TRIM27 Protein (AA 1-513) (Strep Tag)
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- Antigène Voir toutes TRIM27 Protéines
- TRIM27 (Tripartite Motif Containing 27 (TRIM27))
- Type de proteíne
- Recombinant
- Attributs du protein
- AA 1-513
- Origine
- Souris
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Source
- Tobacco (Nicotiana tabacum)
- Purification/Conjugué
- Cette TRIM27 protéine est marqué à la Strep Tag.
- Application
- Western Blotting (WB), ELISA, SDS-PAGE (SDS)
- Séquence
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MASGSVAECL QQETTCPVCL QYFVEPMMLD CGHNICCACL ARCWGAAETN VSCPQCRETF PQRHMRPNRH LANVTQLVKQ LRTERPSGPG GEMGVCEKHR EPLKLYCEQD QMPICVVCDR SREHRGHSVL PLEEAVEGFK EQIQNRLDHL RRVKDLKKRR RAQGEQARAE LLSLTQMERE KIVWEFEQLY HSLKEHEYRL LARLEELDLA IYNSINGAIT QFSCNISHLS GLIAQLEEKQ QQPTRELLQD IGDTLSRAER IRIPEPWITP PDLQEKIHIF AQKCLFLTES LKQFTEKMQS DMEKIQELRE AQLYSVDVTL DPDTAYPSLI LSDNLRQVRY SYLQQDLPDN PERFNLFPCV LGSPCFIAGR HYWEVEVGDK AKWTIGVCED SVCRKGGVTS APQNGFWAVS LWYGKEYWAL TSPMTALPLR TPLQRVGIFL DYDAGEVSFY NVTERCHTFT FSHATFCGPV RPYFSLSYSG GKSAAPLIIC PMSGIDGFSG HVGNHGHSME TSP
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 by multi-step, protein-specific process to ensure correct folding and modification.
- 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 will ensure that you receive a correctly folded 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 in several dilutions and is measured against its specific reference buffer.
- We use the Expasy's protparam tool to determine the absorption coefficient of each protein.
- Purification
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Two step purification of proteins expressed in Almost Living Cell-Free Expression System (ALiCE®):
- In a first purification step, the protein is purified from the cleared cell lysate using StrepTag capture material. Eluate fractions are analyzed by SDS-PAGE.
- Protein containing fractions of the best purification are subjected to second purification step through size exclusion chromatography. Eluate fractions are analyzed by SDS-PAGE and Western blot.
- Pureté
- ≥ 80 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot.
- niveau d'endotoxine
- Low Endotoxin less than 1 EU/mg (< 0.1 ng/mg)
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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
- TRIM27 (Tripartite Motif Containing 27 (TRIM27))
- Autre désignation
- Trim27 (TRIM27 Produits)
- Synonymes
- RFP Protein, RNF76 Protein, AW538890 Protein, Gm19403 Protein, Rfp Protein, TRIM27 Protein, Rfp1 Protein, tripartite motif containing 27 Protein, tripartite motif-containing 27 Protein, TRIM27 Protein, Trim27 Protein
- Sujet
- Zinc finger protein RFP (EC 2.3.2.27) (Ret finger protein) (Tripartite motif-containing protein 27),FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination of various substrates and thereby plays a role in diffent processes including proliferation, innate immunity, apoptosis, immune response or autophagy (PubMed:24144979). Ubiquitinates PIK3C2B and inhibits its activity by mediating the formation of 'Lys-48'-linked polyubiquitin chains, the function inhibits CD4 T-cell activation (By similarity). Acts as a regulator of retrograde transport: together with MAGEL2, mediates the formation of 'Lys-63'-linked polyubiquitin chains at 'Lys-220' of WASHC1, leading to promote endosomal F-actin assembly (By similarity). Has a transcriptional repressor activity by cooperating with EPC1 (By similarity). Induces apoptosis by activating Jun N-terminal kinase and p38 kinase and also increases caspase-3-like activity independently of mitochondrial events (By similarity). May function in male germ cell development (By similarity). Has DNA-binding activity and preferentially bound to double-stranded DNA (By similarity). Forms a complex with and ubiquitinates the ubiquitin-specific protease USP7, which in turn deubiquitinates RIPK1 resulting in the positive regulation of TNF-alpha-induced apoptosis (PubMed:24144979). In addition, acts with USP7 or PTPN11 as an inhibitor of the antiviral signaling pathway by promoting kinase TBK1 ubiquitination and degradation (By similarity). Acts as a negative regulator of NOD2 signaling by mediating ubiquitination of NOD2, promoting its degradation by the proteasome (By similarity). Alternatively, facilitates mitophagy via TBK1 activation (By similarity). Negatively regulates autophagy flux under basal conditions by directly polyubiquitinating ULK1 (By similarity). During starvation-induced autophagy, catalyzes non-degradative ubiquitination of the kinase STK38L promoting its activation and phosphorylation of ULK1 leading to its ubiquitination and degradation to restrain the amplitude and duration of autophagy (By similarity). {ECO:0000250|UniProtKB:P14373, ECO:0000269|PubMed:24144979}.
- Poids moléculaire
- 58.5 kDa
- UniProt
- Q62158
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