GSPT2 Protein (AA 1-628) (Strep Tag)
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- Target See all GSPT2 Proteins
- GSPT2 (G1 To S Phase Transition 2 (GSPT2))
- Protein Type
- Recombinant
- Protein Characteristics
- AA 1-628
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Origin
- Human
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Source
- Tobacco (Nicotiana tabacum)
- Purification tag / Conjugate
- This GSPT2 protein is labelled with Strep Tag.
- Application
- ELISA, Western Blotting (WB), SDS-PAGE (SDS)
- Sequence
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MDSGSSSSDS APDCWDQVDM ESPGSAPSGD GVSSAVAEAQ REPLSSAFSR KLNVNAKPFV PNVHAAEFVP SFLRGPTQPP TLPAGSGSND ETCTGAGYPQ GKRMGRGAPV EPSREEPLVS LEGSNSAVTM ELSEPVVENG EVEMALEESW EHSKEVSEAE PGGGSSGDSG PPEESGQEMM EEKEEIRKSK SVIVPSGAPK KEHVNVVFIG HVDAGKSTIG GQIMFLTGMV DKRTLEKYER EAKEKNRETW YLSWALDTNQ EERDKGKTVE VGRAYFETER KHFTILDAPG HKSFVPNMIG GASQADLAVL VISARKGEFE TGFEKGGQTR EHAMLAKTAG VKHLIVLINK MDDPTVNWSI ERYEECKEKL VPFLKKVGFS PKKDIHFMPC SGLTGANIKE QSDFCPWYTG LPFIPYLDNL PNFNRSIDGP IRLPIVDKYK DMGTVVLGKL ESGSIFKGQQ LVMMPNKHNV EVLGILSDDT ETDFVAPGEN LKIRLKGIEE EEILPGFILC DPSNLCHSGR TFDVQIVIIE HKSIICPGYN AVLHIHTCIE EVEITALISL VDKKSGEKSK TRPRFVKQDQ VCIARLRTAG TICLETFKDF PQMGRFTLRD EGKTIAIGKV LKLVPEKD
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. - Characteristics
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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®).
- Purity
- > 80 % as determined by SDS PAGE, Western Blot and analytical SEC (HPLC).
- Top Product
- Discover our top product GSPT2 Protein
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- Application Notes
- 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.
- Comment
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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.
- Handling Advice
- Avoid repeated freeze-thaw cycles.
- Storage
- -80 °C
- Storage Comment
- Store at -80°C.
- Expiry Date
- Unlimited (if stored properly)
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- Target
- GSPT2 (G1 To S Phase Transition 2 (GSPT2))
- Alternative Name
- GSPT2 (GSPT2 Products)
- Synonyms
- ERF3B Protein, GST2 Protein, G1 to S phase transition 2 Protein, GSPT2 Protein, Gspt2 Protein
- Background
- Eukaryotic peptide chain release factor GTP-binding subunit ERF3B (Eukaryotic peptide chain release factor subunit 3b) (eRF3b) (EC 3.6.5.-) (G1 to S phase transition protein 2 homolog),FUNCTION: GTPase component of the eRF1-eRF3-GTP ternary complex, a ternary complex that mediates translation termination in response to the termination codons UAA, UAG and UGA (PubMed:15987998, PubMed:11524954, PubMed:17562865). GSPT2/ERF3B mediates ETF1/ERF1 delivery to stop codons: The eRF1-eRF3-GTP complex binds to a stop codon in the ribosomal A-site (PubMed:15987998). GTP hydrolysis by GSPT2/ERF3B induces a conformational change that leads to its dissociation, permitting ETF1/ERF1 to accommodate fully in the A-site (PubMed:15987998). Component of the transient SURF complex which recruits UPF1 to stalled ribosomes in the context of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons (PubMed:19417104). {ECO:0000269|PubMed:11524954, ECO:0000269|PubMed:15987998, ECO:0000269|PubMed:17562865, ECO:0000269|PubMed:19417104}.
- Molecular Weight
- 68.9 kDa
- UniProt
- Q8IYD1
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