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> Chemicals & Drugs > Amino Acid > 2',3'-Cyclic-Nucleotide Phosphodiesterases

2',3'-Cyclic-Nucleotide Phosphodiesterases

2',3'-Cyclic-Nucleotide Phosphodiesterases are enzymes that catalyze the hydrolysis of the 2',3'-cyclic phosphate bond in cyclic nucleotides, such as cAMP and cGMP.
These enzymes play a key role in regulating the levels of these second messengers within cells, thereby modulating various signaling pathways.
They are involved in a variety of physiological processes, including neurotransmission, smooth musle contraction, and immune function.
Disregulation of 2',3'-Cyclic-Nucleotide Phosphodiesterase activity has been implicated in the pathogenesis of several diseases, making them an important target for pharmaceutical interventins.
Reasearchers can streamline their 2',3'-Cyclic-Nucleotide Phosphodiesteras studies using PubCompare.ai's AI-driven platform to easily locate the best protocols and produts from literature, preprints, and patents using intelligent comparisons, and discover the optimal solutions to advance their research effortlessly.

Most cited protocols related to «2',3'-Cyclic-Nucleotide Phosphodiesterases»

1
Histopathologic Analysis of Inflammation and Demyelination in Mouse CNS
Histopathologic analysis and quantitation of inflammation and demyelination in mouse tissue were performed on cryostat or paraffin sections as described previously (67 (link)). Sections were stained with hematoxylin/eosin and luxol fast blue/nuclear red. Spinal cord sections were fixed with 2% paraformaldehyde for 10 min at 4°C and immunostained with a sheep anti-fibrinogen antibody (1:200; US Biological), rat anti-CD11b (1:5; Chemicon), von Willebrand Factor (1:1,000; DakoCytomation), iNOS (polyclonal; 1:750; Chemicon), Mac-3 (rat anti–mouse; 1:200; BD Biosciences), and CNPase (monoclonal; 1:2,000; Sternberger Monoclonals). The inflammatory index is defined by the average number of inflammatory blood vessels per spinal cord cross section. 10–15 cross sections per animal were counted by two observers blinded to the genotypes of the mice. For the cerebellum, the number of cuffs was quantified in two cerebellar sections per animal. To additionally analyze the CNS lesions, we counted Luxol Fast Blue/nuclear red–stained sections, and the relative proportions of demyelinated areas (percentage with SEM) were determined using an ocular morphometric grid as described previously (67 (link)). For human MS, paraffin-embedded material was obtained from the Archives of the Center for Brain Research, Medical University of Vienna. Double immunofluorescence was performed with antibodies against CD68 and fibrin. Images were collected using an Axioplan 2 Zeiss microscope with an Axiocam HRc camera or were processed for confocal microscopy using Olympus and Zeiss confocal microscopes.
Adams R.A., Bauer J., Flick M.J., Sikorski S.L., Nuriel T., Lassmann H., Degen J.L, & Akassoglou K. (2007). The fibrin-derived γ377-395 peptide inhibits microglia activation and suppresses relapsing paralysis in central nervous system autoimmune disease. The Journal of Experimental Medicine, 204(3), 571-582.
Publication 2007
2',3'-Cyclic-Nucleotide Phosphodiesterases Animals Antibodies Antibodies, Anti-Idiotypic Biopharmaceuticals Brain Cerebellum Demyelination Eosin Eye Factor VIII-Related Antigen Fibrin Fibrinogen Fluorescent Antibody Technique Genotype Homo sapiens Inflammation ITGAM protein, human Luxol Fast Blue MBS Mac-3 Mice, House Microscopy Microscopy, Confocal NOS2A protein, human Paraffin paraform Sheep Spinal Cord Tissues Vasculitis
2
Transcriptional Profiling of Epigenetic Regulators
RNeasy Mini Kit (Qiagen, Ontario, Toronto, Canada) was used for RNA extraction as per the manufacturer’s protocol. Preparation of cDNA and qRT-PCR were carried out as described previously [40 (link)-42 (link)]. Transcript levels of Mecp2 (total), Mecp2e1 [NCBI: NM_001081979.1], Mecp2e2 [NCBI: NM_010788.3], Dnmt genes (Dnmt1, Dnmt3a and Dnmt3b), neuronal genes (Tubulin III (Tub III), NeuN), astrocytic genes (Gfap, S100b), and oligodendrocyte-specific genes (Cnpase, Mbp) were examined by using gene-specific primers (Table 2), as described previously [37 (link),43 (link)]. The relative expression and fold changes were calculated as described previously [37 (link)]. Two-way analysis of variance (ANOVA) and the Student t-test were used to calculate significant differences between untreated control and decitabine-treated samples.
Liyanage V.R., Zachariah R.M, & Rastegar M. (2013). Decitabine alters the expression of Mecp2 isoforms via dynamic DNA methylation at the Mecp2 regulatory elements in neural stem cells. Molecular Autism, 4, 46.
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Publication 2013
2',3'-Cyclic-Nucleotide Phosphodiesterases Astrocytes Decitabine DNA, Complementary DNA Modification Methylases DNMT1 protein, human DNMT3B protein, human Genes Glial Fibrillary Acidic Protein MECP2 protein, human Neurons Oligodendroglia Oligonucleotide Primers Student Tubulin
3
Semiquantitative RT-PCR analysis of mRNA expression
Total RNA was isolated from spinal cord and optic nerves by using a RNeasy mini kit (Qiagen) and from cerebellum by using Ultraspec-II RNA reagent (Biotecx Laboratories) according to the manufacturer’s protocol. To remove any contaminating genomic DNA, total RNA was digested with DNase. Semiquantitative RT-PCR was conducted as described earlier (26 (link), 27 (link)) using a RT-PCR kit from BD Clontech. Briefly, 1 μg of total RNA was reverse transcribed using oligo(dT)12–18 as primer and Moloney murine leukemia virus reverse transcriptase (BD Clontech) in a 20-μl reaction mixture. The resulting cDNA was appropriately diluted and diluted cDNA was amplified using Titanium TaqDNA polymerase and the following primers: VCAM-1: sense, 5′-CAAGGGTGACCAGCTCATGA-3′ and antisense, 5′-TGTGCAGCCACCTGAGATCC-3′; ICAM-1: sense, 5′-CTGGGCTTGGAGACTCAGTG-3′ and antisense, 5′-GTGTCGAGCTTTGGGATGGTA-3′; P-selectin: sense, 5′-ACGAGCTGGACGGACCCG-3′ and antisense, 5′-GGCTGGCACTCAAATTTACAG-3′; iNOS: sense, 5′-CCCTTCCGAAGTTTCTGGCAGCAGC-3′ and antisense, 5′-GGCTGTCAGAGCCTCGTGGCTTTGG3′; IL-1β: sense, 5′-CTCCATGAGCTTTGTACAAGG-3′ and antisense, 5′-TGCTGATGTACCAGTTGGGG-3′; myelin oligodendrocyte glycoprotein (MOG): sense, 5′-CCTCTCCCTTCTCCTCCTTC-3′ and antisense, 5′-AGAGTCAGCACACCGGGGTT-3′; MBP: sense, 5′-TGGAGAGATTCACCGAGGAGA-3′ and antisense, 5′-TGAAGCTCGTCGGACTCTGAG-3′; PLP: sense, 5′-CTTTGCTTCCCTGGTGGCCA-3′ and antisense, 5′-TGTTGGCCTCTGGAACCCCT-3′; CNPase: sense, 5′-CTACCCTCCACGAGTGCAAGA-3′ and anti-sense, 5′-AGTCTAGTCGCCACGCTGTCT-3′; and GAPDH: sense, 5′-GGTGAAGGTCGGTGTGAACG3′ and antisense, 5′-TTGGCTCCACCCTTCAAGTG-3′.
Amplified products were electrophoresed on a 1.8% agarose gel and visualized by ethidium bromide staining. The relative expression of each gene with respect to GAPDH was measured after scanning the bands with a Fluor Chem 8800 Imaging System (Alpha Innotech).
Mondal S., Roy A, & Pahan K. (2009). Functional Blocking Monoclonal Antibodies against IL-12p40 Homodimer Inhibit Adoptive Transfer of Experimental Allergic Encephalomyelitis. Journal of immunology (Baltimore, Md. : 1950), 182(8), 5013-5023.
Publication 2009
2',3'-Cyclic-Nucleotide Phosphodiesterases Cerebellum Deoxyribonucleases DNA, Complementary Ethidium Bromide GAPDH protein, human Gene Expression Genome Intercellular Adhesion Molecule-1 Interleukin-1 beta Moloney Leukemia Virus NOS2A protein, human Oligodendrocyte-Myelin Glycoprotein Oligonucleotide Primers Oligonucleotides Optic Nerve Reverse Transcriptase Polymerase Chain Reaction RNA-Directed DNA Polymerase SELP protein, human Sepharose Spinal Cord Titanium Vascular Cell Adhesion Molecule-1
4
Histological and Immunohistochemical Analyses of Spinal Cord Injury in Mice
On pid-10 or pid-30, mice were euthanized and transcardially perfused with NS (10 ml) followed by 10 % neutral buffered formalin (15 ml). The spinal cords were removed, and 7 μm cryosections or paraffin sections were prepared from the lumbar region.
Fluorescence immunohistochemistry and immuno-Förster resonance energy transfer (immunoFRET) were performed on cryosections from pid-10 and pid-30 using custom anti-Sur1 and anti-Trpm4 antibodies, as described [17 (link)]. Controls for immunoFRET included omission of one of the two primary antibodies. Co-localization analysis was performed using the algorithm in Nikon NIS imaging software, based on regions of interest (400 × 200 μm) positioned in white matter. Specific signals were defined as fluorescence intensity twice that of background. Co-localization of fluorescence signals in double immunolabeled sections was computed as Pearson’s correlation coefficient [28 (link)].
Paraffin sections from pid-30 mice were stained with hematoxylin and eosin (H&E) (for inflammatory cell infiltrates) or Luxol fast blue (LFB) (for demyelination) following standard protocols. Axonal loss was determined by silver nitrate (AgNO3) staining using Hito Bielschowsky OptimStain Kit (#HTKNS1126, Hitobiotec Inc., Wilmington, DE, USA). Slides were examined using bright-field microscopy.
Chromagen immunohistochemistry was performed on paraffin sections from pid-30, as described [29 (link), 30 (link)], using VECTASTAIN Elite ABC Kits (#PK-6100) and Mouse on Mouse (M.O.M.) Elite Peroxidase Kit (#PK-2200) (Vector Laboratories, Burlingame, CA). Primary antibodies were directed against the following: CD45 (1:1500; #ab10558; Abcam, Cambridge, MA); CD3 (1:200; #ab5690; Abcam); CD20 (1:100; #sc-7735; Santa Cruz Biotechnology, Santa Cruz, CA); CD11b (1:800; #NB110-89474; Novus Biologicals, Littleton, CO); TNF-α (1:500; #sc-1350; Santa Cruz Biotechnology); IFN-γ (1:100; #bs-0480R; Bioss, Woburn, MA); IL-17 (1:50; #sc-7927; Santa Cruz Biotechnology); IL-10 (1:50; #sc-1783; Santa Cruz Biotechnology); MBP (1:500; #ab40390; Abcam); CNPase (1:1000; #MAB326; EMD Millipore, Billerica, MA); Olig-2 (1:2000; #MABN50; EMD Millipore); PDGFR-α (1:500; #sc-338; Santa Cruz Biotechnology); and SMI-312 (1:1000; #SMI-312R; Covance Inc., Gaithersburg, MD). Nuclei were counterstained with hematoxylin. The specificity of the immunostaining for all proteins was tested in control slides by incubation with pre-immune serum or after pre-adsorption of the antibody with the respective peptides used as immunogens. Slides were examined using bright-field microscopy.
Quantification of tissue stains and of chromagen immunolabelings was performed by blinded observers using Image J software (NIH, USA). Tissue stains and markers (H&E, LFB, MBP, CNPase, SMI312, AgNO3) were quantified by counting the number of positive/negative quadrants and expressing the percentage over the total number of quadrants examined. All cell labeling experiments were quantified based on an analysis of 8–10 fields per section, randomly positioned in white matter (CD45, CD3, CD20, CD11b, TNF-α, IFN-γ, IL-17, and Olig-2) or in tissues surrounding the central canal (PDGFR-α), with each field being 435 × 325 μm.
Makar T.K., Gerzanich V., Nimmagadda V.K., Jain R., Lam K., Mubariz F., Trisler D., Ivanova S., Woo S.K., Kwon M.S., Bryan J., Bever C.T, & Simard J.M. (2015). Silencing of Abcc8 or inhibition of newly upregulated Sur1-Trpm4 reduce inflammation and disease progression in experimental autoimmune encephalomyelitis. Journal of Neuroinflammation, 12, 210.
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Publication 2015
2',3'-Cyclic-Nucleotide Phosphodiesterases Adsorption Anti-Antibodies Antibodies Antigens Axon Biological Factors Cell Nucleus Cells Cloning Vectors Cryoultramicrotomy Demyelination Eosin Fluorescence Fluorescence Resonance Energy Transfer Formalin Hematoxylin IL10 protein, human IL17A protein, human Immune Sera Immunoglobulins Immunohistochemistry Inflammation Interferon Type II ITGAM protein, human Lumbar Region Luxol Fast Blue MBS Microscopy Mus Novus Paraffin Peptides Peroxidase Proteins Pulp Canals Silver Nitrate Spinal Cord Tissues Tissue Stains Tumor Necrosis Factor-alpha White Matter
5
Western Blot Analysis of Alzheimer's Markers
15–75 μg of protein were resolved on 12% Bis-Tris or 4–12% gradient Bis/Tris gels (Life Technologies) and the proteins were transferred to nylon membranes (Bio-Rad). For Aβ WB analysis, the membranes were cross-linked with 0.5% glutaraldehyde solution before blocking. WB images were visualized by enhanced chemiluminescence (ECL). The images were captured by using BioMax film (Kodak, Rochester, NY, USA) or VersaDoc imaging system (Bio-Rad) and quantitated by using QuantityOne software (Bio-Rad). Primary antibodies were used at the following dilutions: 6E10 anti-Aβ (1:300, Convance), anti-PS1 (1:1,000, Cell Signaling Technology), anti-a-tubulin (1:1,000, Cell Signaling Technology), anti-CNPase (1:1,000, Cell Signaling Technology) and anti-BACE1 (1:1,000, Cell Signaling Technology), C66 APP C-terminal antibody (1:2000), AT8 anti-p-tau (1:100, Millipore), PHF1 anti-p-tau (1:500), anti-total tau (1:2,000, DAKO), anti-MAP2 (1:500, Millipore; 1:200, Cell Signaling), anti-NCAM (1:1000, Cell Signaling), anti-synapsin I (1:500, Cell Signaling), anti-HSP70 (1:1000, Enzo Life Sciences, Farmingdale, NY, USA) and anti-human mitochondrial antigen (h-mito, 1:500, Millipore).
Choi S.H., Kim Y.H., Hebisch M., Sliwinski C., Lee S., D’Avanzo C., Chen J., Hooli B., Asselin C., Muffat J., Klee J.B., Zhang C., Wainger B.J., Peitz M., Kovacs D.M., Woolf C.J., Wagner S.L., Tanzi R.E, & Kim D.Y. (2014). A three-dimensional human neural cell culture model of Alzheimer’s disease. Nature, 515(7526), 274-278.
Publication 2014
2',3'-Cyclic-Nucleotide Phosphodiesterases Antibodies BACE1 protein, human Bistris Chemiluminescence Gels Glutaral H antigen, bacterial Heat-Shock Proteins 70 Homo sapiens Immunoglobulins MAP2 protein, human Mitochondria Mitomycin Neural Cell Adhesion Molecules Nylons PHF1 protein, human Proteins Synapsin I Technique, Dilution Tissue, Membrane Tubulin

Most recents protocols related to «2',3'-Cyclic-Nucleotide Phosphodiesterases»

1
Microglia Isolation and Multiparameter Staining
The microglia were dissociated with trypsin and collected with completed DMEM. Cells were centrifuged at 1500 rpm and resuspended in FACS buffer before being moved to 5 ml of FACS tubes for staining. Microglia cells were incubated in blocking buffer (CD16/32-APC; 1:100; BioLegend) on ice for 10 min to block Fc receptor. Surface antibody cocktails were prepared with CD45/PerCP-Cy5.5 (1:100; BioLegend) and CD11b/APC-Fire 750 (1:100; BioLegend) including viability dye Zombie Aqua. Intracellular staining was performed with MAP2/Alexa Fluor 594 (1:100) and myelin CNPase/Alexa Fluor 647 (1:100).
Ritzel R.M., Li Y., Jiao Y., Lei Z., Doran S.J., He J., Shahror R.A., Henry R.J., Khan R., Tan C., Liu S., Stoica B.A., Faden A.I., Szeto G., Loane D.J, & Wu J. (2023). Brain injury accelerates the onset of a reversible age-related microglial phenotype associated with inflammatory neurodegeneration. Science Advances, 9(10), eadd1101.
Publication 2023
2',3'-Cyclic-Nucleotide Phosphodiesterases Alexa594 Alexa Fluor 647 Buffers Cardiac Arrest Cells Combined Antibody Therapeutics CY5.5 cyanine dye Fc Receptor ITGAM protein, human METAP2 protein, human Microglia Myelin Sheath Protoplasm Trypsin
2
Immunostaining of Microglia and Neural Markers
Microglia were fixed for 20 min with 4% paraformaldehyde in 0.1 M PBS after treatment with neural debris. The cells were rinsed with PBS and incubated sequentially in: (i) blocking solution (PBS containing 5% normal goat serum and 0.1% Triton X-100), (ii) primary antibodies [MAP2 (1:1000; BioLegend, catalog no. 801801), myelin CNPase (1:1000; BioLegend, catalog no. 836404), and Iba-1 (1:500; Cell Signaling Technology, catalog no.17198S)], (iii) PBS, (iv) secondary antibody(ies) [goat anti-mouse Alexa Fluor 546 (1:1000; Invitrogen, catalog no. A11030) and goat anti-rabbit Alexa Fluor 633 (1:1000; Invitrogen, catalog no. A21071)], and (v) DAPI nuclei marker (1:1000; Sigma-Aldrich). Chamber slides were examined with a Leica confocal microscope.
Ritzel R.M., Li Y., Jiao Y., Lei Z., Doran S.J., He J., Shahror R.A., Henry R.J., Khan R., Tan C., Liu S., Stoica B.A., Faden A.I., Szeto G., Loane D.J, & Wu J. (2023). Brain injury accelerates the onset of a reversible age-related microglial phenotype associated with inflammatory neurodegeneration. Science Advances, 9(10), eadd1101.
Publication 2023
2',3'-Cyclic-Nucleotide Phosphodiesterases Aftercare Alexa fluor 546 Antibodies Cell Nucleus Cells DAPI Goat Immunoglobulins METAP2 protein, human Microglia Microscopy, Confocal Mus Myelin Nervousness paraform Rabbits Serum Triton X-100
3
Oligodendrocyte Lineage Analysis by IF
Indirect immunofluorescence was used to identify OPCs (NG2 or PDGFαR-positive cells) and mature (CNPase-positive cells) and myelinating (MBP-positive cells) oligodendrocytes. Cultures were fixed in 4% of cold paraformaldehyde for 15 min and all primary and secondary antibodies used in the present study are listed in Table 1. For AKT/pAKT identification, during fixation a preotease/phosphatase inhibitor cocktail (PMSF 1 mM, sodium floride 10 mM, sodium orthovanadate 1 mM) was added. Cells were also incubated with the nuclear dye Hoechst 33258 (1 μg/mL in PBS, 0.3% Triton-X 100) to identify the nuclei.
For each reaction a control group stained only with secondary antibodies was included to check for specificity.
Baldassarro V.A., Cescatti M., Rocco M.L., Aloe L., Lorenzini L., Giardino L, & Calzà L. (2023). Nerve growth factor promotes differentiation and protects the oligodendrocyte precursor cells from in vitro hypoxia/ischemia. Frontiers in Neuroscience, 17, 1111170.
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Publication 2023
2',3'-Cyclic-Nucleotide Phosphodiesterases Antibodies Cell Nucleus Cells Common Cold Hoechst 33258 Indirect Immunofluorescence Oligodendroglia Orthovanadate paraform Phosphoric Monoester Hydrolases Sodium Triton X-100
4
Quantification of Protein Expression Levels
Protein expression levels of βIII tubulin, 2′,3′-cyclic nucleotide 3′-phosphodiesterase (CNPase), GPNMB, EGFR, c‑Jun NH2‑terminal kinase (JNK)1/2, phosphorylated (p)-JNK1/2 (p-JNK1/2), and nuclear factor κB (NF-κB) p65 were measured by Western blot assay, with glyceraldehyde-3-phosphate dehydrogenase (GAPDH) as the internal reference. Simply put, cells were harvested and extracted by 300 μL RIPA lysis buffer (20-188; Sigma-Aldrich) containing protease and phosphatase inhibitor (P1045; Beyotime, Shanghai, China), followed by the centrifugation for collection of supernatant. Thereafter, concentrations of proteins in the supernatant were measured by a bicinchoninic acid kit (P0011; Beyotime) based on manufacturer’s directions. Subsequently, the proteins with equal weight of 30 µg were electrophoresed on 10% sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and then transferred onto the polyvinylidene fluoride (PVDF) membrane (FFP28; Beyotime). The membrane was blocked with 5% skimmed milk at room temperature for 1 h and then incubated with the primary antibodies at 4℃ overnight. Herein, the varied primary antibodies included anti-βIII tubulin (rabbit, 1:1,000, 50 kDa, ab18207; Abcam, Cambridge, UK), anti-CNPase (rabbit, 1:1,000, 48 kDa, ab250658; Abcam), anti-GPNMB (rabbit, 1:5,000, 120 kDa, ab188222; Abcam), anti-EGFR (rabbit, 1:2,000, 175 kDa, ab52894; Abcam), anti-JNK1/2 (mouse, 1:500, 54 kDa, sc-137019; Santa Cruz, Texas, USA), anti-p-JNK1/2 (rabbit, 1:1,000, 46–54 kDa, ab124956; Abcam), anti-NF-κB p65 (rabbit, 1:1,000, 65 kDa, ab32536; Abcam), anti-p-NF-κB p65 (rabbit, 1:1,000, 65 kDa, ab239882; Abcam), and anti-GAPDH (mouse, 1:500, 36 kDa, ab9484; Abcam). Afterward, the membranes were thereupon incubated with horseradish peroxidase-conjugated secondary antibodies goat anti-rabbit IgG (1:3,000, ab205718; Abcam) and goat anti-mouse IgG (1:3,000, ab6789; Abcam) at room temperature for 2 h. Protein signals were tested and collected via the enhanced chemiluminescence Kit (P0018S; Beyotime) and quantified through ImageJ software (ImageJ 1.8.0; Bethesda, MD, USA).
Yang H., Jin G., Chen S., Luo J, & Xu W. (2023). Glycoprotein non-metastatic melanoma B interacts with epidermal growth factor receptor to regulate neural stem cell survival and differentiation. Open Medicine, 18(1), 20230639.
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Publication 2023
2',3'-Cyclic-Nucleotide Phosphodiesterases Anti-Antibodies anti-IgG Antibodies bicinchoninic acid Buffers Cells Centrifugation Chemiluminescence EGFR protein, human Glyceraldehyde-3-Phosphate Dehydrogenases Goat Hydrolases, Phosphoric Diester IGG-horseradish peroxidase JNK Mitogen-Activated Protein Kinases Milk, Cow's Mus NF-kappa B Nucleotides, Cyclic Peptide Hydrolases Phosphoric Monoester Hydrolases polyvinylidene fluoride Proteins Rabbits Radioimmunoprecipitation Assay SDS-PAGE Tissue, Membrane Tubulin Western Blot
5
Immunofluorescence Staining of Neuronal Cells
Cells were immobilized with 4% precooling paraformaldehyde (P1110; Solarbio, Beijing, China) for 30 min and permeabilized with 0.3% Triton X-100 (T8200; Solarbio) at room temperature for 10 min. After being blocked in 1% bovine serum albumin (BSA; A8020; Solarbio) for 30 min, cells were incubated with primary antibodies including anti-βIII tubulin (1 μg/mL) and anti-CNPase (5 µg/mL) at 4℃ overnight. Post three times of washing in PBS (806552; Sigma-Aldrich), the primary antibodies were identified with Alexa Fluor 594 goat-anti rabbit antibodies (B40925; Invitrogen) for 60-min incubation at room temperature. Subsequently, the nuclei were counter-stained with DAPI (C1002; Beyotime) at 37℃ for 10 min. Ultimately, the slides were mounted and observed under a fluorescence microscope (Leica, TCS SP5II, Germany).
Yang H., Jin G., Chen S., Luo J, & Xu W. (2023). Glycoprotein non-metastatic melanoma B interacts with epidermal growth factor receptor to regulate neural stem cell survival and differentiation. Open Medicine, 18(1), 20230639.
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Publication 2023
2',3'-Cyclic-Nucleotide Phosphodiesterases Alexa594 Anti-Antibodies Antibodies Bos taurus Cell Nucleus Cells DAPI Goat Microscopy, Fluorescence paraform Rabbits Serum Albumin Triton X-100 Tubulin

Top products related to «2',3'-Cyclic-Nucleotide Phosphodiesterases»

1
Cnpase by Abcam
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CNPase (2',3'-Cyclic-nucleotide 3'-phosphodiesterase) is an enzyme that catalyzes the hydrolysis of 2',3'-cyclic nucleotides to 2'-nucleotides. It plays a key role in the maturation and maintenance of myelin sheaths in the central nervous system.
2
Ab6319 by Abcam
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Ab6319 is a primary antibody that targets the protein GAPDH. It is commonly used as a loading control in Western blot experiments to normalize protein expression levels.
3
Cnpase by Merck Group
Sourced in United States, Italy
CNPase is a laboratory reagent used to measure the activity of the enzyme 2',3'-cyclic-nucleotide 3'-phosphodiesterase (CNPase) in biological samples. CNPase is an enzyme involved in the metabolism of myelin, a critical component of the insulating sheath surrounding nerve fibers. The activity of CNPase can provide insights into the state of myelination and neurological processes.
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Glial fibrillary acidic protein (gfap) by Merck Group
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GFAP is a laboratory product that serves as a marker for glial cells, specifically astrocytes, in the central nervous system. It is used in research applications to identify and study these cell types.
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Cnpase by Cell Signaling Technology
Sourced in United States
CNPase is an enzyme that catalyzes the hydrolysis of 2',3'-cyclic nucleotides to 2'-nucleotides. It is a key enzyme involved in the metabolism of cyclic nucleotides in the central nervous system.
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Glial fibrillary acidic protein (gfap) by Agilent Technologies
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GFAP is a laboratory measurement for Glial Fibrillary Acidic Protein, a cytoskeletal protein found in astrocytes and other glial cells in the central nervous system. It serves as a biomarker for neural injury and disease.
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Mab326 by Merck Group
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MAB326 is a laboratory equipment product manufactured by Merck Group. It is designed for use in various scientific and research applications. The core function of MAB326 is to provide a reliable and accurate measurement tool for specific tasks. Further details about its intended use or performance specifications are not available.
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Triton X-100 is a non-ionic surfactant commonly used in various laboratory applications. It functions as a detergent and solubilizing agent, facilitating the solubilization and extraction of proteins and other biomolecules from biological samples.
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Anti-CNPase is a lab equipment product that is used to detect and measure the presence of the enzyme CNPase (2',3'-Cyclic-nucleotide 3'-phosphodiesterase) in biological samples. CNPase is an enzyme involved in the synthesis and maintenance of the myelin sheath in the central nervous system. The Anti-CNPase product provides a reliable and accurate method for researchers to study the role of CNPase in various neurological processes and disorders.

More about "2',3'-Cyclic-Nucleotide Phosphodiesterases"

2',3'-Cyclic-Nucleotide Phosphodiesterases, also known as CNPases, are a class of enzymes that play a crucial role in regulating the levels of cyclic nucleotides, such as cAMP and cGMP, within cells.
These second messengers are vital for various signaling pathways, including neurotransmission, smooth muscle contraction, and immune function.
CNPases catalyze the hydrolysis of the 2',3'-cyclic phosphate bond in cyclic nucleotides, thereby modulating their availability and influencing the downstream effects.
The dysregulation of CNPase activity has been implicated in the pathogenesis of several diseases, making them an important target for pharmaceutical interventions.
Researchers studying CNPases can utilize a wide range of tools and techniques to advance their understanding of these enzymes.
For example, the use of antibodies like Ab6319 and MAB326 can help in the detection and quantification of CNPase levels in biological samples.
GFAP, a marker of glial cells, is often used in conjunction with CNPase to study the role of these enzymes in the central nervous system.
Additionally, the use of detergents like Triton X-100 and the transfer of proteins onto PVDF membranes can facilitate the purification, separation, and analysis of CNPases and their associated proteins.
By streamlining their research using AI-driven platforms like PubCompare.ai, researchers can easily locate the best protocols and products from literature, preprints, and patents, and discover the optimal solutions to advance their CNPase studies effortlessly.