C-jun (Oncoprotein C-jun) is a component of the transcription factor AP-1 that binds and activates transcription at TRE/AP-1 elements and appears to be a major downstream target of the SAPK/JNK signaling pathway. The transcriptional activity of c-Jun is regulated by phosphorylation at Ser63 and Ser73. Extracellular signals including growth factors, transforming oncoproteins and UV irradiation stimulate phosphorylation of c-Jun at Ser63/73 and activate c-Jun dependent transcription. Mutatio

Insulysin was identified nearly a century ago as an enzyme responsible for the degradation of insulin in cells, although the precise interactions between insulin and insulysin remain elusive. Human insulysin was cloned in 1988, and shown to be a 118 kDa protein that exists primarily as a homodimer, and perhaps also complexed with other molecules. The sequence is well conserved between humans, rats and mice, and the antibody recognizes these species. Insulysin is a metalloproteinase of the

mCherry is a fluorophore (a fluorescent molecule) used in biotechnology as a tracer to follow the flow of fluids, as a marker when tagged to molecules and cells components. mCherry is a monomeric fluorescent construct with peak absorption/emission at 587 nm and 610 nm, respectively. It is resistant to photobleaching and is stable. mCherry is sometimes preferred to other fluorophores due to its colour, as well as its photostability compared to other monomeric fluorophores.

Vesicular stomatitis virus (VSV), an enveloped RNA virus from the Rhabdoviridae family, is released from the plasma membrane of host cells by a process called budding. The glycoprotein (VSV-g) contains a domain in its extracellular membrane proximal stem that appears to be needed for efficient VSV budding.

The V5 epitope tag is derived from a small epitope (Pk) present on the P and V proteins of the paramyxovirus of simian virus 5 (SV5). The V5 tag is usually used with all 14 amino acids (GKPIPNPLLGLDST), although it has also been used with a shorter 9 amino acid sequence (IPNPLLGLD).

The Strep-tag system is a method which allows the purification and detection of proteins by affinity chromatography. The Strep-tag is a synthetic peptide consisting of eight amino acids (Trp-Ser-His-Pro-Gln-Phe-Glu-Lys). This peptide sequence exhibits intrinsic affinity towards Strep-Tactin, a specifically engineered streptavidin and can be N- or C- terminally fused to recombinant proteins. By exploiting the highly specific interaction, Strep-tagged proteins can be isolated in one step from c