Recombinant rabbit monoclonal antibodies are produced using in vitro expression systems. The expression systems are developed by cloning in the specific antibody DNA sequences from immunoreactive rabbits. Then, individual clones are screened to select the best candidates for production. The advantages of using recombinant rabbit monoclonal antibodies include: better specificity and sensitivity, lot-to-lot consistency, animal origin-free formulations, and broader immunoreactivity to diverse targets due to larger rabbit immune repertoire.
Fos and Jun dimerize to form Activator Protein-1 (AP-1), a transcriptional factor that binds to the 12-O-tetradecanoylphorbol 13-acetate (TPA) response element (TRE) of several cellular and viral genes including human collagenase, metallothionein IIa, stromelysin, interleukin 2, SV40 and polyoma. Fos and Jun contain the 'leucine-zipper' motif that allows for dimerization and an adjacent basic domain required for biological activity. The functionally active form of Fos is in a heterodimer with a member of the Jun family. While Jun family members can form functional homodimers, studies indicate that Fos family members do not self-associate and therefore do not bind DNA on their own. The various dimers differ in their ability to transactivate AP-1 dependent genes.
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Protein Aliases: Activator protein 1; AH119; AP1; Avian sarcoma virus 17 (v-jun) oncogene homolog; enhancer-binding protein AP1; immediate early; Jun A; Jun activation domain binding protein; Jun oncogene; jun proto-oncogene; p39; Proto-oncogene c-Jun; Transcription factor AP-1; V-jun avian sarcoma virus 17 oncogene homolog; v-jun sarcoma virus 17 oncogene homolog
Gene Aliases: AP-1; AP1; c-Jun; JUN; Junc; Rjg-9