TRIM21
Spezies: Human
Wirt: Tobacco (Nicotiana tabacum)
Recombinant
>80 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot.
SDS, WB, ELISA
TRIM21
Spezies: Human
Wirt: HEK-293 Cells
Recombinant
> 80 % as determined by SDS-PAGE and Coomassie blue staining
AbP, STD
Applikationshinweise
Optimal working dilution should be determined by the investigator.
Beschränkungen
Nur für Forschungszwecke einsetzbar
Format
Liquid
Konzentration
0.1-2 mg/mL
Buffer
20 mM Tris-HCl based buffer, pH 8.0
Lagerung
-80 °C,4 °C,-20 °C
Informationen zur Lagerung
Store at -20°C, for extended storage, conserve at -20°C or -80°C. Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
E3 ubiquitin-protein ligase whose activity is dependent on E2 enzymes, UBE2D1, UBE2D2, UBE2E1 and UBE2E2. Forms a ubiquitin ligase complex in cooperation with the E2 UBE2D2 that is used not only for the ubiquitination of USP4 and IKBKB but also for its self-ubiquitination. Component of cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes such as SCF(SKP2)-like complexes. A TRIM21-containing SCF(SKP2)-like complex is shown to mediate ubiquitination of CDKN1B ('Thr-187' phosphorylated-form), thereby promoting its degradation by the proteasome. Monoubiquitinates IKBKB that will negatively regulates Tax-induced NF-kappa-B signaling. Negatively regulates IFN-beta production post-pathogen recognition by polyubiquitin-mediated degradation of IRF3. Mediates the ubiquitin-mediated proteasomal degradation of IgG1 heavy chain, which is linked to the VCP-mediated ER-associated degradation (ERAD) pathway. Promotes IRF8 ubiquitination, which enhanced the ability of IRF8 to stimulate cytokine genes transcription in macrophages. Plays a role in the regulation of the cell cycle progression. Enhances the decapping activity of DCP2. Exists as a ribonucleoprotein particle present in all mammalian cells studied and composed of a single polypeptide and one of four small RNA molecules. At least two isoforms are present in nucleated and red blood cells, and tissue specific differences in RO/SSA proteins have been identified. The common feature of these proteins is their ability to bind HY RNAs.2.