The U box is a domain of approximately 70 amino acids that is present in proteins from yeast to humans. The prototype U box protein, yeast Ufd2, was identified as a ubiquitin chain assembly factor that cooperates with a ubiquitin-activating enzymes (E1, E2), and a ubiquitin-protein ligase (E3) to catalyze ubiquitin chain formation on artificial substrates. UFD1L is an essential component of the ubiquitin-dependent proteolytic pathway which degrades ubiquitin fusion proteins. The ternary complex containing UFD1L, VCP and NPLOC4 binds ubiquitinated proteins and is necessary for the export of misfolded proteins from the ER to the cytoplasm, where they are degraded by the proteosome. In mammalian cells the membrane bound ubiquitin ligase gp75 promotes degradation of sterol regulated degradation of HMG CoA reductase and misfolded endoplasmic reticulum proteins. The ubiquitin fusion degradation 1 like (UFD1L) protein plays a critical role in ER associated degradation in association with Npl4 and VCP proteins. Interaction of VCP-UFD1L-Npl4 complex recognizes polyubiquitin chains and transfers the ubiquitinated proteins to proteosomes. The UFD1L also directly interacts with membrane bound gp75 as a cofactor and accelerate the ubiquitination and degradation of reductase and eventually promotes receptor mediated uptake of low density lipoproteins, thus plays an important role in cholesterol metabolism (1). It is shown that UFD1L-Npl4 complex is a negative regulator of retrotranslocation of A1 chain of the cholera toxin (CT) to the cytosol across the ER, delaying the retro-translocation of ERAD substrates independently of its association with VCP (2). The NPLOC4-UFD1L-VCP complex regulates spindle disassembly at the end of mitosis and is necessary for the formation of a closed nuclear envelope. It may be involved in the development of some ectoderm-derived structures.
UFD1L gene is located on chromosome22q1.2 and is expressed during embryogenesis in the eyes and in the linear ear primordial. UFD1L gene is expressed in patients with DiGeorge (DGS) and velo-cardial facial (VCF) syndrome which suggest that proteolytic pathways that recognize ubiquitin fusion proteins for degrradtioin is conserved in vertebrates and UFD1L gene hemizygosity is the cause of some of the CATCH-22 (acronym for cardiac defects, abnormal facies, thymic hypoplasia, cleft palate and hypocalcimea) associated developmental defects in DGS and VCSF syndromes (3). UFD1L is expressed in adult heart, skeletal muscle and pancreas, and in fetal liver and kidney. UFD1L is a 307 amino acid protein apparent MW is 38kDa.
FabGennix has made and characterized a rabbit antibody against UFD1Lprotein. The UFD1L antibodies are affinity purified over immobilized affinity matrix and stabilized in the presence of preservatives for long-term storage. UFD1L-FITC conjugated antibody was further purified to remove un-conjugated fluorophore was stabilized for long-term storage. FabGennix will conjugate this antibody to secondary enzymes (alkaline phosphatase or horseradish peroxidase) and other fluorophores upon request at a nominal charge. FabGennix Int. Inc. stocks limited quantities of western blot positive controls for UFD1L in ready-to-use buffers and antigenic blocking protein/peptide for immuno-depletion assays of UFD1L-101AP antibody. FabGennix Int. Inc., has a wide range of antibodies and reagents for biomedical research community. For a complete listing please visit www. FabGenix.Com.
For research use only, not for diagnostic or therapeutic use.
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