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identification and analysis of the genes Sp100, Csprs, and Ifi75 (show SP110 Proteins) in two members of the genus Mus (show TRPV6 Proteins), M. musculus and M. caroli
that Sp100 represses viral transcription and replication in differentiated cells
Data suggest that nuclear antigen Sp100C is a multifaceted histone H3 (show HIST3H3 Proteins) methylation and phosphorylation sensor.
These results suggest that high-risk human papillomavirus 31 target interferon kappa to prevent Sp100 expression and identify Sp100 as an interferon (show IFNA Proteins)-stimulated gene with anti-human papillomavirus activity.
PML (show PML Proteins), hDaxx (show DAXX Proteins) and Sp100 primarily act as cellular restriction factors during lytic human cytomegalovirus replication and during the dynamic process of reactivation but do not serve as key determinants for the establishment of latency.
Sp100 repressed viral transcription and replication only during the initial stages of viral establishment, suggesting that Sp100 acts as a repressor of incoming human papillomavirus type 18 DNA.
Sp100 depletion promotes Adenovirus progeny production and early viral protein synthesis.
Two regions within the N-terminal of the herpes simplex virus 1 ICP0 facilitate the degradation and dissociation of host PML (show PML Proteins) and dissociation of Sp100 from ND10.
Sp100 is recruited to activated arrays in cells expressing the herpes simplex virus type 1 E3 ubiquitin ligase (show MUL1 Proteins), ICP0, which degrades all Sp100 isoforms except unsumoylated Sp100A.
The results suggest that hantavirus infection interferes with DAXX (show DAXX Proteins)-mediated apoptosis, and expression of interferon-activated (show MNDA Proteins) Sp100 and ISG-20 (show ISG20 Proteins) proteins may indicate intracellular intrinsic antiviral attempts.
SP100 and Adeno (show ADORA2A Proteins)-associated virus 2 Rep78 are both located in the nucleolus, which provides the spatial possibility for their interaction.
This gene encodes a subnuclear organelle and major component of the PML (promyelocytic leukemia)-SP100 nuclear bodies. PML and SP100 are covalently modified by the SUMO-1 modifier, which is considered crucial to nuclear body interactions. The encoded protein binds heterochromatin proteins and is thought to play a role in tumorigenesis, immunity, and gene regulation. Alternatively spliced variants have been identified for this gene\; one of which encodes a high-mobility group protein.
SP100 nuclear antigen
, nuclear autoantigen Sp-100
, nuclear autoantigen Sp-100-like
, nuclear dot-associated Sp100 protein
, speckled 100 kDa
, SP100-HMG nuclear autoantigen
, nuclear antigen Sp100
, Nuclear autoantigen Sp-100
, SP140 nuclear body protein