Septin-9 Polyclonal Antibody, Invitrogen™

Description

• Immunogen sequence: LGVKNSEPSA RHVDSLSQRS PKASLRRVEL SGPKAAEPVS RRTELSIDIS SKQVENAGAI GPSRFGLKRA EVLGHKTPEP APRRTEITIV KPQESA The maf oncogene was identified by structural analysis of the AS42 avian transforming retrovirus genome
• The Maf family is divided into two subclasses, large Mafs (vMaf, cMaf, MafB and Nrl) and small Mafs (MafF, MafK, and MafG)
• Both subclasses contain leucinezipper motifs, which allow homodimerization as well as heterodimerization with a variety of other bZip transcription factors
• Large Mafs also contain an acidic transactivation domain absent in the small Maf proteins
• Although they do not possess inherent transactivation activity, small Maf proteins can act as positive regulators of transcription by targeting transcriptionally active dimerization partners to specific DNA regulatory elements
• Conversely, small Mafs can act also as negative regulators of transcription by recruiting transcriptional repressors or by forming homodimers that can replace active dimers
• Human MafF was isolated in a yeast one-hybrid system from a human myometrium cDNA library
• Human MAFF encodes a 164 amino acids proten
• Like other small MAFF proteins, it contains an extended leucine zipper structure and lacks an N-terminal transactivating domain
• The three small Maf proteins have been implicated in a number of physiological processes, including development, differentiation, haematopoiesis and stress response
• Interestingly, these three proteins regulate the stress response via different mechanisms.