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c-jun (proto oncogene)
Purification and Quality Control
The His-tag recombinant protein is purified by affinity chromatography in combination with FPLC columns.
The purified c-Jun is greater than 90% homogeneous based on SDS-PAGE analysis.
Unit Definition (Activity)
1 unit equals 1 nanogram of purified protein.
Applications
c-jun can be applied in DNA and protein-protein interaction assays.
Formulation and Storage
The protein is in 20mM Tris-HCl pH7.9,100mM NaCl, 0.2mM EDTA, 1mM DTT and 20% glycerol. Stored at -70°C before use. Avoid repeated freeze thaw cycles.
Synonym
AP-1; AP1; c-Jun and Homo sapiens jun oncogene (JUN).
Protein Sequence
MTAKMETTFY DDALNASFLP SESGPYGYSN PKILKQSMTL NLADPVGSLK PHLRAKNSDL
LTSPDVGLLK LASPELERLI IQSSNGHITT TPTPTQFLCP KNVTDEQEGF AEGFVRALAE
LHSQNTLPSV TSAAQPVNGA GMVAPAVASV AGGSGSGGFS ASLHSEPPVY ANLSNFNPGA
LSSGGGAPSY GAAGLAFPAQ PQQQQQPPHH LPQQMPVQHP RLQALKEEPQ TVPEMPGETP
PLSPIDMESQ ERIKAERKRM RNRIAASKCR KRKLERIARL EEKVKTLKAQ NSELASTANM
LREQVAQLKQ KVMNHVNSGC QLMLTQQLQT F
Background
The transcription factor AP-1 (activator protein-1) is involved in cellular proliferation, transformation and death. AP-1 and nuclear factor B (NF-kB) can be specifically targeted to prevent cancer induction in mouse models. AP-1 can be produced by 18 different dimeric combinations of proteins from the Jun (c-Jun, JunB and JunD) and Fos (c-Fos, FosB, Fra-1 and Fra-2) families, including Jun homodimers and Jun–Fos heterodimers (1–4). The Jun and Fos proteins contain a basic-region leucine zipper (bZIP) domain, and are capable of binding to other bZIP proteins including those from the ATF, MAF, CNC and C/EBP (CCAAT/enhancer-binding protein) subfamilies (5]) Jun–Jun and Jun–Fos dimers bind with highest affinity to the 12-O-tetradecanoylphorbol-13-acetate (TPA) response element (TRE) [TGA(C/G)TCA] (6), although many other `AP-1-like sites` have been reported. Binding to any of these sites can be tissue-specific, or affected by neighboring sequences, and dependent upon interactions with other transcription factors or cofactors. Jun and Fos proteins can also dimerize with other bZIP proteins, allowing them to target other DNA binding sites, such as the cAMP response element (CRE), the antioxidant response elements (ARE), and half-sites composed of half of a TRE site and half of a MAF- or CNC-binding site. In addition, AP-1 proteins can interact with other proteins, including the p65 subunit of NF-kB, CBP (CRE-binding-protein-binding protein) (p300), SMAD-3 and -4, and the retinoblastoma protein (see 5 for a more complete list), further increasing the combinatorial potential of Jun and Fos proteins. AP-1 regulates a variety of cellular processes, including proliferation, differentiation and apoptosis, and contributes to both basal and stimulus-activated gene expression. It is activated by growth factors, hormones, stress, cytokines, ROS and ultraviolet radiation Activation occurs both transcriptionally and post-translationally, and is signaled predominantly through the mitogen-activated protein kinase (MAPK) cascade (7). The combinatorial diversity of AP-1 proteins and other interacting factors appears to influence how specific cell types respond to a stimulus. The growth-promoting activity of c-Jun is mediated by repression of tumor suppressors, as well as up-regulation of positive cell cycle regulators. Mostly, c-Jun is a positive regulator of cell proliferation, whereas JunB has the converse effect (8).
References
1. Curran T. and Franza B.R. Jr (1988) Cell 55, 395-397
2. Rauscher F.J.D. et al. (1988) Science, 240, 1010-1016
3. Rauscher F.J.D. et al. (1988) Cell 52, 471-480
4. Wagner E.F. (2001) Oncogene 20, 2333-2497
5. Chinenov Y. and Kerppola T.K. (2001) Oncogene 20, 2438-2452
6. Angel P. et al. (1987) Cell 49, 729-739
This products is recommended For RESEARCH USE ONLY and is Not qualified for Use in Diagnostic or Therapeutic Procedures.
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