Human TRIM27 protein (Recombinant) (N-His) (STJP007612)
SPECIFICATIONS
HostE.coli
ImmunogenHomo sapiens (Human)
General Information
| Short Description | Recombinant-Human TRIM27-N-His protein was developed from e.coli for the region N-His. For use in research applications. |
| Applications | ELISA/Immunogen/SDS-PAGE/WB |
| Host | E.coli |
| Note | STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS. |
Product Properties
| Dilution Range | Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details. |
| Formulation | Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol. |
| Storage Instruction | Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at-20 to-80°C for twelve months from the date of receipt. |
Target Information
| Gene Symbol | TRIM27 |
| Gene ID | 5987 |
| Uniprot ID | TRI27_HUMAN |
| Immunogen | Homo sapiens (Human) |
| Immunogen Region | Ser315-Pro513 |
Additional Info
| 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. 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. 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. In addition, acts with USP7 or PTPN11 as an inhibitor of the antiviral signaling pathway by promoting kinase TBK1 ubiquitination and degradation. Acts as a negative regulator of NOD2 signaling by mediating ubiquitination of NOD2, promoting its degradation by the proteasome. Alternatively, facilitates mitophagy via stabilization of active TBK1. Negatively regulates autophagy flux under basal conditions by directly polyubiquitinating ULK1. 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. (Microbial infection) Positively regulates hepatitis C virus replication by suppressing type I IFN response during infection. |
| Protein Name | Zinc Finger Protein RfpRing Finger Protein 76Ret Finger ProteinTripartite Motif-Containing Protein 27 |
| Database Links | Reactome: R-HSA-3232142Reactome: R-HSA-8948751Reactome: R-HSA-9635465 |
| Cellular Localisation | NucleusCytoplasmPml BodyEarly EndosomeMitochondrionNuclear Or Cytoplasmic Depending On The Cell TypeColocalized With Pml And Eif3s6 In Nuclear BodiesRecruited To Retromer-Containing Endosomes Via Interaction With Magel2Co-Localizes With P62/Sqstm1 And Tbk1 In Cytoplasmic Structures That Are Closely Associated With The Mitochondria |
| Alternative Protein Names | Zinc Finger Protein Rfp proteinRing Finger Protein 76 proteinRet Finger Protein proteinTripartite Motif-Containing Protein 27 proteinTRIM27 proteinRFP proteinRNF76 protein |
Information sourced from Uniprot.org