The SOX-11 transcription factor is a member of the SOX family known to be involved in embryonic development regulation and cell fate determination. The protein acts as a transcriptional regulator and appears to modulate fundamental aspects of normal embryonic nervous system development and tumorigenesis. SOX-11 is not found expressed in adult tissues except for the adult immature neuron.
AP-endonuclease (APE1/Ref-1) is an essential multifunctional protein involved in the repair of oxidative DNA damage as well as in transcriptional regulation in tumor cells. It functions as an apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions, and may also play a role in the epigenetic regulation of gene expression and the protection from granzymes-mediated cellular repair leading to cell death.
NF-kappa-B is a ubiquitous transcription factor involved in several biological processes such as inflammation, immunity, differentiation, cell growth, tumor genesis and apoptosis. Unlike the majority of transcription factors that reside in the nucleus, NFkB is predominantly bound to IkBs protein inhibitors and is located in the cytoplasm. There are two major signaling pathways involved in the activation of NFkB, canonical and non-canonical. [1] In the canonical NF-kB pathway, NF-kB activation is dependent on the inducible degradation of IkBs, particularly IkBa.
RNA polymerase II is a large 12-subunit complex that synthesizes all mRNAs and several non-coding RNAs in eukaryotic cells. It is a DNA-dependent RNA polymerase enzyme that catalyzes transcription of DNA into RNA based on the four ribonucleoside triphosphate building blocks. RNA polymerase II is regulated through DNA-binding transcriptional regulators in both gene and cell type-specific manners.
Protein arginine methylation is a prevalent posttranslational modification in eukaryotic cells. It regulates RNA processing, trafficking and nascent pre-RNA metabolism, receptor-mediated signal transduction, and transcriptional activation processes. PRMT6 was originally identified through a genome-wide search for human protein arginine N-methyltransferase (PRMT) family members. This particular enzyme has type I PRMT activity and with regards to substrate specificity, is functionally distinct from two other previously characterized type I enzymes - PRMT1 and PRMT4.
