID: 23388391
poly(A) polymerase Gld2, deadenylase PARN, and translation inhibitory factor neuroguidin (Ngd) are components of a dendritic CPEB-associated polyadenylation apparatus PMID: 22727665
The atomic force microscopy images of single PARN molecules reveal compact ellipsoidal dimers (10.9 x 7.6 x 4.6nm). PMID: 21741754
PARN harbors specificity for adenosine recognition in its active site and that the nucleotides surrounding the scissile bond are critical for adenosine recognition. PMID: 19901024
residues of human PARN, Asp(28), Glu(30), Asp(292), and Asp(382), are essential for catalysis but are not required for stabilization of the PARN x RNA substrate complex. PMID: 11742007
Results show that tristetraprolin can promote the deadenylation of AU-rich element (ARE)-containing, polyadenylated substrates by poly(A) RNase. PMID: 12748283
study of binding and coordination of divalent metal ions in the active site of PARN PMID: 15358788
The crystal structure of C-terminal truncated human PARN determined in two states (free and RNA-bound forms) reveals that PARN is folded into two domains, an R3H domain and a nuclease domain PMID: 16281054
CUG-BP binds specifically to both of these RNAs and stimulates poly(A) shortening by PARN. Moreover, CUG-BP interacts with PARN in extracts by coimmunoprecipitation, and this interaction can be recapitulated using recombinant proteins PMID: 16601207
The entire RNA-recognition motif (RRM) domain not only contributes to the substrate binding and efficient catalysis of PARN, but also stabilizes the overall structures of the protein. PMID: 17391638
REsults describe the crystal structure of the poly(A)-specific ribonuclease (PARN)-RRM domain with a bound 7-methylguanosine triphosphate nucleotide, revealing a novel binding mode for the m(7)G cap. PMID: 18694759
PARN is an allosteric enzyme, and potassium ions and the cap analogue are effectors with binding sites located at the RRM domain. PMID: 19103158
Xenopus oocytes contain cytoplasmic (p62) and nuclear (p74) isoforms of PARN. p62 is proteolytically derived from p74. Both isoforms are expressed throughout oogenesis and early development. PMID: 11424938
The m7GpppG cap has multiple effects on PARN activity. In cis, the 5'cap stimulates deadenylation by increasing PARN processivity. In trans, low concentrations of cap stimulate PARN activity whereas high concentrations inhibit deadenylation. PMID: 11359775
PARN is a poly(A)-specific member of the RNase D family of 3' exoribonucleases. It is distributed between the nucleus and the cytoplasm and is not stably associated with ribosomes. Xenopus PARN catalyzes deadenylation during oocyte maturation. PMID: 9736620
Deadenylation by the mammalian and amphibian poly(A)-specific exoribonuclease, PARN, is stimulated by the presence of an m(7)-guanosine cap on substrate RNAs. PARN exhibits intrinsic cap-binding activity. PMID: 10698948
PARN binds to the 5' cap on substrate mRNAs. Cap-binding is stimulated by a poly(A) tail and competed by eIF4E. Cap-PARN interactions integrate regulated mRNA stability and translation. PMID: 10882133

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.