- CITATIONS: 2
|Application ||WB, IHC-P, FC, E|
|Calculated MW||65401 Da|
|Antigen Region||557-586 aa|
|Other Names||Septin-9, MLL septin-like fusion protein MSF-A, MLL septin-like fusion protein, Ovarian/Breast septin, Ov/Br septin, Septin D1, SEPT9, KIAA0991, MSF|
|Target/Specificity||This SEPT9 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 57-85 amino acids from the C-terminal region of human SEPT9.|
|Precautions||SEPT9 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Filament-forming cytoskeletal GTPase (By similarity). May play a role in cytokinesis (Potential). May play a role in the internalization of 2 intracellular microbial pathogens, Listeria monocytogenes and Shigella flexneri.|
|Cellular Location||Cytoplasm, cytoskeleton Note=In an epithelial cell line, concentrates at cell-cell contact areas. After TGF-beta1 treatment and induction of epithelial to mesenchymal transition, colocalizes partly with actin stress fibers. During bacterial infection, displays a collar shape structure next to actin at the pole of invading bacteria|
|Tissue Location||Widely expressed. Isoforms are differentially expressed in testes, kidney, liver heart, spleen, brain, peripheral blood leukocytes, skeletal muscle and kidney. Specific isoforms appear to demonstrate tissue specificity. Isoform 5 is the most highly expressed in fetal tissue. Isoform 1 is detected in all tissues except the brain and thymus, while isoform 2, isoform 3, and isoform 4 are detected at low levels in approximately half of the fetal tissues|
Provided below are standard protocols that you may find useful for product applications.
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.
Proc. Natl. Acad. Sci. U.S.A. 96:6428-6433(1999). Cancer Res. 60: 4729-4734, 2000. Oncogene 20: 5930-5939, 2001.
If you have any additional inquiries please email technical services at email@example.com.