The liver cancer cell lines Bel-7402 (Cell bank of Chinese Academy of Sciences, Shanghai, China), SMMC-7721 (Cell bank of Chinese Academy of Sciences, Shanghai, China), Huh7 (Cobioer, Nanjing, China), HepG2 (Cobioer, Nanjing, China), SK-Hep1 (Cell bank of Chinese Academy of Sciences, Shanghai, China), Bel-7404 (Cell bank of Chinese Academy of Sciences, Shanghai, China) and hepatocyte lines THLE-3 (Biovector, NTCC, Beijing, China) and HL-7702 (Cell bank of Chinese Academy of Sciences, Shanghai, China) were cultured in DMEM. Cells were treated with D -glucose or L -glucose (Sigma, St Louis, MO, USA) at a final concentration from 5.5 to 50 mM, PuGNAc (Sigma) at a final concentration of 25 μM, GlcNAc (Sigma) at a concentration of 4 mM, NaCl (Sangon, Shanghai, China) at a final concentration of 50 mM and Cycloheximide (CHX, sigma) at a final concentration of 50 μg ml−1. The lentiviral-based OGT expression plasmid and OGT-shRNA (sh4) were purchased from Origene (Beijing, China), and the OGT-sh7 was purchased from Genechem (Shanghai, China) The expression plasmids encoding YAP-sh1&2, YAP, YAP-FLAG, TEAD4-Myc, CREB-HA, βTrCP-FLAG, c-Fos and the pUAS-Luc/TEAD-Gal4 system were constructed, as previously described by us7 (link)30 (link)67 (link). The wild type, S208A, T213A, T216A, S217A, S227A, S229A and T241A-YAP-FLAG expression plasmids were constructed using pcDNA3.1(+) or pLJM-based lentiviral plasmid as the backbone. Promoter regions of human OGT, Nudt9 and SLC5A3 genes were PCR amplified from gDNA of Bel-7402 cells and cloned into pGL4.21 (Promega, Madison, WI, USA) vectors. The primers used for this study are listed in Supplementary Data 1 .
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C-fos Genes
C-fos Genes
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Most cited protocols related to «C-fos Genes»
beta-Transducin Repeat-Containing Proteins
Cancer of Liver
Cell Lines
Cells
Chinese
Cloning Vectors
Cycloheximide
Genes
Glucose
Glucose, (L)-Isomer
Hepatocyte
Homo sapiens
N-acetylglucosaminono-1,5-lactone O-(phenylcarbamoyl)oxime
NUDT9
Oligonucleotide Primers
Paragangliomas 4
Plasmids
Promega
Short Hairpin RNA
Sodium Chloride
v-fos Genes
Vertebral Column
Rats were administered a daily oral administration (gavage) of either water, FOS (3 g/kg) or GOS (4 g/kg), for 5 weeks (n = 8/group). This dosing regimen was based on previous studies (Anthony et al., 2006 (link)). Copies of Bifidobacteria spp. genes in DNA extracted from faecal pellets were determined with standard QPCR at the end of the study, as previously described (Ketabi et al., 2011 (link)). Twenty-four hours after the last gavage, the animals were sacrificed, their brains removed and trunk blood collected in EDTA-coated tubes. Blood was centrifuged (5000 rpm, 15 min) to obtain plasma which was then stored at −80 °C. The frontal cortex and hippocampus were dissected out from half of the harvested brains. Brain hemispheres and isolated regions were snap-frozen in isopentane on dry-ice and stored with plasmas at −80 °C prior to use. Additional faecal pellets were collected from each animal (n = 8/group), weighed, homogenised in PBS (1:1, w/v), and then centrifuged at 14,000 rpm for 10 min at 4 °C. Supernatants were removed and stored at −80 °C prior to HPLC analysis.
Administration, Oral
Animals
Bifidobacterium
BLOOD
Brain
Cerebral Hemispheres
Dry Ice
Edetic Acid
Feces
Freezing
Genes
High-Performance Liquid Chromatographies
isopentane
Lobe, Frontal
Pellets, Drug
Plasma
Rattus
Seahorses
Treatment Protocols
Tube Feeding
Soluble pMHCI manufacture, tetramerization and biophysical studies were performed as previously described 31 (link). The mutations in HLA-A68 and the biophysical validation of their effects are published elsewhere 13 (link), 31 (link). In order to obtain the sequence of an HLA-A68-restricted TCR, cDNA from c23 was used as a template in 42 separate PCR using a primer set to cover all TCRAV and TCRAJ genes. Only one reaction generated a product. Sequencing confirmed a TCR α chain made from the TCRAV 14 gene with a TCRAJ 20 joining region (IMGT nomenclature). The TCRB sequence was generated by a single PCR with a combined primer set 34 (link). The reaction yielded a single product. Sequence analysis showed a TCRBV 7-9 gene with a TCRBJ 1-1 joining region. The TCR α chain was cloned into pGMT7 expression vector as a fusion construct with the c-jun leucine zipper region 35 (link). A TCR β chain pGMT7 expression vector was constructed to express the TCR chain as a fusion with the v-fos leucine zipper 35 (link). Expression vectors were transformed into Escherichia coli Rosetta DE3 (pLysS) and protein was produced as inclusion bodies by inducing protein expression with 0.5 mM isopropyl-β-d -thiogalactopyranoside.
Following cell harvest by centrifugation, inclusion bodies were isolated by sonication and purified with three successive detergent washes using 0.5% Triton X-100. Inclusion bodies were given a final wash in resuspension buffer to remove any detergent before being resolubilized in guanidine solution (6 M guanidine, 50 mM Tris pH 8.1, 100 mM NaCl, 10 mM EDTA, 10 mM dithiothreitol). Insoluble material was pelleted by centrifugation and the supernatant stored at –80°C. TCR-zipper chains were refolded at a 5:1 ratio of α:β chain. Each solubilized inclusion body chain was diluted to 5 mg/mL in guanidine solution. To ensure complete denaturation, dithiothreitol was added to a concentration of 10 mM and chains were incubated at 37°C for 30 min. Refolding of soluble TCR was initiated by injecting the dissolved α and β chain inclusion bodies simultaneously into a vigorously stirring refolding buffer (5 M urea, 0.4 Ml -arginine, 100 mM Tris pH 8.1, 6.5 mM cysteamine-HCl, 3.7 mM cystamine di-hydrochloride) chilled to 4°C, to a final concentration of 60 mg/L.
The solution was left for 3 h, then dialyzed for 24 h against ten volumes of demineralized water, followed by ten volumes of 10 mM Tris pH 8.1. All dialysis steps were carried out at 4°C. Dialyzed TCR was isolated from impurities by filtering and loading onto a POROS 50 HQ anion exchange column (Applied Biosystems). The column was washed with 10 mM Tris pH 8.1 and bound protein was eluted with a NaCl gradient (0–1 M) in the same buffer. Correctly refolded protein was confirmed by reduced and non-reduced sodium dodecyl sulfate (SDS)-PAGE. Fractions containing correctly refolded TCR were pooled, concentrated and further purified on a Superdex 200 gel filtration column (Amersham Biosciences, Uppsala, Sweden) in HEPES-buffered saline (HEPES pH 7.4, 150 mM NaCl, 3 mM EDTA). The final purified c23 TCR was analyzed by SDS-PAGE in reducing and non-reducing conditions. Peak fractions were pooled and concentrated prior to BIAcore™ surface plasmon resonance studies.
Following cell harvest by centrifugation, inclusion bodies were isolated by sonication and purified with three successive detergent washes using 0.5% Triton X-100. Inclusion bodies were given a final wash in resuspension buffer to remove any detergent before being resolubilized in guanidine solution (6 M guanidine, 50 mM Tris pH 8.1, 100 mM NaCl, 10 mM EDTA, 10 mM dithiothreitol). Insoluble material was pelleted by centrifugation and the supernatant stored at –80°C. TCR-zipper chains were refolded at a 5:1 ratio of α:β chain. Each solubilized inclusion body chain was diluted to 5 mg/mL in guanidine solution. To ensure complete denaturation, dithiothreitol was added to a concentration of 10 mM and chains were incubated at 37°C for 30 min. Refolding of soluble TCR was initiated by injecting the dissolved α and β chain inclusion bodies simultaneously into a vigorously stirring refolding buffer (5 M urea, 0.4 M
The solution was left for 3 h, then dialyzed for 24 h against ten volumes of demineralized water, followed by ten volumes of 10 mM Tris pH 8.1. All dialysis steps were carried out at 4°C. Dialyzed TCR was isolated from impurities by filtering and loading onto a POROS 50 HQ anion exchange column (Applied Biosystems). The column was washed with 10 mM Tris pH 8.1 and bound protein was eluted with a NaCl gradient (0–1 M) in the same buffer. Correctly refolded protein was confirmed by reduced and non-reduced sodium dodecyl sulfate (SDS)-PAGE. Fractions containing correctly refolded TCR were pooled, concentrated and further purified on a Superdex 200 gel filtration column (Amersham Biosciences, Uppsala, Sweden) in HEPES-buffered saline (HEPES pH 7.4, 150 mM NaCl, 3 mM EDTA). The final purified c23 TCR was analyzed by SDS-PAGE in reducing and non-reducing conditions. Peak fractions were pooled and concentrated prior to BIAcore™ surface plasmon resonance studies.
Aluminum
Amygdaloid Body
Anabolism
Antibodies
Brain
c-fos Genes
Cells
Chickens
DAPI
Dopamine
Equus asinus
Hypothalamus
Immune Sera
Immunoglobulins
Immunohistochemistry
Mus
Nervousness
Nucleus, Arcuate
Phosphates
Proteins
Rabbits
Saline Solution
Serum
Tissues
Transcription, Genetic
Tyrosine
Tyrosine 3-Monooxygenase
Because the IEG expression patterns form clusters of brain areas across brain subdivisions that can be misleading in defining subdivision boundaries and because we examined multiple species for which cerebral subdivision organization is not well characterized, we sought reliable markers of brain subdivision boundaries to define the anatomical locations of IEG expression. Nissl staining was not suitable for unambiguously defining brain subdivision boundaries. Thus, in addition to Nissl staining, we found that GluR1 [15] (link) and FoxP1 [16] (link) expression patterns were valuable and critical for identifying brain subdivisions in all avian species. GluR1 shows enriched expression in the hippocampus, mesopallium, and striatum, low expression in the pallidum and in primary thalamic recipient neurons (L2, B, part of E, and IH), intermediate expression elsewhere, and differential expression in songbird vocal nuclei (high in AreaX, low in HVC, RA, and MAN). FoxP1 shows highly enriched expression in the mesopallium and striatum, low expression in the hyperpallium and nidopallium, and lower expression in the primary thalamic recipient neurons (L2, B, part of E, and IH), the pallidum and arcopallium. FoxP1 also shows differential expression in songbird vocal nuclei (higher in HVC, RA, and Area X; lower in MAN), the parrot analogs of Area X (higher in MMSt) and HVC (higher in NLC) as previously noted [16] (link), and, as we note here, the hummingbird analog of HVC (higher in VLN).
When using these genes and many others as brain subdivision markers (Jarvis et al, in preparation), it becomes apparent that what has been previously labeled as dorsal hyperstriatum (HD) and ventral hyperstriatum (HV) in the old avian brain nomenclature [29] (link), [31] (link) is marked with mesopallium enriched genes, such as GluR1 and FoxP1. Thus, here we follow the practice of some of our recent publications [26] (link), [27] (link) of labeling the formally named dorsal hyperstriatum (HD) as dorsal mesopallium (MD) and the formally named ventral hyperstriatum (HV) as ventral mesopallium (MV), due to the presence of mesopallium specific gene expression.
For the budgerigar brain we used the term supra-lateral nidopallium (SLN) to describe the area that stretches dorsally, ventrally, and caudally around the vocal nucleus NLC. The caudal and ventral areas have previously been called the superior central nucleus of the lateral nidopallium and ventral nucleus of the lateral nidopallium (NLs and NLv) [30] (link).
In addition to the above definitions, we also sought to define a more global terminology that can be applied across multiple avian species for names of homologous brain structures that are in different topological positions among species. When possible, we used a non-coordinate terminology for this purpose. For primary thalamic receiving populations, we labeled functionally adjacent regions with names that were associated with these populations. Thus, for the visually-activated areas adjacent to and near the entopallium that have been called lateral nidopallium (LN) and lateral ventral mesopallium (LMV), we called them nidopallium adjacent to the entopallium (Ne) and ventral mesopallium near the entopallium (MVe). For somatosensory areas near basorostralis, we called them Nb and MVb. For the auditory areas near Field L2, we called them N-L2 (for L1 and L3), and MV-L2 (for caudal mesopallium, CM); we note here that based on the FoxP1 expression, CM and the vocal nuclei Av and MO of songbirds, the MO of parrots, and the VAM of hummingbirds are all within the ventral mesopallium. This naming scheme allowed us to easily compare expression patterns across species.
Finally, while the presence of seven comparable cerebral vocal nuclei amongst the three vocal learning bird groups has been published [5] (link)–[7] (link) and reviewed [10] (link), we briefly review the evidence, particularly for the lesser studied nuclei, to help clarify the definitions used in this study. We define a vocal nucleus as a continuous anatomical structure that has vocalizing-associated activation. In this regard, HVC, RA, NIf, Av, MO, and Area X of songbirds can be defined as one structure each. LMAN and MMAN in zebra finches has been noted to be discontinuous [71] (link), [80] (link). However, we noted that this is not the case for all songbirds. In canaries, for example, LMAN and MMAN are one continuous structure (Fig. S9A Fig. S9B
When using these genes and many others as brain subdivision markers (Jarvis et al, in preparation), it becomes apparent that what has been previously labeled as dorsal hyperstriatum (HD) and ventral hyperstriatum (HV) in the old avian brain nomenclature [29] (link), [31] (link) is marked with mesopallium enriched genes, such as GluR1 and FoxP1. Thus, here we follow the practice of some of our recent publications [26] (link), [27] (link) of labeling the formally named dorsal hyperstriatum (HD) as dorsal mesopallium (MD) and the formally named ventral hyperstriatum (HV) as ventral mesopallium (MV), due to the presence of mesopallium specific gene expression.
For the budgerigar brain we used the term supra-lateral nidopallium (SLN) to describe the area that stretches dorsally, ventrally, and caudally around the vocal nucleus NLC. The caudal and ventral areas have previously been called the superior central nucleus of the lateral nidopallium and ventral nucleus of the lateral nidopallium (NLs and NLv) [30] (link).
In addition to the above definitions, we also sought to define a more global terminology that can be applied across multiple avian species for names of homologous brain structures that are in different topological positions among species. When possible, we used a non-coordinate terminology for this purpose. For primary thalamic receiving populations, we labeled functionally adjacent regions with names that were associated with these populations. Thus, for the visually-activated areas adjacent to and near the entopallium that have been called lateral nidopallium (LN) and lateral ventral mesopallium (LMV), we called them nidopallium adjacent to the entopallium (Ne) and ventral mesopallium near the entopallium (MVe). For somatosensory areas near basorostralis, we called them Nb and MVb. For the auditory areas near Field L2, we called them N-L2 (for L1 and L3), and MV-L2 (for caudal mesopallium, CM); we note here that based on the FoxP1 expression, CM and the vocal nuclei Av and MO of songbirds, the MO of parrots, and the VAM of hummingbirds are all within the ventral mesopallium. This naming scheme allowed us to easily compare expression patterns across species.
Finally, while the presence of seven comparable cerebral vocal nuclei amongst the three vocal learning bird groups has been published [5] (link)–[7] (link) and reviewed [10] (link), we briefly review the evidence, particularly for the lesser studied nuclei, to help clarify the definitions used in this study. We define a vocal nucleus as a continuous anatomical structure that has vocalizing-associated activation. In this regard, HVC, RA, NIf, Av, MO, and Area X of songbirds can be defined as one structure each. LMAN and MMAN in zebra finches has been noted to be discontinuous [71] (link), [80] (link). However, we noted that this is not the case for all songbirds. In canaries, for example, LMAN and MMAN are one continuous structure (
Most recents protocols related to «C-fos Genes»
siRNA was injected into the ARC as described above. The sequences of the full-length Fos and Jun B genes were obtained from GenBank. Six recombinant adenovirus plasmids expressing siRNAs targeting c-Fos or Jun B were designed (Table S1 ) and synthesized (Tuoran Biotech, Shanghai). It was confirmed that the sequences did not have homology to any other mouse genes, as determined with BLAST tool on the NCBI website. The most suitable siRNA was determined. EA and behavioral tests were performed 1 day after c-Fos and Jun B genes were knockdown after the administration of siRNA.
CHOP protein is a transcription factor that is activated in association with ERS and P38 MAPK activation and promotes the production of pro-inflammatory cytokines. Inflammation-related genes, such as Fas and Stat, are also associated with ERS and increased intracellular calcium release. GADD34, XBP1, and PAR-2 might be upregulated through P38 MAPK phosphorylation in the ERS reaction. The expression of Nos2 is increased during inflammatory responses, resulting in increased production of nitric oxide. Increased expression of Ptgs2 leads to increased production of prostaglandin E2 and promotes an inflammatory response. JAK2 cooperates with STAT1 and STAT3 to generate cellular signaling pathways and provides important clues to understanding various inflammatory diseases. The induction of ASC and NLRP3 inflammasomes plays an intermediate role in a series of inflammatory cascades from ERS to pyroptosis. c-Jun and c-Fos play important roles in regulating inflammation-related gene expression. The transcription of target genes such as Chop, Jak2, Fas, c-Jun, c-Fos, Stat-1, Stat-3, Nos2, Ptgs2, Gadd34, Xbp1, Par-2, Nlrp3, and Asc was evaluated using quantitative real-time RT-PCR [20 (link)].
We have used the studies cited in the references to make a review from the latest results at the field of neurobiology, genetics, and neuropsychology to analyze what are the mechanisms regulating human behavior at neural and psychological level under conditions of stress. We try to formulate how sensory information influences response behavior by semi-analytical, information theoretical, statistical and neuropsychological methods. To understand more human behavior in the psychological conditions of stress we must start from the underlying principles of neurobiology and genetics. It can be done by the method of relating neurobiological models to behavioral models of signaling pathways.
Calcium influx into the postsynaptic neuron can alter cellular function by activating new gene transcription. Calcium influx activates a number of signaling pathways converging on transcription factors within the nucleus, which in turn control the expression of a large number of neuronal activity regulated genes. Signaling pathways mediate activity-dependent transcription in experience-dependent neural development and plasticity. This neuronal activity regulates by the signal transduction pathways the activity-dependent gene expression program. On the other side, neuronal activity-regulated genes showing how this activity-regulated program controls neuronal development [1, 2] . The c-fos mRNA is induced by synaptic activity resulting from sensory experience due the Fos protein with Jun family members comprised the AP-1 transcriptional complex, which is critical for the organism's adaptive responses to experience. A brain-specific deletion of the c-fos gene displays deficits in synaptic plasticity and defects in learning and memory. Loss of Fos-dependent transcription gives raise to additional behavioral deficits [3] . The activity-regulated transcriptional program uncovered a mechanism by which calcium-dependent gene induction alters the function of specific synapses. Examples,
Calcium influx into the postsynaptic neuron can alter cellular function by activating new gene transcription. Calcium influx activates a number of signaling pathways converging on transcription factors within the nucleus, which in turn control the expression of a large number of neuronal activity regulated genes. Signaling pathways mediate activity-dependent transcription in experience-dependent neural development and plasticity. This neuronal activity regulates by the signal transduction pathways the activity-dependent gene expression program. On the other side, neuronal activity-regulated genes showing how this activity-regulated program controls neuronal development [1, 2] . The c-fos mRNA is induced by synaptic activity resulting from sensory experience due the Fos protein with Jun family members comprised the AP-1 transcriptional complex, which is critical for the organism's adaptive responses to experience. A brain-specific deletion of the c-fos gene displays deficits in synaptic plasticity and defects in learning and memory. Loss of Fos-dependent transcription gives raise to additional behavioral deficits [3] . The activity-regulated transcriptional program uncovered a mechanism by which calcium-dependent gene induction alters the function of specific synapses. Examples,
We first took 50 mg of fresh rat heart tissue to extract total RNA according to the kit instructions. After the RNA concentration was detected and determined using an Ultra Trace UV-Vis Spectrophotometer (model number: DYCZ-40D, DeNovix, DE, USA), total RNA from all samples was diluted to 200 ng/μL and then reverse transcribed into cDNA. The instruments used in the experiment include a PCR machine (model number: DS-11, Thermo Fisher Scientific, Waltham, MA, USA) and a real-time PCR instrument (model number: ABI ProFle LightCycler 9, Roche, Basel, Switzerland). The amplification reaction system used is real-time fluorescent quantitative PCR. Relative quantitative analysis of mRNA was performed after 40 cycles using the ΔΔ CT method to detect the relative expression levels of mRNA of relevant genes. Tianjin Boyou Biotechnology Co., Ltd. (Tianjin, China) provided the primers we needed (Table 1). Notes: COL : collagen ; COL : collagen ; α-SMA: α-smooth muscle actin; c-Fos: c-Fos proto-oncogene; F: forward primer; R: reverse primer.
The in situ hybridization (ISH) procedure was carried out as previously described [65 (link), 66 (link)] with oligonucleotide probes specifically complementary to the sequence of the mRNA of the immediate early genes C-Fos (nucleotides 159-203 of the NCBI Reference Sequence NM_022197.2) or Zif268 (nucleotides 1680-1724 of the NCBI Reference Sequence NM_012551.3), tailed by 3’OH incorporation of 35S-dATP (1250 mCi/mmol, Perkin Elmer, UK) by a terminal Deoxynucleotidyl transferase (Promega, M1875) with a specificity of 2.5 × 106 cpm/ml (C-Fos) or 3 × 106 cpm/ml (Zif268).
Following fixation and pre-hybridization treatments aiming at reducing non-specific hybridization, slides were incubated overnight at 42 °C in the hybridization buffer (50% deionized formamide, 10% dextran sulfate, 50 ng/ml denaturated salmon sperm DNA, 5% Sarcosyl, 0.2% SDS, 1 mM EDTA, 300 nM NaCl, 5X Denhardt’s in 2X standard sodium citrate (SSC)) with the probes diluted at a concentration of 8.75 ng/ml (C-Fos) or 6.25 ng/ml (Zif268). Slides were then washed in decreasing concentration of SSC and dehydrated in increased ethanol concentration baths. Sections were exposed to Biomax MR films (Kodak, Rochester, USA) for four weeks (Zif268-labeled sections) or 6 weeks (C-Fos-labeled sections) at room temperature. Films were revealed in a dark room. Pictures of each brain section were taken on a Northern light (Imaging Res Inc.) light table with a Qicam (QImaging) camera equipped with a SIGMA 50 mm 1:2.8 DG MacroD Fast 1394 (Nikon) objective and subsequently analyzed with ImageJ software [67 (link)]. A region of interest was drawn for each striatal territory in which the optical density reflective of the mRNA level was measured (according to the rat brain atlas [68 ]). As shown in Supplementary Fig.1A, B , the optical density in an mRNA-free part of the brain (i.e., corpus callosum) was defined as background, and this value was subtracted to that obtained from the area of interest to compute the relative optical density used as the dependent variable in subsequent analyses.
Following fixation and pre-hybridization treatments aiming at reducing non-specific hybridization, slides were incubated overnight at 42 °C in the hybridization buffer (50% deionized formamide, 10% dextran sulfate, 50 ng/ml denaturated salmon sperm DNA, 5% Sarcosyl, 0.2% SDS, 1 mM EDTA, 300 nM NaCl, 5X Denhardt’s in 2X standard sodium citrate (SSC)) with the probes diluted at a concentration of 8.75 ng/ml (C-Fos) or 6.25 ng/ml (Zif268). Slides were then washed in decreasing concentration of SSC and dehydrated in increased ethanol concentration baths. Sections were exposed to Biomax MR films (Kodak, Rochester, USA) for four weeks (Zif268-labeled sections) or 6 weeks (C-Fos-labeled sections) at room temperature. Films were revealed in a dark room. Pictures of each brain section were taken on a Northern light (Imaging Res Inc.) light table with a Qicam (QImaging) camera equipped with a SIGMA 50 mm 1:2.8 DG MacroD Fast 1394 (Nikon) objective and subsequently analyzed with ImageJ software [67 (link)]. A region of interest was drawn for each striatal territory in which the optical density reflective of the mRNA level was measured (according to the rat brain atlas [68 ]). As shown in Supplementary Fig.
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More about "C-fos Genes"
Explore the versatility of C-fos Genes: Uncover the power of PubCompare.ai's AI-driven research protocol optimization to enhance reproducibility in your C-fos Genes studies.
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Empower your C-fos Genes studies and unlock new insights with the help of PubCompare.ai's AI-driven research optimization platform.
Our cutting-edge platform helps you rapidly locate the best protocols from literature, pre-prints, and patents, utilizing intelligent comparisons to identify the most effective methods and products.
Delve into the world of C-fos, a crucial immediate early gene that plays a pivotal role in cellular signaling and gene expression.
Understand how C-fos mRNA and protein levels can serve as markers of neuronal activity and cellular stress response.
Leverage TRIzol reagent, the gold standard for RNA extraction, to isolate high-quality RNA from your C-fos Genes samples.
Complement this with the High-Capacity cDNA Reverse Transcription Kit or the PrimeScript RT reagent kit to generate cDNA for downstream analysis.
Optimize your C-fos Genes expression studies with the RNeasy Mini Kit or the RNeasy Plus Mini Kit, providing efficient and reliable RNA purification.
Utilize the NanoDrop spectrophotometer to assess the quantity and purity of your RNA samples.
Explore TaqMan Gene Expression Assays, designed with Primer Express version 2.0, to accurately quantify C-fos Genes expression levels using real-time PCR.
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