- CITATIONS: 1
|Application ||FC, WB, E|
|Other Accession||D4ABP9, Q9DC63, A6H7H7|
|Calculated MW||54561 Da|
|Antigen Region||395-422 aa|
|Other Names||F-box only protein 3, FBXO3, FBX3|
|Target/Specificity||This FBXO3 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 395-422 amino acids from the C-terminal region of human FBXO3.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||FBXO3 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Substrate recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. Mediates the ubiquitination of HIPK2 and probably that of EP300, leading to rapid degradation by the proteasome. In the presence of PML, HIPK2 ubiquitination still occurs, but degradation is prevented. PML, HIPK2 and FBXO3 may act synergically to activate p53/TP53-dependent transactivation.|
|Cellular Location||Nucleus. Note=Colocalizes with PML at the peripheries of nuclear bodies|
Provided below are standard protocols that you may find useful for product applications.
FBXO3 encodes a member of the F-box protein family which is characterized by an approximately 40 amino acid motif, the F-box. The F-box proteins constitute one of the four subunits of the ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box), which function in phosphorylation-dependent ubiquitination. The F-box proteins are divided into 3 classes: Fbws containing WD-40 domains, Fbls containing leucine-rich repeats, and Fbxs containing either different protein-protein interaction modules or no recognizable motifs.
Shima,Y., et.al., Mol. Cell. Biol. 28 (23), 7126-7138 (2008)
Ilyin,G.P., et.al., Genomics 67 (1), 40-47 (2000)
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