TRIM27 Protein (AA 1-513) (His tag)
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- Target See all TRIM27 Proteins
- TRIM27 (Tripartite Motif Containing 27 (TRIM27))
- Protein Type
- Recombinant
- Protein Characteristics
- AA 1-513
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Origin
- Human
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Source
- HEK-293 Cells
- Purification tag / Conjugate
- This TRIM27 protein is labelled with His tag.
- Purpose
- Predefined custom protein recombinant TRIM27 Protein expressed in mammalian cells.
- Sequence
- MASGSVAECL QQETTCPVCL QYFAEPMMLD CGHNICCACL ARCWGTAETN VSCPQCRETF PQRHMRPNRH LANVTQLVKQ LRTERPSGPG GEMGVCEKHR EPLKLYCEED QMPICVVCDR SREHRGHSVL PLEEAVEGFK EQIQNQLDHL KRVKDLKKRR RAQGEQARAE LLSLTQMERE KIVWEFEQLY HSLKEHEYRL LARLEELDLA IYNSINGAIT QFSCNISHLS SLIAQLEEKQ 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 with the expression system. Our team may suggest an additional tag depending on the complexity of the protein. If you have a special request, please contact us.
- Specificity
- If you are looking for a specific domain and are interested in a partial protein or a different isoform, please contact us regarding an individual offer.
- Characteristics
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Key Benefits:
- Predefined custom protein - from design to production - by highly experienced protein experts.
- Protein expressed in mammalian cells and purified in one-step affinity chromatography
- The optimized expression system ensures reliability for intracellular, secreted and transmembrane proteins.
- State-of-the-art algorithm used for plasmid design (Gene synthesis).
If you are not interested in a full length protein, please contact us for individual protein fragments.
The big advantage of ordering our predefined custom 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. - Purity
- > 90 % as determined by Bis-Tris PAGE, anti-tag ELISA, Western Blot and analytical SEC (HPLC)
- Grade
- custom-made
- Top Product
- Discover our top product TRIM27 Protein
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Want other Options for this Protein ?
!Discover Our Catalog and Custom Protein Service Options!ProductExpression SystemConjugateOriginPriceExpression System Escherichia coli (E. coli)Conjugate His tagOrigin HumanPrice $663.94Expression System Escherichia coli (E. coli)Conjugate His tagOrigin HumanPrice $385.20Your project requires further customization? Contact us and discover our custom protein solutions
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- Application Notes
- We expect the protein to work for functional studies. As the protein has not been tested for functional studies yet we cannot offer a guarantee though.
- Restrictions
- For Research Use only
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- Format
- Liquid
- Buffer
- The buffer composition is at the discretion of the manufacturer.
- Handling Advice
- Avoid repeated freeze-thaw cycles.
- Storage
- -80 °C
- Storage Comment
- Store at -80°C.
- Expiry Date
- 12 months
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- Target
- TRIM27 (Tripartite Motif Containing 27 (TRIM27))
- Alternative Name
- TRIM27 (TRIM27 Products)
- Background
- Zinc finger protein RFP (EC 2.3.2.27) (RING finger protein 76) (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:22829933, PubMed:24144979, PubMed:29688809, PubMed:36111389). Ubiquitinates PIK3C2B and inhibits its activity by mediating the formation of 'Lys-48'-linked polyubiquitin chains, the function inhibits CD4 T-cell activation. 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 (PubMed:23452853). Has a transcriptional repressor activity by cooperating with EPC1. Induces apoptosis by activating Jun N-terminal kinase and p38 kinase and also increases caspase-3-like activity independently of mitochondrial events. May function in male germ cell development. Has DNA-binding activity and preferentially bound to double-stranded DNA. 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 (PubMed:26358190, PubMed:29688809). Acts as a negative regulator of NOD2 signaling by mediating ubiquitination of NOD2, promoting its degradation by the proteasome (PubMed:22829933). Alternatively, facilitates mitophagy via stabilization of active TBK1 (PubMed:36111389). Negatively regulates autophagy flux under basal conditions by directly polyubiquitinating ULK1 (PubMed:35670107). 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 (PubMed:35670107). {ECO:0000269|PubMed:10976108, ECO:0000269|PubMed:12807881, ECO:0000269|PubMed:22128329, ECO:0000269|PubMed:22829933, ECO:0000269|PubMed:23452853, ECO:0000269|PubMed:24144979, ECO:0000269|PubMed:26358190, ECO:0000269|PubMed:29688809, ECO:0000269|PubMed:35670107, ECO:0000269|PubMed:36111389}., FUNCTION: (Microbial infection) Positively regulates hepatitis C virus replication by suppressing type I IFN response during infection. {ECO:0000269|PubMed:29688809}.
- Molecular Weight
- 58.5 kDa
- UniProt
- P14373
- AlphaFold
- P14373
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