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NOS1 protein, human

The NOS1 protein, human, is an enzyme that catalyzes the production of nitric oxide, a signaling molecule involved in various physiological processes.
It is expressed in the brain, nerves, and other tissues, and has been implicated in neurological disorders, cardiovascular function, and immune response.
Researchers can use PubCompare.ai to identify the most reliable and effective methods for studying the NOS1 protein, optimizing research protocols for reproducibility and accuracy.
Expereincing the power of this AI-powered tool can help advance research into the diverse roles and functions of the NOS1 protein in the human body.

Most cited protocols related to «NOS1 protein, human»

1
Identifying Replicated Cell Types Across Datasets
Cited 18 times
In cases where cell identity was undefined across datasets (i.e., cortical interneuron subtypes) we treated each subtype label as a positive for each other subtype, and assessed similarity using HVGs. For example, Int1 from the Zeisel dataset was used as the positive (training) set, and all other subtypes were considered the test set in turn. Mean AUROCs from both testing and training folds are plotted in the heatmap in Fig. 4. Reciprocal best matches across datasets and AUROCs ≥0.95 were used to identify putative replicated types for further assessment with our supervised framework (detailed above). New cell-type labels encompassing these replicate types (e.g., a combined Sst Chodl label containing Int1 (Zeisel), Sst Chodl (Tasic), and Sst Nos1 (Paul)) were generated for MetaNeighbor across random and GO sets, and for meta-analysis of differential expression. While only reciprocal top hits across laboratories were used to define putative replicate cell types, cross-validation within laboratories was performed to fill in AUROC scores for cell types within each laboratory.
Crow M., Paul A., Ballouz S., Huang Z.J, & Gillis J. (2018). Characterizing the replicability of cell types defined by single cell RNA-sequencing data using MetaNeighbor. Nature Communications, 9, 884.
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Publication 2018
Adrenal Cortex Cells DNA Replication Interneurons NOS1 protein, human
2
Radiation-Induced Organ Damage in Mice
Cited 15 times
All animal experiments and procedures were approved by the Institutional Animal Care and Use Committee (IACUC) at University of Pittsburgh. Experiments were performed on NOS1−/−, NOS2−/−, NOS3−/− and control background strain C57BL/6NHsd mice 6–10 weeks of age.
Thoracic irradiation was administered to female mice by a linear accelerator to a dose of 20 Gy using an established model of radiation-induced organizing alveolitis/fibrosis at around 120–150 days in the C57/B6NHsd mouse (24 (link)). Mice were followed for development of radiation lung damage and survival.
Total-body irradiation (TBI) to the LD50/30 of 9.5 Gy (25 (link)) was delivered to male mice by a 137Cs irradiator (Mark MKI-68, J. L. Shepherd and Associates, San Fernando, CA) at a dose rate of 80 cGy per minute. Mice were followed for development of gastrointestinal and/or hematopoietic syndrome and survival.
Whole-brain irradiation was administered to mice using a linear accelerator to a dose of 9.5 Gy to the head and neck region only. Mice were followed for development of neurological signs or seizures.
Rajagopalan M.S., Stone B., Rwigema J.C., Salimi U., Epperly M.W., Goff J., Franicola D., Dixon T., Cao S., Zhang X., Buchholz B.M., Bauer A.J., Choi S., Bakkenist C., Wang H, & Greenberger J.S. (2010). Intraesophageal Manganese Superoxide Dismutase-Plasmid Liposomes Ameliorates Novel Total-Body and Thoracic Radiation Sensitivity of NOS1−/− Mice. Radiation research, 174(3), 297-312.
Publication 2010
Brain Females Head Hematological Disease Institutional Animal Care and Use Committees Linear Accelerators Males Mice, House Mice, Inbred C57BL Neck Nitric Oxide Synthase Type II NOS1 protein, human NOS3 protein, human Radiation Fibrosis Radiation Pneumonitis Radiotherapy Seizures Strains Whole-Body Irradiation
3
Generating Genetically Modified Mouse Lines
Cited 11 times
We bred all mice in our colony in the Unit for Laboratory Animal Medicine at the University of Michigan. All animals and procedures used were in accordance with the guidelines and with the approval of the University Committee on the Use and Care of Animals. We provided all animals ad libitum access to food and water. We purchased male C57Bl/6J animals for breeding studies and Gt(ROSA)26Sortm1(EYFP)Cos (ROSAEYFP) mice from Jackson Labs. We produced PomcEYFP and AgrpEYFP animals by crossing PomcCre and AgrpCre animals5 (link),36 (link) onto the ROSAEYFP background.
To generate Nos1cre, PCR amplification produced a 6 kb fragment containing the mouse genomic Nos1 sequence centered on the STOP codon in the final (3’) exon for insertion into pCR2.1. PCR mutagenesis created an AscI site 60 bp 3’ to the STOP codon, for the introduction of the IRES-Cre-Frt-Neo-Frt sequences to generate pCRNos1-IRES-Cre-Frt-Neo-Frt. NotI/NheI digestion excised the entire insert for subcloning into NotI/XbaI-cut pPNT backbone to generate pPNT-Nos1-IRES-Cre for targeting. NotI digestion linearized the vector for electroporation into R1 ES cells. We used Taqman-based qPCR screening to initially identify correctly targeted clones37 (link), followed by Southern blotting for final confirmation. We injected correctly targeted ES cells into blastocysts to generate chimeras, which we bred to C57Bl/6 animals to establish germline transmission.
We bred Nos1cre mice with ROSAEGFP mice to generate Nos1cre;ROSAEGFP (Nos1EGFP) animals for the analysis of Nos1cre expression. We also bred Nos1cre animals with Leprfl/fl mice. Due to the periodic expression of Nos1cre during gametogenesis, we bred Nos1cre;leprΔ/+ to Leprfl/fl mice in order to obtain littermate Nos1cre;LeprΔ/fl (LeprNOS1KO), Nos1cre; LeprΔ/+ and LeprΔ/fl (control) and Nos1cre;LeprΔ/Δ (LeprKO) animals for study. We genotyped the offspring by PCR.
Leshan R.L., Greenwald-Yarnell M., Patterson C.M., Gonzalez I.E, & Myers MG J.r. (2012). Leptin action via hypothalamic nitric oxide synthase-1 neurons controls energy balance. Nature medicine, 18(5), 820-823.
Publication 2012
Animals Animals, Laboratory Blastocyst Chimera Cloning Vectors Codon, Terminator Digestion Electroporation Embryonic Stem Cells Exons Food Gametogenesis Genome Germ Line Internal Ribosome Entry Sites Males Mice, House Mice, Laboratory Mutagenesis NOS1 protein, human Pharmaceutical Preparations Rosa Transmission, Communicable Disease Vertebral Column
4
Generating Genetically Modified Mouse Lines
Cited 11 times
We bred all mice in our colony in the Unit for Laboratory Animal Medicine at the University of Michigan. All animals and procedures used were in accordance with the guidelines and with the approval of the University Committee on the Use and Care of Animals. We provided all animals ad libitum access to food and water. We purchased male C57Bl/6J animals for breeding studies and Gt(ROSA)26Sortm1(EYFP)Cos (ROSAEYFP) mice from Jackson Labs. We produced PomcEYFP and AgrpEYFP animals by crossing PomcCre and AgrpCre animals5 (link),36 (link) onto the ROSAEYFP background.
To generate Nos1cre, PCR amplification produced a 6 kb fragment containing the mouse genomic Nos1 sequence centered on the STOP codon in the final (3’) exon for insertion into pCR2.1. PCR mutagenesis created an AscI site 60 bp 3’ to the STOP codon, for the introduction of the IRES-Cre-Frt-Neo-Frt sequences to generate pCRNos1-IRES-Cre-Frt-Neo-Frt. NotI/NheI digestion excised the entire insert for subcloning into NotI/XbaI-cut pPNT backbone to generate pPNT-Nos1-IRES-Cre for targeting. NotI digestion linearized the vector for electroporation into R1 ES cells. We used Taqman-based qPCR screening to initially identify correctly targeted clones37 (link), followed by Southern blotting for final confirmation. We injected correctly targeted ES cells into blastocysts to generate chimeras, which we bred to C57Bl/6 animals to establish germline transmission.
We bred Nos1cre mice with ROSAEGFP mice to generate Nos1cre;ROSAEGFP (Nos1EGFP) animals for the analysis of Nos1cre expression. We also bred Nos1cre animals with Leprfl/fl mice. Due to the periodic expression of Nos1cre during gametogenesis, we bred Nos1cre;leprΔ/+ to Leprfl/fl mice in order to obtain littermate Nos1cre;LeprΔ/fl (LeprNOS1KO), Nos1cre; LeprΔ/+ and LeprΔ/fl (control) and Nos1cre;LeprΔ/Δ (LeprKO) animals for study. We genotyped the offspring by PCR.
Leshan R.L., Greenwald-Yarnell M., Patterson C.M., Gonzalez I.E, & Myers MG J.r. (2012). Leptin action via hypothalamic nitric oxide synthase-1 neurons controls energy balance. Nature medicine, 18(5), 820-823.
Publication 2012
Animals Animals, Laboratory Blastocyst Chimera Cloning Vectors Codon, Terminator Digestion Electroporation Embryonic Stem Cells Exons Food Gametogenesis Genome Germ Line Internal Ribosome Entry Sites Males Mice, House Mice, Laboratory Mutagenesis NOS1 protein, human Pharmaceutical Preparations Rosa Transmission, Communicable Disease Vertebral Column
5
Characterization of Antibodies for Neuroscience Research
Cited 9 times
The nNOS antibody labels a band of 155 kDa in Western blots of rat hypothalamus, and immunostaining is abolished by pre-incubation of the antibody with nNOS (Herbison et al., 1996 (link)). The mouse monoclonal antibody NeuN was raised against cell nuclei extracted from mouse brain and found to react with a protein specific for neurons (Mullen et al., 1992 (link)). We have reported that NeuN apparently labels all neurons but no glial cells in the rat spinal dorsal horn (Todd et al., 1998 (link)). The GABA antibody was raised against GABA conjugated to porcine thyroglobulin with glutaraldehyde, and shown to be specific for GABA, with negligible cross-reactivity against other amino acids, including glutamate, aspartate, glycine or taurine (Pow and Crook, 1993 (link)). The two PKCγ antibodies were raised against peptides corresponding to the C-terminus of mouse PKCγ. The guinea pig antibody recognises a single band of appropriate molecular weight in Western blots of brain homogenates of wild-type, but not PKCγ−/− mice (Yoshida et al., 2006 (link)). The rabbit VGAT antibody is directed against amino acids 75–87 of rat VGAT conjugated to keyhole limpet haemocyanin and stains bands of the appropriate molecular weight in Western blots of rat brain extracts (Takamori et al., 2000 (link)). We have reported that immunostaining in the rat dorsal horn with this antibody is abolished by pre-incubation with the immunising peptide at 10−6 M (Polgár et al., 2011 (link)). The gephyrin antibody was generated against an extract of rat spinal cord synaptic membranes (Pfeiffer et al., 1984 (link)). It has been extensively characterised and shown to bind to a 93 kDa peripheral membrane protein (gephyrin) in extracts of rat brain membranes (Becker et al., 1989 (link)).
Sardella T.C., Polgár E., Watanabe M, & Todd A.J. (2011). A quantitative study of neuronal nitric oxide synthase expression in laminae I–III of the rat spinal dorsal horn. Neuroscience, 192(6-2), 708-720.
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Publication 2011
Amino Acids Antibodies Aspartate Brain Cavia porcellus Cell Nucleus Cross Reactions gamma Aminobutyric Acid gephyrin Glutamate Glutaral Glycine Hypothalamus Immunoglobulins keyhole-limpet hemocyanin Membrane Proteins Mice, House Monoclonal Antibodies Neuroglia Neurons NOS1 protein, human Peptides Pigs Posterior Horn Cells Posterior Horn of Spinal Cord Rabbits SCA14 PKCgamma protein, human Spinal Cord Staining Staphylococcal Protein A Synaptic Membranes Taurine Thyroglobulin Tissue, Membrane Verbascum Western Blot

Most recents protocols related to «NOS1 protein, human»

1
Candidate Gene Screening for Tobacco Mutants
Not available on PMC !

Example 5

Three tobacco lines, FC401 wild type (Wt); FC40-M207 mutant line fourth generation (M4) and FC401-M544 mutant line fourth generation (M4) were used for candidate gene screening. Low anatabine traits were confirmed for the two tobacco mutant lines (M207 and M544) in root and leaf before screening (see FIG. 3).

RNA was extracted from root tissues of wild type (Wt) FC401, M207 and M544 with RNeasy Plus Mini kit from Quiagen Inc. following the manufacturer's protocol. cDNA libraries were prepared from the RNAs using In-Fusion® SMARTer® Directional cDNA Library Construction Kit from Clontech Inc. cDNA libraries were diluted to 100 ng/μl and used as the template for candidate gene PCR screening.

PCR amplifications were performed in 50 μl final volumes that contained 50-100 ng of template DNA (i.e., the cDNA library) and 0.2 μM of primers (Fisher Scientific) using the Platinum® Taq DNA Polymerase High Fidelity kit (Life Technology Inc.). Thermocycling conditions included a 5 min incubation at 94° C.; followed by 34 cycles of 30 seconds at 94° C., 30 seconds at 58° C., 1 min 30 seconds at 68° C.; with a final reaction step of 68° C. for 7 mins. The PCR products were evaluated by agarose gel electrophoresis, and desired bands were gel purified and sequenced using an ABI 3730 DNA Analyzer (ABI).

51 candidate genes (listed in Table 4) were cloned from F401, Wt, M207 and M544 lines, and sequenced for single nucleotide polymorphism (SNP) detection.

TABLE 4
Listing of Candidate Genes for Screening
Quinolinate Synthase A-1Pathogenesis related protein 1
Allene oxide synthaseAllene oxide cyclase
ET861088.1 Methyl esteraseFH733463.1 TGACG-sequence specific transcription factor
FH129193.1 Aquaporin-TransportFH297656.1 Universal stress protein
Universal stress protein Tabacum sequenceFH077657.1 Scarecrow-like protein
FH864888.1 EIN3-binding F-box proteinFH029529.1 4,5 DOPA dioxygenase
FI010668.1 Ethylene-responsive transcription EB430189 Carboxylesterase
factor
DW001704 Glutathione S transferaseEB683763 Bifunctional inhibitor/lipid transfer protein/seed
storage 2S albumin
DW002318 Serine/threonine protein kinaseDW004086 Superoxide dismutase
DW001733 Lipid transfer protein DIRIDW001944 Protein phosphatase 2C
DW002033EB683763 Bifunctional inhibitor/lipid transfer protein/seed
storage 2S albumin
DW002318 Serine/threonine protein kinaseDW002576 Glycosyl hydrolase of unknown function DUF1680
EB683279EB683763
EB683951FG141784 (FAD Oxidoreductase)
BBLa-Tabacum sequencesBBLb
BBLeBBLd
PdrlPdr2
Pdr3Pdr5a
Pdr5bNtMATEl
NtMATE2NtMATE3
WRKY8EIG-I24
WRKY3WRKY9
EIG-E17AJ748263.1 QPT2 quinolinate phosphoribosyltransferase
AJ748262.1 QPT1

US11873500B2. Genetic locus imparting a low anatabine trait in tobacco and methods of using (2024-01-16). ALTRIA CLIENT SERVICES LLC [US]. Inventors: Chengalrayan Kudithipudi [US], Alec J. Hayes [US], Robert Frank Hart [US], Yanxin Shen [US], Jesse Frederick [US], Dongmei Xu [US].
Full text: Click here
Patent 2024
Albumins allene oxide cyclase allene oxide synthase Amino Acid Sequence anatabine Carboxylesterase cDNA Library Dioxygenases Dopa Electrophoresis, Agar Gel Esterases Ethylenes Genes Glutathione S-Transferase Heat Shock Proteins Histocompatibility Testing Hydrolase lipid transfer protein Neoplasm Metastasis Nicotiana Nicotinate-nucleotide pyrophosphorylase (carboxylating) NOS1 protein, human Oligonucleotide Primers Oxidoreductase pathogenesis Plant Leaves Plant Roots Platinum Protein-Serine-Threonine Kinases Protein-Threonine Phosphatase Protein Kinases protein methylesterase Protein Phosphatase Protein Phosphatase 2C Proteins Quinolinate RNA Single Nucleotide Polymorphism Superoxide Dismutase Synapsin I Taq Polymerase Transcription, Genetic Transcription Factor Transfer Factor Water Channel
2
Genetic Regulation of Nitric Oxide Signaling
Animal procedures were approved by the National Institute of Diabetes and Digestive and Kidney Diseases Animal Care and Use Committee and carried out in accordance with the National Institutes of Health Guidelines for the Care and Use of Laboratory Animals. Mice were maintained under a specific pathogen–free and thermostable environment (23°C) and photoperiod conditions (12/12 h light/dark cycle) with free access to food (NIH-31, 14% kcal/fat, 3.0 kcal/g, Teklad Diets) and water. All mice were on a C57BL/6 background. eNOS−/− mice and nNOS−/− mice were purchased from Jackson Laboratory (stock no. 002684 and 002986, respectively). nNOS−/− mice were bred by mating heterozygous females to homozygous males or by mating homozygous females to heterozygous males. Mouse genotype was determined at weaning by PCR analysis of extracted DNA. Pep Boy with CD45.2 mice (Jackson Laboratory, stock no. 002014) were used as recipient mice for bone marrow transplantation.
Lee J., Dey S., Rajvanshi P.K., Merling R.K., Teng R., Rogers H.M, & Noguchi C.T. (2023). Neuronal nitric oxide synthase is required for erythropoietin stimulated erythropoiesis in mice. Frontiers in Cell and Developmental Biology, 11, 1144110.
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Publication 2023
Animals Animals, Laboratory Bone Marrow Transplantation Diabetes Mellitus Diet Digestive System Females Food Genotype Heterozygote Homozygote Kidney Diseases Males Mice, House NOS1 protein, human NOS3 protein, human Specific Pathogen Free
3
Effect of nNOS Inhibitor on Erythroleukemia Cells
EPO-dependent murine HCD57 erythroleukemia cells were grown in Iscove’s modified Dulbecco’s medium (IMDM), 25% fetal bovine serum (FBS), 10 μg/mL gentamicin (Invitrogen, Thermo Fisher Scientific, Grand Island, NY, United States), at 37°C in a 5% CO2 environment with either 0.2 U/mL or 2 U/mL EPO (Amgen, Thousand Oaks, CA, United States) (Sawyer and Jacobs-Helber, 2000 (link)). The human K562 chronic myeloid leukemia cell line was cultured in RPMI 1640 medium, 10% fetal bovine serum (FBS), and 1% Penicillin/Streptomycin (Invitrogen) at 37°C with 5% CO2. To investigate the effect of nNOS inhibitor, HCD57 and K562 cells were cultured with nNOS inhibitor, 7-Nitroindazole (7-NI; #00240 Biotium, Fremont, CA, United States) at different concentrations (10, 100, 200 μM). HCD57 cells were harvested at day 4 for analysis of gene and protein expression. For erythroid differentiation of K562 cells, cells were stimulated with 30 μM of hemin (Millipore Sigma, St. Louis, MO, United States).
Lee J., Dey S., Rajvanshi P.K., Merling R.K., Teng R., Rogers H.M, & Noguchi C.T. (2023). Neuronal nitric oxide synthase is required for erythropoietin stimulated erythropoiesis in mice. Frontiers in Cell and Developmental Biology, 11, 1144110.
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Publication 2023
7-nitroindazole Acute Erythroblastic Leukemia Cell Lines Cells Culture Media Differentiations, Cell Fetal Bovine Serum Genes Gentamicin Hemin Homo sapiens K562 Cells Leukemias, Chronic Granulocytic Mus NOS1 protein, human Penicillins Proteins Quercus Streptomycin
4
Busulfan Conditioning and Bone Marrow Transplantation
Recipient female Pep Boy (CD45.2) mice at 8–10 weeks received 20 mg/kg of pharmaceutical grade busulfan by intraperitoneal injection (Hayakawa et al., 2009 (link)) 1 day prior to transplantation. Bone marrow cells were collected from female WT and nNOS−/− mice at 8–10 weeks and were infused by direct injection intravenously into the tail vein of Pep Boy mice. After 11–12 weeks following transplantation, blood was drawn from the recipient Pep Boy mice by nicking of the tail vein to analyze engraftment rate. Mice were then treated with EPO (Amgen, Thousand Oaks, CA, United States) at 3,000 units/kg three times/week for 1 week and hematocrit levels were determined.
Lee J., Dey S., Rajvanshi P.K., Merling R.K., Teng R., Rogers H.M, & Noguchi C.T. (2023). Neuronal nitric oxide synthase is required for erythropoietin stimulated erythropoiesis in mice. Frontiers in Cell and Developmental Biology, 11, 1144110.
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Publication 2023
BLOOD Bone Marrow Cells Busulfan Females Injections, Intraperitoneal Mus NOS1 protein, human Pharmaceutical Preparations Quercus Tail Transplantation Veins Volumes, Packed Erythrocyte
5
Immunoblotting of Cardiac Proteins
Immunoblotting in LV homogenates was performed to evaluate protein levels of GTPCH (1:10,000 dilution; a gift from S.Gross, Cornell University; New York), iNOS (1: 1,100 dilution; Abcam), nNOS (1:1,000 dilution; Santa Cruz Biotechnology), eNOS (1:5,000 dilution; BD Bioscience), CD102 (1:1,000; R&D systems), SERCA2A (1:5,000 dilution; Santa Cruz Biotechnology), total phospholamban (1:2,000 dilution; PLB, Badrilla), phosphor-Thr17-PLB (1:2,000 dilution; Badrilla), phosphor-Ser16-PLB (1:2,000 dilution; Badrilla), NCX1 (1:1,000 dilution, Santa Cruz), phospho-extracellular signal-regulated protein kinases (1:500 dilution; ERK1/2), total ERK1/2 (1:500 dilution;), catalase (1:5,000 dilution; Calbiochem), MnSOD (1:5,000 dilution; Stressgen Bioreagents), EcSOD (1:750 dilution; Stressgen Bioreagents), Cu/ZnSOD (1:500 dilution; Stressgen Bioreagents), and β-tubulin (1:20,000; Abcam), followed by appropriate HRP-conjugated secondary antibody (1:10,000–20,000 dilution; Promega). Protein bands were visualized by enhanced chemiluminescence (Super West Pico Chemiluminescence, Thermo Scientific).
Chuaiphichai S., Chu S.M., Carnicer R., Kelly M., Bendall J.K., Simon J.N., Douglas G., Crabtree M.J., Casadei B, & Channon K.M. (2023). Endothelial cell-specific roles for tetrahydrobiopterin in myocardial function, cardiac hypertrophy, and response to myocardial ischemia-reperfusion injury. American Journal of Physiology - Heart and Circulatory Physiology, 324(4), H430-H442.
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Publication 2023
Catalase Chemiluminescence Immunoglobulins Mitogen-Activated Protein Kinase 3 Mitogen-Activated Protein Kinases NOS1 protein, human NOS2A protein, human NOS3 protein, human phospholamban Phosphorus Promega Proteins SOD2 protein, human Technique, Dilution Tubulin

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More about "NOS1 protein, human"

The NOS1 (Nitric Oxide Synthase 1) protein, also known as neuronal nitric oxide synthase (nNOS), is a crucial enzyme found in the human body.
It plays a pivotal role in the production of nitric oxide (NO), a versatile signaling molecule involved in various physiological processes.
NOS1 is primarily expressed in the brain, nerves, and other tissues, and has been implicated in a wide range of functions, including neurological disorders, cardiovascular function, and immune response.
Researchers can utilize advanced tools like PubCompare.ai to identify the most reliable and effective methods for studying the NOS1 protein.
This AI-powered platform allows researchers to optimize their research protocols for reproducibility and accuracy, ensuring that their findings are robust and reliable.
By comparing protocols from literature, preprints, and patents, researchers can locate the best approaches for investigating the diverse roles and functions of the NOS1 protein.
When studying the NOS1 protein, researchers may employ various techniques and reagents, such as TRIzol reagent for RNA extraction, β-actin as a reference gene, the RNeasy Mini Kit for purifying RNA, PVDF membranes and Hybond for Western blotting, and antibodies like Ab76067 for detecting the NOS1 protein.
Additionally, the High-Capacity cDNA Reverse Transcription Kit can be used to convert RNA into cDNA, which can then be analyzed using techniques like real-time PCR.
Lipofectamine 2000 is a common transfection reagent used to introduce genetic material into cells for studying the NOS1 protein.
By leveraging the insights and capabilities of tools like PubCompare.ai, researchers can optimize their research protocols, improve the reproducibility and accuracy of their findings, and advance our understanding of the diverse roles and functions of the NOS1 protein in the human body.
Expereincing the power of this AI-powered tool can help researchers unlock new avenues of discovery and drive progress in the field of nitric oxide signaling and its implications for human health and disease.