PARN Protein (AA 1-624) (Strep Tag)
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- Antigène Voir toutes PARN Protéines
- PARN (Poly A Specific Ribonuclease (PARN))
- Type de proteíne
- Recombinant
- Attributs du protein
- AA 1-624
- Origine
- Souris
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Source
- Tobacco (Nicotiana tabacum)
- Purification/Conjugué
- Cette PARN protéine est marqué à la Strep Tag.
- Application
- SDS-PAGE (SDS), Western Blotting (WB), ELISA
- Séquence
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MEIIRSNFKI NLHKVYQAIE EADFFAIDGE FSGISDGPSV TALTSGFDTP EERYQKLKKH SMDFLLFQFG LCAFKYDHTD SKHVTKSFNF YVFPKPFSRS SPDVKFVCQS SSIDFLASQG FDFNKVFCSG IPYLNQEEER QLREQFDEKR SQANGAGALA KCPVTIPEDQ KKFIDQVIEK IEDFLQSEEK RSLELDPCTG FQRKLIYQTL SWKYPKGIHV ETLETDKKER HIVISKVDEE ERKRREQEKY TKEQEELNDA VGFSRVIHAI ANSGKLVVGH NMLLDVMHTI HQFYCPLPAD LNEFKEMAIC VFPRLLDTKL MASTQPFKDI INNTSLAELE KRLKETPFDP PKVESAEGFP SYDTASEQLH EAGYDAYITG LCFISMANYL GSLLSPPKMC VSARSKLIEP FFNKLFLMRV MDIPYLNLEG PDLQPKRDHV LHVTFPKEWK TSDLYQLFSA FGNIQISWID DTSAFVSLSQ PEQVQIAVNT SKYAESYRIQ TYAEYVGKKQ EGKQVKRKWT EDSWKEVDRK RPHMQGPCYH SNSFTAAGVL GKRTLSPDPR EAALEDRESE EVSDSELEQT DSCTDPLPEG RKKSKKLKRM KKELSLAGSV SDSPAVLFEV PDTW
Sequence without tag. The proposed Strep-Tag is based on experience s with the expression system, a different complexity of the protein could make another tag necessary. In case you have a special request, please contact us. - Attributs du produit
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Key Benefits:
- Made in Germany - from design to production - by highly experienced protein experts.
- Protein expressed with ALiCE® and purified in one-step affinity chromatography
- These proteins are normally active (enzymatically functional) as our customers have reported (not tested by us and not guaranteed).
- State-of-the-art algorithm used for plasmid design (Gene synthesis).
This protein is a made-to-order protein and will be made for the first time for your order. Our experts in the lab try to ensure that you receive soluble protein.
The big advantage of ordering our made-to-order proteins in comparison to ordering custom made proteins from other companies is that there is no financial obligation in case the protein cannot be expressed or purified.
Expression System:- ALiCE®, our Almost Living Cell-Free Expression System is based on a lysate obtained from Nicotiana tabacum c.v.. This contains all the protein expression machinery needed to produce even the most difficult-to-express proteins, including those that require post-translational modifications.
- During lysate production, the cell wall and other cellular components that are not required for protein production are removed, leaving only the protein production machinery and the mitochondria to drive the reaction. During our lysate completion steps, the additional components needed for protein production (amino acids, cofactors, etc.) are added to produce something that functions like a cell, but without the constraints of a living system - all that's needed is the DNA that codes for the desired protein!
Concentration:- The concentration of our recombinant proteins is measured using the absorbance at 280nm.
- The protein's absorbance will be measured against its specific reference buffer.
- We use the Expasy's ProtParam tool to determine the absorption coefficient of each protein.
- Purification
- One-step Strep-tag purification of proteins expressed in Almost Living Cell-Free Expression System (AliCE®).
- Pureté
- > 80 % as determined by SDS PAGE, Western Blot and analytical SEC (HPLC).
- Top Product
- Discover our top product PARN Protéine
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- Indications d'application
- In addition to the applications listed above we expect the protein to work for functional studies as well. As the protein has not been tested for functional studies yet we cannot offer a guarantee though.
- Commentaires
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ALiCE®, our Almost Living Cell-Free Expression System is based on a lysate obtained from Nicotiana tabacum c.v.. This contains all the protein expression machinery needed to produce even the most difficult-to-express proteins, including those that require post-translational modifications.
During lysate production, the cell wall and other cellular components that are not required for protein production are removed, leaving only the protein production machinery and the mitochondria to drive the reaction. During our lysate completion steps, the additional components needed for protein production (amino acids, cofactors, etc.) are added to produce something that functions like a cell, but without the constraints of a living system - all that's needed is the DNA that codes for the desired protein! - Restrictions
- For Research Use only
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- Format
- Liquid
- Buffer
- The buffer composition is at the discretion of the manufacturer. If you have a special request, please contact us.
- Conseil sur la manipulation
- Avoid repeated freeze-thaw cycles.
- Stock
- -80 °C
- Stockage commentaire
- Store at -80°C.
- Date de péremption
- Unlimited (if stored properly)
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- Antigène
- PARN (Poly A Specific Ribonuclease (PARN))
- Autre désignation
- Parn (PARN Produits)
- Synonymes
- parn-A Protein, xparn Protein, DAN Protein, RGD1565449 Protein, zgc:56067 Protein, 1200003I18Rik Protein, poly(A)-specific ribonuclease L homeolog Protein, poly(A)-specific ribonuclease Protein, poly(A)-specific ribonuclease (deadenylation nuclease) Protein, parn.L Protein, PARN Protein, Parn Protein, parn Protein
- Sujet
- Poly(A)-specific ribonuclease PARN (EC 3.1.13.4) (Polyadenylate-specific ribonuclease),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 (By similarity). Also able to recognize poly(A) tails of microRNAs such as MIR21 and H/ACA box snoRNAs (small nucleolar RNAs) leading to leading to microRNAs degradation or snoRNA increased stability (By similarity). {ECO:0000250|UniProtKB:O95453}.
- Poids moléculaire
- 71.6 kDa
- UniProt
- Q8VDG3
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