Cyclic AMP-dependent transcription factor ATF-5 (Atf5), mouse, recombinant

Organism: Mus musculus (Mouse). Source: E.coli. Expression Region: 1-283aa. Protein Length: Full Length. Tag Info: N-terminal 10xHis-tagged and C-terminal Myc-tagged. Target Protein Sequence: MSLLATLGLE LDRALLPASG LGWLVDYGKL PLAPAPLGPY EVLGGALEGG LPGGGEPLAG DGFSDWMTER VDFTALLPLE APLPPGTLPP PSPAPPDLEA MASLLKKELE QMEDFFLDAP LLPPPSPPPP PPPAAAPSLP LPLPLPTFDL PQPPTLDTLD LLAVYCRSEA GPGDSGLSTL PVPQQPPPLA PLPSPARPAP YPSPASTRGD RKQKKRDQNK SAALRYRQRK RAEGEALEGE CQGLEARNRE LRERAESVER EIQYVKDLLI EVYKARSQRT RST. Purity: Greater than 85% as determined by SDS-PAGE. Endotoxin: Not test. Biological Activity: n/a. Form: Liquid or Lyophilized powder. Buffer: If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0. Reconstitution: We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20 °C/-80 °C. Our default final concentration of glycerol is 50%. Customers could use it as reference. Storage: The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20 °C/-80 °C. The shelf life of lyophilized form is 12 months at -20 °C/-80 °C. Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4 °C for up to one week. Relevance: Transcription factor that either stimulates or represses gene transcription through binding of different DNA regulatory elements such as cAMP response element (CRE) (consensus: 5'-GTGACGT[AC][AG]-3'), ATF5-specific response element (ARE) (consensus: 5'-C[CT]TCT[CT]CCTT[AT]-3') but also the amino acid response element (AARE), present in many viral and cellular promoters. Critically involved, often in a cell type-dependent manner, in cell survival, proliferation, and differentiation. Its transcriptional activity is enhanced by CCND3 and slightly inhibited by CDK4. Important regulator of the cerebral cortex formation, functions in cerebral cortical neuroprogenitor cells to maintain proliferation and to block differentiation into neurons. Must be down-regulated in order for such cells to exit the cycle and differentiate. Participates in the pathways by which SHH promotes cerebellar granule neuron progenitor cells proliferation. Critical for survival of mature olfactory sensory neurons (OSN), directs expression of OSN-specific genes. May be involved in osteogenic differentiation. Promotes cell proliferation and survival by inducing the expression of EGR1 sinergistically with ELK1. Once acetylated by EP300, binds to ARE sequences on target genes promoters, such as BCL2 and EGR1. Plays an anti-apoptotic role through the transcriptional regulation of BCL2, this function seems to be cell type-dependent. Cooperates with NR1I3/CAR in the transcriptional activation of CYP2B6 in liver. In hepatic cells, represses CRE-dependent transcription and inhibits proliferation by blocking at G2/M phase. May act as a negative regulator of IL1B transduction pathway in liver. Upon IL1B stimulus, cooperates with NLK to activate the transactivation activity of C/EBP subfamily members. Besides its function of transcription factor, acts as a cofactor of CEBPB to activate CEBPA and promote adipocyte differentiation. Regulates centrosome dynamics in a cell-cycle- and centriole-age-dependent manner. Forms 9-foci symmetrical ring scaffold around the mother centriole to control centrosome function and the interaction between centrioles and pericentriolar material. Reference: "Mouse Atf5: molecular cloning of two novel mRNAs, genomic organization, and odorant sensory neuron localization." Hansen M.B., Mitchelmore C., Kjaerulff K.M., Rasmussen T.E., Pedersen K.M., Jensen N.A. Genomics 80:344-350(2002). Function: nan