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Nycodenz

Nycodenz is a high-density gradient medium used for the separation and purification of cells, organelles, and other biological macromolecules.
It is a non-ionic, water-soluble compound that creates a density gradient when centrifuged, allowing the target molecules or structures to be isolated based on their unique densities.
Nycodenz is commonly employed in techniques such as gradient centrifugation, cell fractionation, and organelle isolation, making it a valuable tool for researchers studying cellular and subcellular components.
The PubCompare.ai platform can help optimize Nycodenz research protocols by providing easy access to literature, pre-prints, and patent data, enabling researchers to identify the best protocols and products for their specific needs and save time on manual searching and comparisons.

Most cited protocols related to «Nycodenz»

Isolation and Characterization of Intestinal and Splenic Dendritic Cells

Cited 17 times

For LpDCs, total Lp cells after digestion with Liberase CI were passed through 70- and 40-μm cell strainers. Cells were resuspended in 1.077 g/cm³ iso-osmotic NycoPrep medium (Accurate Chemical & Scientific Corp.), and the low-density fraction was collected after centrifugation at 1,650 g for 15 min. Nycodenz gradient excludes debris and red blood cells and decreases lymphocyte numbers without changing the composition of the different subsets of LpDC (Fig. S5, available at http://www.jem.org/cgi/content/full/jem.20070663/DC1). Cells were washed and incubated with a mixture of mAb containing α−CD11c (HL-3), α−MHC II (AF6-120.1), α−CD16/32 (2.4G2), and α−CD103 mAb (2E7), as well as the non-DC components α−DX5 (DX5), α-NK1.1 (PK136), and α−B220 (RA3-6B2, all from eBioscience). DCs were defined as CD11c⁺MHCII⁺ cells and non-DCs were excluded when sorted by flow cytometry on a FACSVantage or FACSAria. In some experiments, CD103⁺ and CD103⁻ DCs were separated. Purity was verified by flow cytometry on a FACSCalibur. I-A^b+CD11c⁺ cells were >90%.
For SpDCs, spleens were cut into fragments and digested by 100 mg/ml Liberase CI and 150 mg/ml DNase I, and then dissociated in Ca²⁺-free medium in the presence of EDTA. IA^b+CD11c⁺ SpDCs were further purified for LpDCs, resulting in >98% purity. For phenotypic analysis, I-A^b+CD11c⁺ DCs were stained with fluorescent dye-conjugated α-CD11b (M1/70), α-CD103 (2E7; all from eBioscience), α-CD40 (3/23), α-CD80 (16-10A) (1 (link)), and α-CD86 (GL-1; all from BD Biosciences) mAb and analyzed by flow cytometry on a FACSCalibur or LSR II (BD Biosciences).

Sun C.M., Hall J.A., Blank R.B., Bouladoux N., Oukka M., Mora J.R, & Belkaid Y. (2007). Small intestine lamina propria dendritic cells promote de novo generation of Foxp3 T reg cells via retinoic acid. The Journal of Experimental Medicine, 204(8), 1775-1785.

Publication 2007

alpha HML-1 Cells Centrifugation Chief Cells, Gastric Deoxyribonucleases Edetic Acid Erythrocytes Flow Cytometry Fluorescent Dyes ITGAM protein, human Liberase Lymphocyte Count Nycodenz Osmosis Phenotype

Quantifying Malaria Parasite Sexual Differentiation

Cited 10 times

Sexual differentiation was induced in tightly synchronized P. falciparum parasites (28±2 hpi) by incubating the cells for 22 hours in CM (220 μL per well of a 96-well plate; 0.3-0.5% parasitemia; 2.5% hematocrit) or in −SerM as described (Brancucci et al., 2015 (link)). If not stated otherwise, cell line Pf2004/164tdTom was used for all experiments. To determine the effect of culture perturbations on sexual commitment, serum fractions as well as nutrients or inhibitor compounds (solved in either RPMI, DMSO, chloroform, ethanol or methanol) were added to the bottom of empty wells (glass bottom dishes were used for chloroform-containing samples) and directly resuspended in parasite culture after allowing volatile solvents to evaporate. To determine sexual differentiation in reticulocyte-enriched blood, tightly synchronized parasites were magnet purified at 46±2 hpi using MACS CS columns in a SuperMACS (Miltenyi Biotec) before incubating pure schizont-infected erythrocytes (>99%) with the blood sample to be tested. These culture perturbations were then tested for effects on parasite sexual differentiation as described (Brancucci et al., 2015 (link)). In brief, following the 22 hour testing phase (see above), cells of each well were washed 3 times in 200 μL +SerM medium before being resuspended in 220 μL +SerM medium. Henceforth, medium was exchanged daily. Parasitemia and gametocytemia was quantified using flow cytometry at 20-30 hpi (MACS Quant, Analyzer 10) and 72-96 hpi (BD Fortessa), respectively. Cytometry data were analysed using FlowJo software and sexual differentiation rates were determined by dividing gametocytemia of each well with the corresponding parasitemia measurements. Assays were run in biological triplicates. Each biological replicate contained technical triplicates.
P. berghei sexual commitment assays were performed using a parasite line expressing an RFP reporter under the gametocyte-specific gene PBANKA_1018700 (Sinha et al., 2014 (link)) and GFP under the constitutive PBANKA_0905600 promoter, in the 507cl1 background line (RMgm-7). Mature schizonts were intravenously (IV) administered to naïve TO mice. Ring stage parasites were isolated at 4 hpi and mature trophozoites and gametocytes were removed by passing through a MACS LD column (Miltenyi Biotec). Infected erythrocytes were incubated in −SerM medium, −SerM medium supplemented with 20 μM LysoPC (−SerM/LysoPC), or serum-complemented medium (+SerM) for 20 hours. Mature schizont stage parasites were then isolated on a 55% Nycodenz (Axis-Shield POC)/RPMI gradient and injected intravenously into 2 or 3 naïve mice. GFP-expressing cells were examined by flow cytometry at 16 hpi to calculate parasitemia, while cells expressing both RFP and GFP (gametocytes) were assessed at 21 hpi. Gametocytemia was calculated as [(RFP⁺ and GFP⁺ cells)/GFP⁺ cells]^∗100.

Brancucci N.M., Gerdt J.P., Wang C., De Niz M., Philip N., Adapa S.R., Zhang M., Hitz E., Niederwieser I., Boltryk S.D., Laffitte M.C., Clark M.A., Grüring C., Ravel D., Blancke Soares A., Demas A., Bopp S., Rubio-Ruiz B., Conejo-Garcia A., Wirth D.F., Gendaszewska-Darmach E., Duraisingh M.T., Adams J.H., Voss T.S., Waters A.P., Jiang R.H., Clardy J, & Marti M. (2017). Lysophosphatidylcholine Regulates Sexual Stage Differentiation in the Human Malaria Parasite Plasmodium falciparum. Cell, 171(7), 1532-1544.e15.

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Publication 2017

Biological Assay Biopharmaceuticals BLOOD Cell Lines Cells Chloroform DNA Replication Epistropheus Erythrocytes Ethanol Flow Cytometry Genes, Reporter Hyperostosis, Diffuse Idiopathic Skeletal LY353381hydrochloride LYSO-PC Methanol Mus Nutrients Nycodenz Parasitemia Parasites Reticulocytes Schizonts Selective Estrogen Receptor Modulators Serum Sex Differentiation Solvents Sulfoxide, Dimethyl Trophozoite Volumes, Packed Erythrocyte

Fecal Microbiota Separation and Extraction

Cited 10 times

A part of each stool sample was submitted to a density gradient in order to separate the microbiota from the rest of the fecal material, according to the method of Courtois and colleagues with some modifications25 (link). Two grams of feces were homogenized in 18 mL of sterile NaCl 0.9% (w/v), in a laboratory paddle blender (Stomacher Lab Blender 400, Seward Ltd. UK) for 1 min. A solution of Nycodenz® 80% (w/v) (PROGEN Biotechnik GmbH, Heidelberg, Denmark) was prepared in ultrapure water, and sterilized at 121 °C for 15 min. A volume of 10.5 mL of the diluted, homogenized fecal sample was placed on top of 3.5 mL of the Nycodenz® solution, and centrifuged for 40 min at 4 °C (10,000 × g, TST41.14 rotor, Kontron, Milan, Italy). The upper phase, containing soluble debris, was discarded after the centrifugation step, and the layers corresponding to the microbiota extracted with 10.5 mL of PBS (Fig. 1) were collected. Cellular suspensions were kept on ice for 5 minutes, in order to allow non-soluble debris to precipitate, were then washed twice, and stored in aliquots of 1 mL, at −80 °C, until DNA extraction was performed. In all the cases, DNA directly from homogenized stool samples, or from the corresponding separated microbiota fractions was extracted using the QIAamp DNA Stool Mini kit (Qiagen Ltd., Strasse, Germany), as described in a previous work26 (link).

Hevia A., Delgado S., Margolles A, & Sánchez B. (2015). Application of density gradient for the isolation of the fecal microbial stool component and the potential use thereof. Scientific Reports, 5, 16807.

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Publication 2015

Cells Centrifugation Feces Microbial Community Normal Saline Nycodenz Progens Sterility, Reproductive

Isolation and Purification of Lung Dendritic Cells

Cited 10 times

Lungs were extracted, minced, and digested with Liberase TM (100 μg ml⁻¹; Roche, Indianapolis, IN), together with collagenase XI (250 μg ml⁻¹), hyaluronidase 1a (1 mg ml⁻¹), and DNase I (200 μg ml⁻¹; Sigma, St Louis, MO) for 1 h at 37°C. Minced mediastinal LNs were digested with the same enzymes for 30 min. In some experiments, lung tissues were digested with collagenase D (1 mg ml⁻¹) (Roche) and DNase I (200 μg ml⁻¹). The reaction was stopped by the addition of EDTA (20 mM final concentration). A single-cell suspension was prepared by sieving the digested tissue through a 70 μm nylon strainer (BD Biosciences, Bedford, MA). DCs were enriched by discontinuous phase-density centrifugation with 16 % Nycodenz (Accurate Chemical, Westbury, NY), and then washed with phosphate-buffered saline containing 0.5 % bovine serum albumin and 2 mM EDTA. DC numbers per lung were calculated based on the total number of recovered cells and the percentages of DCs in those preparations. Total CD11c^hi DCs or DC subsets were purified by sorting on a fluorescence-activated cell sorting Vantage or fluorescence-activated cell sorting ARIA-II flow cytometer (BD Biosciences). Purity was consistently > 98 %. Cell morphologies were assessed by light microscopy following centrifugation onto glass slides. Antigens were delivered to the airway by oropharyngeal aspiration, and DCs harvested 16 or 24 h later. The following antigens were instilled in a total volume of 50 μl phosphate-buffered saline; 100 μg endotoxin-free OVA (Profos AG, Regensburg, Germany); 10 μg cockroach antigens (Greer, Lenoir, NC); and 10 μg house dust mite (Greer). LPS was removed from CA using ProteoSpin endotoxin removal kit (Norgen Biotek, Thorold, ON, Canada). Unless stated otherwise, OVA was delivered to the airways together with 10 pg LPS (Sigma). In some experiments, 1 μg poly I:C (Invivogen, San Diego, CA) was used as the adjuvant. For allergen tracking experiments, OVA, CA, and HDM were labeled with Alexa Fluor-647 (Invitrogen, Carlsbad, CA).

Nakano H., Free M., Whitehead G., Maruoka S., Wilson R., Nakano K, & Cook D. (2011). Pulmonary CD103+ dendritic cells prime Th2 responses to inhaled allergens. Mucosal immunology, 5(1), 53-65.

Publication 2011

Alexa Fluor 647 Allergens Antigens Cells Centrifugation Cockroaches Collagenase collagenase 1 Deoxyribonuclease I Dermatophagoides pteronyssinus Edetic Acid Endotoxins Enzymes Hyaluronidase Liberase Light Microscopy Lung Mediastinum NRG1 protein, human Nycodenz Nylons Oropharynxs Pharmaceutical Adjuvants Phosphates Poly I-C Saline Solution Serum Albumin, Bovine Tissues

Efficient Extraction and Purification of Microbial Cells from Sediment

Cited 8 times

Sediment slurry (250 μl) was diluted with 150 μl of 2.5% NaCl solution, and 50 μl of detergent mix [100 mM EDTA, 100 mM sodium pyrophosphate, 1% (v/v) Tween 80] and 50 μl methanol were added. Next, the sample was vigorously shaken for 60 min at 500 r.p.m. using a Shake Master (Bio Medical Science, Tokyo, Japan). After shaking, the sediment slurry was sonicated at 20 W for 1 min using a Model UH-50 Ultrasonic Homogenizer (SMT, Tokyo, Japan), and then carefully layered onto a high-density cushion solution. Either 50% (w/v) Nycodenz (Kallmeyer et al., 2008 ) or various combinations of 50–80% (w/v) Nycodenz and 40–80% (w/v) sodium polytungstate were used to prepare the high-density solutions. Samples were centrifuged at either 4500× g or 15 000× g for 15–300 min, after which the supernatant, including the high-density layer(s), was carefully removed and transferred to a separate vial. Next, 900 μl of 2.5% NaCl solution was added to the remaining high-density solution and sediment pellet, which was resuspended and centrifuged again at 5000× g for 15 min. The resulting supernatant was also transferred to a separate vial. The remaining pellet was resuspended in 100 μl of 1% hydrofluoric acid and allowed to stand for 20 min. The reaction was stopped by adding 100 μl of 1.5 M Tris-base, and the sample was shaken again for 10 min after addition of 150 μl of 2.5% NaCl solution and 50 μl each of detergent mix and methanol. The vial was then sonicated in a water bath for 30 s, and layering onto the high-density solution and subsequent centrifugation steps were repeated as described above.

Morono Y., Terada T., Kallmeyer J, & Inagaki F. (2013). An improved cell separation technique for marine subsurface sediments: applications for high-throughput analysis using flow cytometry and cell sorting. Environmental Microbiology, 15(10), 2841-2849.

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Publication 2013

Bath Centrifugation Detergents Edetic Acid Hydrofluoric acid Methanol Nycodenz Sodium Sodium Chloride sodium pyrophosphate Tromethamine Tween 80 Ultrasonics

Most recents protocols related to «Nycodenz»

Purification of P. berghei Ookinetes

Ookinetes were produced using the P. berghei line PbRFP, a P. berghei ANKA line that constitutively expresses RFP. Two female Swiss mice were injected intraperitoneally with 200 µl phenylhydrazine (6 mg/ml in PBS) to stimulate reticulocytosis. Two days later, the mice were infected intraperitoneally with 20*10⁶ iRBC PbRFP. Mice were bled three days post infection and 500 µl blood was transferred to 10 ml ookinete medium (RPMI supplemented with 20% (v/v) FCS, 50 µg/ml hypoxanthine, and 100 µM xanthurenic acid, adjusted to pH 7.8 – 8.0) at 19 °C. After 22 h of culture, ookinete cultures were underlaid with 5 ml 55% Nycodenz/PBS and centrifuged for 25 min at 210 xg without brake. The interphase containing purified ookinetes was collected, washed in PBS and immediately plunge frozen for EM.

Ferreira J.L., Pražák V., Vasishtan D., Siggel M., Hentzschel F., Binder A.M., Pietsch E., Kosinski J., Frischknecht F., Gilberger T.W, & Grünewald K. (2023). Variable microtubule architecture in the malaria parasite. Nature Communications, 14, 1216.

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Publication 2023

BLOOD Females Freezing Hypoxanthine Infection Interphase Mouse, Swiss Mus Nycodenz phenylhydrazine xanthurenic acid

Isolation and Culture of Hepatic Stellate Cells

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Publication 2023

Anesthesia Cells Collagenase Culture Media G-800 Hepatocyte Ketamine Liver Mus Nycodenz Pronase Stem Cells, Hematopoietic Vena Cavas, Inferior

Isolation and Analysis of Liver Immune Cells

We isolated primary hepatocytes and NPCs as previously described (20 (link), 49 (link)). Briefly, we anesthetized mice and digested livers by perfusion of EGTA buffer and collagenase buffer (MilliporeSigma, C5138) through the inferior vena cava, purified hepatocytes with Percoll, and concentrated the remaining NPCs by Nycodenz density centrifugation. We analyzed NPCs by multicolor flow cytometry using an LSRFortessa (BD Biosciences). Briefly, we centrifuged isolated cells at 450g for 5 minutes at 4°C, washed in cold staining buffer (PBS, 2% BSA), resuspended 1 × 10⁶ to 10 × 10⁶ NPCs in Zombie Aqua Fixable Viability Dye (BioLegend, 423101) diluted 1:1,000 in PBS, and then incubated for 15–30 minutes at room temperature in the dark. After another wash, we incubated NPCs with TruStain FcX Fc receptor blocker (BioLegend, 101319) for 5 minutes, then with fluorochrome-conjugated antibodies against mouse CD45 (BioLegend, 103157), CD11b (BioLegend, 101239), CD11c (BioLegend, 117329), Ly6C (BioLegend, 128011), Ly6G (BioLegend, 127617), F4/80 (BioLegend, 123130), CD3 (BioLegend, 100236), B220 (BioLegend, 103224), and NK1.1 (BioLegend, 156508) diluted at 1:200 for 20 minutes at 4°C in staining buffer. Gating strategy is shown in Supplemental Figure 1. After staining, we fixed cells with 4% paraformaldehyde for 15 minutes at room temperature, washed, and then resuspended in staining buffer prior to sample acquisition. Total NPCs were further fractionated by FACS, using vitamin A fluorescence of HSCs as previously described (49 (link)), or antibody-based cell sorting of lymphoid cells with CD45-APC (BD Biosciences, 559864), myeloid cells with CD11b-FITC (BD Biosciences, 553310), and cholangiocytes with EpCAM-PE (Invitrogen, 12579182). We analyzed data using FCS Express7 (De Novo Software).

Kang J., Postigo-Fernandez J., Kim K., Zhu C., Yu J., Meroni M., Mayfield B., Bartolomé A., Dapito D.H., Ferrante AW J.r., Dongiovanni P., Valenti L., Creusot R.J, & Pajvani U.B. (2023). Notch-mediated hepatocyte MCP-1 secretion causes liver fibrosis. JCI Insight, 8(3), e165369.

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Publication 2023

Antibodies Buffers Cells Centrifugation Cold Temperature Collagenase Egtazic Acid Fc Receptor Flow Cytometry Fluorescein-5-isothiocyanate Fluorescence Fluorescent Dyes Hepatocyte Immunoglobulins ITGAM protein, human Liver Lymphoid Cells Mus Myeloid Cells Nycodenz paraform Percoll Perfusion Stem Cells, Hematopoietic TACSTD1 protein, human Vena Cavas, Inferior Vitamin A

Quantifying Female Gamete Antibody Binding

In vitro cultured Plasmodium falciparum NF54 gametocytes were activated to generate female gametes, which were purified with Nycodenz.⁶⁹ (link) Per condition 10,000 female gametes were incubated with monoclonal antibodies diluted in SIFA buffer (1% heat-inactivated FCS, 0.05% sodium azide in PBS) for 1 h at 4 ˚C. Samples were washed 3 times with SIFA buffer. Gametes were stained with Hoechst 33342 DNA stain (1:200 dilution) (Invitrogen, cat no. H3570) and anti-human IgG-AF488 (1:400 dilution) (Invitrogen, cat no. A-11013) for 1 h at 4 ˚C in the dark. Gametes were then washed 3 times with SIFA buffer, fixed with 4% paraformaldehyde and imaged with an ImageXpress Pico automated cell imaging system (Molecular devices). Gametes were then analyzed with MetaXpress software (Molecular devices). Hemozoin and Hoechst-positive gametes were selected and positivity for human antibodies was determined using signal from negative control antibodies as a threshold.

Ivanochko D., Fabra-García A., Teelen K., van de Vegte-Bolmer M., van Gemert G.J., Newton J., Semesi A., de Bruijni M., Bolscher J., Ramjith J., Szabat M., Vogt S., Kraft L., Duncan S., Lee S.M., Kamya M.R., Feeney M.E., Jagannathan P., Greenhouse B., Sauerwein R.W., Richter King C., MacGill R.S., Bousema T., Jore M.M, & Julien J.P. (2023). Potent transmission-blocking monoclonal antibodies from naturally exposed individuals target a conserved epitope on Plasmodium falciparum Pfs230. Immunity, 56(2), 420-432.e7.

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Publication 2023

anti-IgG Antibodies Buffers Cells Gametes hemozoin HOE 33342 Homo sapiens Medical Devices Monoclonal Antibodies Nycodenz Ovum paraform Plasmodium falciparum Sodium Azide Stains Technique, Dilution

Antibody Binding to Plasmodium Gametes

In vitro cultured Plasmodium falciparum NF54 gametocytes were activated to generate female gametes, which were purified with Nycodenz.²⁶ (link) Per condition 10,000 female gametes were incubated with monoclonal antibodies diluted in SIFA buffer (1% heat-inactivated FCS, 0.05% sodium azide in PBS) for 1 hour at 4 ˚C. Samples were washed 3 times with SIFA buffer. Gametes were stained with Hoechst 33342 DNA stain (1:200 dilution) (Invitrogen, cat no. H3570) and anti-human IgG-AF488 (1:400 dilution) (Invitrogen, cat no. A-11013) for 1 hour at 4 ˚C in the dark. Gametes were then washed 3 times with SIFA buffer, fixed with 4% paraformaldehyde and imaged with an ImageXpress Pico automated cell imaging system (Molecular devices). Gametes were then analyzed with MetaXpress software (Molecular devices). Hemozoin and Hoechst-positive gametes were selected and positivity for human antibodies was determined using signal from negative control antibodies as a threshold.

Fabra-García A., Hailemariam S., de Jong R.M., Janssen K., Teelen K., van de Vegte-Bolmer M., van Gemert G.J., Ivanochko D., Semesi A., McLeod B., Vos M.W., de Bruijni M.H., Bolscher J.M., Szabat M., Vogt S., Kraft L., Duncan S., Kamya M.R., Feeney M.E., Jagannathan P., Greenhouse B., Dechering K.J., Sauerwein R.W., King C.R., MacGill R.S., Bousema T., Julien J.P, & Jore M.M. (2023). Highly potent, naturally acquired human monoclonal antibodies against Pfs48/45 block Plasmodium falciparum transmission to mosquitoes. Immunity, 56(2), 406-419.e7.

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Publication 2023

anti-IgG Antibodies Buffers Cells Gametes hemozoin HOE 33342 Homo sapiens Medical Devices Monoclonal Antibodies Nycodenz Ovum paraform Plasmodium falciparum Sodium Azide Stains Technique, Dilution

Top products related to «Nycodenz»

Nycodenz by Axis-Shield

Sourced in Norway, United Kingdom

Nycodenz is a water-soluble, non-ionic iodinated density gradient medium used for the separation and purification of cells, organelles, and other biological macromolecules by density gradient centrifugation.

Nycodenz by Merck Group

Sourced in United States

Nycodenz is a non-ionic, iso-osmotic density gradient medium. It is used for the separation and purification of cells, organelles, and macromolecules by density gradient centrifugation.

Pronase e by Merck Group

Sourced in United States, Germany, Belgium, China, United Kingdom

Pronase E is a highly purified protease enzyme derived from the bacterium Streptomyces griseus. It is a broad-spectrum enzyme that can hydrolyze a wide range of protein substrates, including casein, gelatin, and collagen. Pronase E is commonly used in various laboratory applications that require efficient protein digestion or removal.

Dnase 1 by Roche

Sourced in United States, Switzerland, Germany, Japan, United Kingdom, France, Canada, Italy, Macao, China, Australia, Belgium, Israel, Sweden, Spain, Austria

DNase I is a lab equipment product that serves as an enzyme used for cleaving DNA molecules. It functions by catalyzing the hydrolytic cleavage of phosphodiester bonds in the DNA backbone, effectively breaking down DNA strands.

Nycodenz by Progen Biotechnik

Sourced in Germany

Nycodenz is a non-ionic iodinated gradient medium used for the separation and isolation of cells, organelles, and other biological macromolecules through density gradient centrifugation. It forms a continuous density gradient upon centrifugation, allowing for the effective separation of different components based on their buoyant densities.

Collagenase d by Roche

Sourced in Switzerland, United States, Germany, United Kingdom, France, Japan, Canada, Australia, Ireland

Collagenase D is an enzyme solution used for the dissociation and isolation of cells from various tissues. It is a mixture of proteolytic enzymes that cleave the collagen present in the extracellular matrix, allowing for the release of individual cells.

Dulbecco modified eagle medium (dmem) by Thermo Fisher Scientific

Sourced in United States, China, United Kingdom, Germany, France, Australia, Canada, Japan, Italy, Switzerland, Belgium, Austria, Spain, Israel, New Zealand, Ireland, Denmark, India, Poland, Sweden, Argentina, Netherlands, Brazil, Macao, Singapore, Sao Tome and Principe, Cameroon, Hong Kong, Portugal, Morocco, Hungary, Finland, Puerto Rico, Holy See (Vatican City State), Gabon, Bulgaria, Norway, Jamaica

DMEM (Dulbecco's Modified Eagle's Medium) is a cell culture medium formulated to support the growth and maintenance of a variety of cell types, including mammalian cells. It provides essential nutrients, amino acids, vitamins, and other components necessary for cell proliferation and survival in an in vitro environment.

Fetal bovine serum (fbs) by Thermo Fisher Scientific

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Fetal Bovine Serum (FBS) is a cell culture supplement derived from the blood of bovine fetuses. FBS provides a source of proteins, growth factors, and other components that support the growth and maintenance of various cell types in in vitro cell culture applications.

Collagenase 4 by Merck Group

Sourced in United States, Germany, United Kingdom, France, China, Sao Tome and Principe, Israel, Canada, Macao, Italy, Australia, Japan, Switzerland, Senegal

Collagenase IV is a purified enzyme used to dissociate and isolate cells from various tissue types. It is effective in breaking down collagen, a major structural component of the extracellular matrix.

Pronase by Roche

Sourced in United States, Germany, Switzerland, United Kingdom

Pronase is a broad-spectrum proteolytic enzyme derived from the bacterium Streptomyces griseus. It is commonly used in laboratory settings to digest and break down proteins in various applications.

What is Nycodenz and how is it used in research?

What are some common challenges or considerations when using Nycodenz in research?

One common challenge with Nycodenz is ensuring the optimal concentration and gradient formation for the specific application. Researchers may need to experiment with different Nycodenz concentrations and centrifugation conditions to achieve the desired separation and purity of their target molecules or structures. Additionally, the viscosity of Nycodenz solutions can make handling and pipetting more difficult compared to other gradient media.

Are there different types or variations of Nycodenz available for research?

Yes, there are several variations of Nycodenz that researchers can use depending on their specific needs. For example, there are different grades of Nycodenz (e.g., ACS reagent grade, cell culture grade) with varying levels of purity and suitability for different applications. Some researchers may also use Nycodenz in combination with other gradient media, such as sucrose or Percoll, to create more complex density gradients for improved separation and purification.

How can PubCompare.ai help researchers optimize their Nycodenz protocols?

PubCompare.ai allows researchers to screen protocol literature more efficiently and leverage AI to pinpoint critical insights. The platform can help researchers identify the most effective protocols related to Nycodenz for their specific research goals. The AI-driven analysis can highlight key differences in protocol effectiveness, enabling researchers to choose the best option for reproducibility and accuracy, and saving them time on manual searching and comparisons.

What are some common applications of Nycodenz in research?

Nycodenz is widely used in a variety of research applications, including: 1) Purification of organelles, such as mitochondria, nuclei, and endoplasmic reticulum, by density gradient centrifugation. 2) Isolation of specific cell types or subpopulations, such as immune cells or stem cells, based on their density differences. 3) Separation and analysis of macromolecular complexes, such as viruses or protein aggregates. 4) Fractionation of subcellular compartments for proteomic or lipidomic analyses. The versatility of Nycodenz makes it a valuable tool across many fields of biology and biochemistry.

More about "Nycodenz"

Nycodenz is a high-density gradient medium commonly used in cell biology research for the separation and purification of cells, organelles, and other biological macromolecules.
It is a non-ionic, water-soluble compound that creates a density gradient when centrifuged, allowing target molecules or structures to be isolated based on their unique densities.
Nycodenz is frequently employed in techniques such as gradient centrifugation, cell fractionation, and organelle isolation, making it a valuable tool for researchers studying cellular and subcellular components.
The use of Nycodenz can be complemented by other reagents like Pronase E, a proteolytic enzyme used for cell dissociation, and DNase I, which helps to reduce DNA clumping during cell isolation.
Collagenase D, another enzyme, is often used in conjunction with Nycodenz for the isolation of specific cell types, such as primary cells from tissues.
The culture medium DMEM (Dulbecco's Modified Eagle Medium) and the supplement FBS (Fetal Bovine Serum) are commonly used in cell culture experiments that involve Nycodenz-based separations.
Collagenase IV, a more specific form of the collagenase enzyme, can also be utilized in Nycodenz-based protocols for the isolation of particular cell populations.
The PubCompare.ai platform can help researchers optimize their Nycodenz research protocols by providing easy access to literature, pre-prints, and patent data.
This allows researchers to identify the best protocols and products for their specific needs, saving time on manual searching and comparisons.
With the help of PubCompare.ai, researchers can ensure they are using the most effective and efficient Nycodenz-based techniques for their studies.