Recombinant Human FAT10 Agarose Protein, CF

Human Leukocyte Antigen-F Associated Transcript 10 (FAT10), also known as Ubiquitin D (UBD), is a 165 amino acid (aa) member of the Ubiquitin-like family of proteins. Human FAT10 has a predicted molecular weight of 18.5 kDa and shares 69% aa sequence identity with mouse FAT10 (1). Human FAT10 mRNA is expressed as a single transcript in lymphoblastoid lines and dendritic cells, but more than one mRNA transcript has been identified for murine FAT10 (1,2). FAT10 can also be induced by IFN-gamma and TNF-alpha in some cell lines (1). Structurally, FAT10 consists of two Ubiquitin-like domains that are connected by a short linker. Like Ubiquitin, FAT10 has a C-terminal glycine residue that can be used to form isopeptide bonds with target proteins. FAT10-conjugated proteins are targeted to the proteasome where the 26S Proteasome subunit S5a/Angiocidin binds to FAT10 and enables subsequent degradation of the conjugated protein (3). In addition to S5a/Angiocidin, FAT10 has been shown to interact with Huntingtin, Ataxin-1, MAD2, and NUB1L (4,5). FAT10 has been implicated in a number of biological processes such as cell cycle control, antigen presentation, and cytokine response (1,6-8). This protein is covalently coupled to agarose beads via primary amines allowing for a fully functional C-terminus. It is useful for isolation and capture of FAT10 interacting proteins and/or enzymes that have an affinity for this Ubiquitin-like protein.