Anti-SP100, clone PCRP-SP100-1B9

0.2 mg/ml in 1X PBS with 0.1 mg/ml BSA (US sourced), 0.05% sodium azide. The human SP100 gene encodes an autoantigen that co-localizes with PML and NDP52 in distinct nuclear domains, called nuclear dots (NDs) or ND10 nuclear bodies. Papova-, adeno-, and herpesviruses begin their transcription and DNA-replication at NDs, which play a role in autoimmunity, viral infections and in the etiology of acute promyelocytic leukemia. SP-100 is an interferon inducible protein that has two splice variants. One splice variant contains a highly conserved copy of the DNA-binding high mobility group 1 protein sequence, and thus represents a novel HMG-box protein. This alternatively spliced variant of SP-100 has a unique expression and localization pattern that is distinct from the SP-100 full-length protein. The SP100 protein is covalently modified by the small ubiquitin-related protein SUMO-1. SP-100 contains a functional nuclear localization signal and an ND-targeting region, which overlaps with the SP-100 homodimerization domain. Protein function: Together with PML, this tumor suppressor is a major constituent of the PML bodies, a subnuclear organelle involved in a large number of physiological processes including cell growth, differentiation and apoptosis. Functions as a transcriptional coactivator of ETS1 and ETS2 according to PubMed:11909962. Under certain conditions, it may also act as a corepressor of ETS1 preventing its binding to DNA according to PubMed:15247905. Through the regulation of ETS1 it may play a role in angiogenesis, controlling endothelial cell motility and invasion. Through interaction with the MRN complex it may be involved in the regulation of telomeres lengthening. May also regulate TP53-mediated transcription and through CASP8AP2, regulate FAS-mediated apoptosis. Also plays a role in infection by viruses, including human cytomegalovirus and Epstein-Barr virus, through mechanisms that may involve chromatin and/or transcriptional regulation. [The UniProt Consortium]