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.
Eukaryotic cells contain 3 different types of prenyltransferases that attach either a farnesyl group (15 carbons) or a geranylgeranyl group (20 carbons) in thioether linkage to C-terminal cysteine residues in a variety of proteins. These posttranslational modifications provide a mechanism for membrane localization of proteins that lack a transmembrane domain. CAAX farnesyltransferase (FTase) attaches a farnesyl group from farnesyl pyrophosphate to cysteine residues at the fourth position from the C terminus of proteins that end in the CAAX box, where C is cysteine, A is usually but not always an aliphatic amino acid, and X is typically methionine or serine. This enzyme has the ability to farnesylate peptides as short as 4 residues in length that conform to the CAAX consensus sequence. The gene for the beta subunit of CAAX farnesyltransferase (FNTB) has been pinpointed to 14q23-q24 by Southern blot hybridization and PCR analyses of panels of human/Chinese hamster somatic cell hybrid lines and by fluorescence chromosomal in situ hybridization.
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Protein Aliases: CAAX farnesyltransferase subunit beta; EC 220.127.116.11; farnesyltransferase beta subunit; ft beta; FTase beta; FTase-beta; Protein farnesyltransferase subunit beta; Ras proteins prenyltransferase subunit beta
Gene Aliases: FNTB; FPTB