SEPT9 Antibody / Septin 9

Western blot: 1:500-1:2000,Immunohistochemistry (FFPE): 1:25,Flow cytometry: 1:25 (1x10e6 cells)

The stated application concentrations are suggested starting points. Titration of the Septin 9 antibody may be required due to differences in protocols and secondary/substrate sensitivity.

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.

Purified

In 1X PBS, pH 7.4, with 0.09% sodium azide

A portion of amino acids 57-85 from the human protein were used as the immunogen for the Septin 9 antibody.

This Septin 9 antibody is available for research use only.

Cytoplasmic

Antigen affinity purified

Human

Q9UHD8