Rabbit UBE2L3 Polyclonal Antibody | anti-UBE2L3 antibody
UBE2L3 Antibody (C-term)
IHC-P: 1:50-100
Western Blot (WB)
(All lanes : Anti-UBE2L3 Antibody (C137) at 1:1000 dilutionLane 1: mouse testis lysatesLane 2: rat testis lysatesLane 3: human testis lysatesLane 4: U87-MG whole cell lysatesLane 5: K562 whole cell lysates Lane 6: PC-12 whole cell lysates Lane 7: NIH/3T3 whole cell lysatesLysates/proteins at 20 ug per lane.SecondaryGoat Anti-Rabbit IgG, (H+L),Peroxidase conjugated at 1/10000 dilutionPredicted band size : 18 kDaBlocking/Dilution buffer: 5% NFDM/TBST.)
Immunohistochemistry (IHC)-Paraffin
(Formalin-fixed and paraffin-embedded human cancer tissue reacted with the primary antibody, which was peroxidase-conjugated to the secondary antibody, followed by DAB staining. This data demonstrates the use of this antibody for immunohistochemistry; clinical relevance has not been evaluated. BC = breast carcinoma; HC = hepatocarcinoma.)
Background: The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). UBE2L3 is a member of the E2 ubiquitin-conjugating enzyme family. This enzyme is demonstrated to participate in the ubiquitination of p53, c-Fos, and the NF-kB precursor p105 in vitro.
NCBI and Uniprot Product Information
NCBI Description
The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. This enzyme is demonstrated to participate in the ubiquitination of p53, c-Fos, and the NF-kB precursor p105 in vitro. Several alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Sep 2009]
Uniprot Description
UBE2L3: Ubiquitin-conjugating enzyme E2 that specifically acts with HECT-type and RBR family E3 ubiquitin-protein ligases. Does not function with most RING-containing E3 ubiquitin-protein ligases because it lacks intrinsic E3-independent reactivity with lysine: in contrast, it has activity with the RBR family E3 enzymes, such as PARK2 and ARIH1, that function like function like RING-HECT hybrids. Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'-linked polyubiquitination. Involved in the selective degradation of short-lived and abnormal proteins. Down- regulated during the S-phase it is involved in progression through the cell cycle. Regulates nuclear hormone receptors transcriptional activity. May play a role in myelopoiesis. Interacts with PARK2; involved in ubiquitination and degradation of misfolded proteins. Interacts with UBE3A; used by the papilloma virus HPV-16 E6 protein to ubiquitinate p53/TP53. Interacts with CCNB1IP1, CBL, ZAP70, RNF19A, RNF19B and RNF144B. Interacts with ARIH1. Interacts with ARIH2 (via RING-type 1). Interacts with NCOA1; they functionally interact to regulate progesterone receptor transcriptional activity. May interact with NR3C1. Ubiquitous, with highest expression in testis. Belongs to the ubiquitin-conjugating enzyme family.
Protein type: Nuclear receptor co-regulator; Ubiquitin conjugating system; EC 6.3.2.19; Ubiquitin ligase; Ligase
Chromosomal Location of Human Ortholog: 22q11.21
Cellular Component: cytoplasm; nucleus; ubiquitin ligase complex
Molecular Function: protein binding; enzyme binding; ubiquitin protein ligase binding; transcription coactivator activity; ubiquitin-protein ligase activity; ATP binding; ligase activity
Biological Process: ubiquitin-dependent protein catabolic process; cell proliferation; protein polyubiquitination; regulation of transcription, DNA-dependent; transcription, DNA-dependent; positive regulation of protein ubiquitination; positive regulation of ubiquitin-protein ligase activity; protein modification process; protein ubiquitination