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Carnation

Carnations are a popular and widely cultivated flower species of the genus Dianthus.
These fragrant blooms are often used in cut flower arrangements, bouquets, and corsages.
Carnations come in a variety of colors, including red, white, pink, yellow, and purple.
They are known for their ruffled, frilly petals and long, slender stems.
Carnations are perennial plants that can grow in USDA hardiness zones 5-9.
They thrive in well-drained soil and full sun exposure.
Carnations are an important horticultural crop, with global production and trade supporting a sizable industry.
Researchers utilize carnations to study plant biology, genetics, and cultivation practices in order to improve quality, yield, and disease resistancde.

Most cited protocols related to «Carnation»

1
SDS-PAGE and Western Blot Analysis
Cited 44 times
Protein samples were treated for 30 min at 50°C in a sample-treating solution containing 2% SDS and 5% β-mercaptoethanol. The samples were then loaded onto a 12% or 15% SDS-polyacrylamide gel (7.0×8.3 cm ×0.75 mm) and electrophoresed using Mini-Protean Tetra system (Bio-Rad) at 15 mA (current constant). After electrophoresis, proteins separated on the gel were transferred onto a methanol-activated PVDF membrane (Immobilon-P, pore size 0.45 µm, Millipore) or a nitrocellulose membrane (Protran BA85, pore size 0.45 µm, Whatman) for 2 h using TE22 Mighty Small Transfer system (Hoefer Scientific) at 100 V (voltage constant). The membrane was then treated with or without phosphate-buffered saline (PBS) containing 0.4% PFA for 30 min at room temperature, followed by blocking for 1 h with 5% skim milk (Carnation) in Tris-buffered saline containing 0.1% Tween-20 (TBS-T). The membrane was then incubated for 1 h with a primary antibody in TBS-T containing 1% skim milk. As primary antibody, mouse monoclonal anti-α-syn antibodies 4D6 and LB509 (Santa Cruz Biotechnology) and rabbit monoclonal anti-phospho α-syn antibody EP1536Y (Epitomics, Burlingame, CA) were used at a dilution 1∶1,000, and rabbit polyclonal anti-actin antibody (Sigma) was also used at a dilution 1∶5,000. After washing with TBS-T containing 1% skim milk for 5 min three times, the membrane was incubated for 1 h with a secondary antibody, horseradish peroxidase-conjugated anti-mouse IgG or anti-rabbit IgG antibody (Santa Cruz Biotechnology), in TBS-T containing 1% skim milk. After washing with TBS-T for 10 min three times, protein bands on the membrane were detected by chemiluminescence method using ECL-Plus immunoblotting detection system (GE Healthcare).
Lee B.R, & Kamitani T. (2011). Improved Immunodetection of Endogenous α-Synuclein. PLoS ONE, 6(8), e23939.
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Publication 2011
2-Mercaptoethanol Actins Anti-Antibodies anti-IgG Antibodies, Anti-Idiotypic Carnation Chemiluminescence Electrophoresis Horseradish Peroxidase Immobilon P Immunoglobulins Membrane Proteins Methanol Mice, House Milk, Cow's Nitrocellulose Phosphates polyacrylamide gels polyvinylidene fluoride Proteins Rabbits Saline Solution Technique, Dilution Tetragonopterus Tissue, Membrane Tween 20
2
C. elegans Whole-Mount Immunohistochemistry
Cited 11 times

C. elegans were grown at 22.5°C on nematode growth media (NGM) as described previously [85] . N2 wild type, lmp-1(nr2045)[67] (link), unc-10(md1117)[17] (link), and snb-1(md247)[12] (link) strains were used in the study.
Two fixation conditions were used for the whole-mount immunohistochemistry: Bouin's [86] (link) and methanol/acetone. For the methanol/acetone fix, tubes of frozen worms (washed off of large NGM plates) were thawed on ice and incubated in 2 volumes of cold methanol at 4°C for 10 minutes, sonicated on ice with a tip sonicator two times for 5 seconds each at maximal setting to break open the worms. The tube was incubated on ice for 10 minutes and spun down briefly in a microcentrifuge. The supernatant was aspirated and 2 volumes of −20°C acetone were added to the pellet. The worms were incubated on ice for 10 minutes and spun down briefly in a microcentrifuge. The supernatant was removed and 2 volumes of AbA (PBS + 0.05% Tween-20 + 0.5% BSA) were added to the pellet. The worms were then incubated with rolling agitation at RT for 30 minutes and spun down in a microcentrifuge. The supernatant was aspirated and two volumes of AbA + 20% glycerol was added to the pellet. The worms were then aliquoted and flash frozen in liquid N2 and stored at −80°C until needed.
For immunostaining, fixed worms were incubated in BLOCK [2% BSA + 2% gelatin+ 2% powdered milk (Carnation) +0.05% Tween-20 in PBS] for 1–2 hours. The worms were washed three times in PBST (PBS +0.1% Tween20), and incubated overnight at 4°C with a 1∶10 dilution of the hybridoma tissue culture supernatant in BLOCK. Worms were washed three times in PBST and incubated for 1 hour with the secondary antibody diluted in BLOCK. The secondary antibodies used to visualize the binding pattern of the primary antibodies were goat anti-mouse IgG Alexa Fluor® 488 or 568 (Invitrogen, Carlsbad, CA) at a 1∶2000 dilution. Gonads and intestines were fixed and stained as previously described [87] (link).
Samples were examined on a Zeiss Akioskop equipped with an X-CITE 120 mercury bulb (EXFO) and standard epifluorescence filters. Images were captured using a Regita EXi cooled CCD camera and viewed using the Open Lab software (Improvision, PerkinElmer, Boston, MA). Image panels were assembled in Photoshop. In some cases, the corners of rotated images were colored to match the background. Additionally, other stained material in the field of view was excised to simplify images and replaced with background signal. Original images are available upon request. Gonad and Intestine images were assembled as previously described [87] (link).
Hadwiger G., Dour S., Arur S., Fox P, & Nonet M.L. (2010). A Monoclonal Antibody Toolkit for C. elegans. PLoS ONE, 5(4), e10161.
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Publication 2010
Acetone alexa fluor 488 anti-IgG Antibodies Caenorhabditis elegans Carnation Cold Temperature Culture Media Freezing Gelatins Glycerin Goat Gonads Helminths Hybridomas Immunoglobulins Immunohistochemistry Intestines Medulla Oblongata Mercury Methanol Milk, Cow's Mus Nematoda Strains Technique, Dilution Tissues Tween 20
3
Immunohistochemistry of Tendon Pathology
Cited 10 times
Immunohistochemical analysis was performed on flexor digitorum tendons collected from normal controls (n=12), trained controls (n = 9), and rats that had performed either the HRHF task for 3 (n = 4), 6 (n=4) or 12 weeks (n=4), or the LRNF task for 3 (n=3), 6 (n=4) or 12 weeks (n = 3). Animals were euthanized, perfused transcardially with 4% paraformaldehyde in PO4 buffer, and forearm musculotendinous tissues were dissected as a mass off the forearm bones as shown in Figure 3K,L, and sectioned longitudinally as a soft tissue mass (en bloc) as described previously (19 (link), 23 (link)). Sections, on slides, were incubated in 3% H2O2 in methanol (4°C) for 30 min, washed, incubated in 4% dried milk in PBS (Blotto) for 20 min, and then overnight at rm temp with a Substance P antibody (# MAB1566, Chemicon, Temecula, CA; 1:500 dilution with 4% carnation milk in PBS). After washing, sections were incubated for 2 hrs at rm temp with goat anti-mouse peroxidase-conjugated (HRP) secondary antibody (Jackson ImmunoResearch, West Grove, PA) diluted 1:100 with PBS. HRP was visualized as a black immunoreactive stain using diaminobenzidene (DAB) with cobalt (Sigma-Aldrich, St. Louis, MO). For IL-1β and periostin like factor (PLF; labels activated fibroblasts producing this matricellular protein), sections were immunolabeled and detected with HRP-DAB as previously described (21 (link),24 (link)). Eosin and/or nuclear red were used as counterstains. A series of adjacent sections were also stained with hematoxylin and eosin (H&E) only. Sections were dehydrated and coverslipped with DPX mounting medium. For connective tissue growth factor (CTGF; a fibroblast growth factor that induces collagen production and an activated fibroblast marker), sections were immunolabeled and detected with Cy3 (red fluorescence), and coverslipped with 80% glycerol in PBS, as previously described (22 (link)). Negative control slides included omission of either the primary antibody or the secondary antibody.
Selected sections were double-labeled after Substance P immunolabeling with either anti-ED1 (detects a 90 kDa lysosomal membrane protein in monocytes/macrophages) or anti-PGP9.5 (a pan neuronal marker). After Substance P immunolabeling with secondary antibody conjugated to Cy2 (green tag; Jackson, diluted 1:100 in PBS for 2 hrs), tissue sections were washed, digested with 0.5% pepsin in 0.01 N HCl for 20 min at rm temp, and then incubated with goat serum (4%) in PBS for 30 min at rm temp. Sections were then incubated with either anti-ED1 (MAB1435, Chemicon, Temecula, CA, 1:250 dilution in 4% goat serum in PBS) or anti-PGP9.5 (ab8189, Abcam, Cambridge, MA, 1:50 dilution in 10% goat serum in PBS) overnight at rm temp. Sections were incubated with appropriate secondary antibodies conjugated to Cy3 (red tag; Jackson). Slides were coverslipped with 80% glycerol in PBS. Selected sections were also double-labeled with CTGF and collagen type I antibodies as described previously (22 (link)).
Fedorczyk J.M., Barr A.E., Rani S., Gao H., Amin M., Amin S., Litvin J, & Barbe M.F. (2010). Exposure dependent increases in IL-1beta, Substance P, CTGF and tendinosis in flexor digitorum tendons with upper extremity repetitive strain injury. Journal of orthopaedic research : official publication of the Orthopaedic Research Society, 28(3), 298-307.
Publication 2009
Animals Antibodies Buffers Carnation Cobalt Collagen Collagen Type I Connective Tissue Growth Factor Eosin Fibroblast Growth Factor Fibroblasts Fluorescence Forearm Glycerin Goat Immunoglobulins Interleukin-1 beta Lysosome-Associated Membrane Glycoproteins Macrophage Methanol Milk, Cow's Monocytes Mus Neurons paraform Pepsin A Peroxidase Peroxide, Hydrogen POSTN protein, human Proteins Rattus Serum Stains Substance P Technique, Dilution Tendons Tissues UCHL1 protein, human Ulna
4
Structural Analysis of DcaAQP Genes
Cited 7 times
Information of introns and exons for DcaAQP genes was obtained from Carnation DB, Exon-intron structure was analyzed by GSDS 2.0 (http://gsds.cbi.pku.edu.cn/) [71 (link)] using default parameters. Conserved motifs were generated by MEME suit (http://meme-suite.org/tools/meme) [72 (link)], and the following parameter settings were used: the number of motifs was set as 10, the optimum width of motifs was 3 to 60, and other parameters were set as default values [40 (link),63 (link)]. The transmembrane domain prediction was studied using TMHMM Server v.2.0 (http://www.cbs.dtu.dk/services/TMHMM/). The MW and pI of the amino acid sequences were predicted using online program ProtParam (http://web.expasy.org/protparam/). Subcellular localization was analyzed by Plant-mPloc server (http://www.csbio.sjtu.edu.cn/bioinf/plant-multi/) [40 (link)].
Kong W., Bendahmane M, & Fu X. (2018). Genome-Wide Identification and Characterization of Aquaporins and Their Role in the Flower Opening Processes in Carnation (Dianthus caryophyllus). Molecules : A Journal of Synthetic Chemistry and Natural Product Chemistry, 23(8), 1895.
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Publication 2018
Amino Acid Sequence Carnation Exons Genes Introns Plants
5
Laminar Flow Adhesion Assay for Cell-Cadherin Binding
Cited 7 times
The modified laminar flow adhesion assay performed was a modification of the one described previously (Brieher et al., 1996 (link)). In brief, borosilicate glass capillaries (1.1 mm internal diameter) (Sutter Instrument) were precoated with protein A (Amersham Pharmacia Biotech) 100 μg/ml in PBS++ during 5 h at 4°C, and nonspecific binding sites were then blocked with 0.5% casein hydrolysate enzymatic (ICN Biochemicals, Cleveland, OH) in PBS++ for 2 h at 4°C. Then these capillaries were coated overnight at 4°C with the Fc–cadherin fusion proteins at various concentrations (100, 20, 10, and 5 μg/ml). To control the amount of Fc–cadherin fusion protein bound to protein A on the surface, the total Fc-containing protein concentration is maintained at 100 μg/ml by adding the appropriate amount of 1 mg/ml Fc (Human IgG, Fc Fragment, Plasma, Calbiochem) in PBS. Nonspecific binding sites were then blocked with 5% milk (nonfat dry milk; Carnation, Nestle) in HBSS containing 1 mM CaCl2. CHO cells or the stable cell line C-CHO were grown under standard conditions then harvested by a method that leaves cell surface cadherins intact (incubation with crystalline trypsine [0.01% wt/vol] in PBS++), washed, and resuspended in HBSS/1 mM CaCl2 or HBSS/1 mM EDTA. At that point, cells were infused into the coated capillary from a reservoir using a pump. After 1 min, the flow was stopped, and the cells were allowed to bind to the surface under static conditions for 10 min. Capillaries were observed with a phase microscope, and the number of cells attached to the substrate in a 20× field was counted. Flow was initiated, and the number of cells remaining in the field was counted after 30 s. Subsequently, the flow was doubled every 30 s, and the number of cells remaining in the field was counted at the end of each time point. Data were normalized to the number of cells present in the field before starting the flow.
Chappuis-Flament S., Wong E., Hicks L.D., Kay C.M, & Gumbiner B.M. (2001). Multiple cadherin extracellular repeats mediate homophilic binding and adhesion. The Journal of Cell Biology, 154(1), 231-243.
Publication 2001
Binding Sites Biological Assay Cadherins Capillaries Carnation casein hydrolysate Cell Lines Cells CHO Cells Edetic Acid Enzymes Hemoglobin, Sickle Homo sapiens Immunoglobulin Fc Fragments Microscopy Milk, Cow's Plasma Proteins Staphylococcal Protein A Training Programs Trypsin

Most recents protocols related to «Carnation»

1
Vase Life of White Carnation Flowers
This experiment was performed at the vase life chamber, Horticulture Department laboratory, Agriculture Faculty, Tanta University, Egypt. The cut flowers of white carnation cv. Madam Collette (Dianthus caryophyllus L.) were brought from Floramax Farm company. The flowers were harvested at the fully open stage (the commercial stage of carnation flowers when the outer petals are fully expanded) [2 ] and trimmed to 40 cm in length. Their lower leaves were removed before recording their weight.
Gururani M.A., Atteya A.K., Elhakem A., El-Sheshtawy A.N, & El-Serafy R.S. (2023). Essential oils prolonged the cut carnation longevity by limiting the xylem blockage and enhancing the physiological and biochemical levels. PLOS ONE, 18(3), e0281717.
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Publication 2023
Carnation Faculty Flowers VASE peptide
2
Preserving Cut Carnation Flowers
Cut carnation flowers were kept in jars containing 100 mL of the prepared preservative solution, supplemented with 5 g/L sucrose w/v, at 19 ± 2°C, 63 ± 5% relative humidity, and 12 h photoperiod at a light intensity of 10–12 μmol m–2 s–1 irradiance using white and cool fluorescent lamps. To prevent contamination and evaporation, the mouth of the bottle was covered using a plastic film [38 ]. The flowers were observed daily. Carnation longevity was estimated as the number of days required for 75% of the cut flowers to lose their turgor and ornamental value (characterized by wilting of the flowers).
Gururani M.A., Atteya A.K., Elhakem A., El-Sheshtawy A.N, & El-Serafy R.S. (2023). Essential oils prolonged the cut carnation longevity by limiting the xylem blockage and enhancing the physiological and biochemical levels. PLOS ONE, 18(3), e0281717.
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Publication 2023
Carnation Flowers Humidity Light Oral Cavity Pharmaceutical Preservatives Sucrose
3
Quantification of Hydrogen Peroxide in Carnation Leaves
The protocol reported by Patterson et al. [44 (link)] was used to quantify H2O2 levels in carnation leaves. Leaf samples (0.5 g) were pulverized in 6 mL of cooled acetone (100% v/v) and centrifuged at 12,000 g for 10 min at 4°C. About 1 mL of the supernatant was mixed with 0.1 mL of Ti(SO4)2 solution (5% w/v) and 0.2 mL of concentrated NH4OH solution, respectively. The mixture was then centrifuged at 3000 g for 10 min. dissolved in 4 mL of H2SO4 (2 M). The optical density of the solution was measured spectrophotometrically at 412 nm.
Gururani M.A., Atteya A.K., Elhakem A., El-Sheshtawy A.N, & El-Serafy R.S. (2023). Essential oils prolonged the cut carnation longevity by limiting the xylem blockage and enhancing the physiological and biochemical levels. PLOS ONE, 18(3), e0281717.
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Publication 2023
Acetone Carnation Peroxide, Hydrogen Plant Leaves Vision
4
Western Blot Protein Expression Analysis
Whole-cell lysates were harvested in RIPA buffer with EDTA (Cat# BP-115D, Boston BioProducts, Inc., Milford, MA, USA), 1X Halt protease inhibitor (Cat# 78430, ThermoFisher Scientific, Waltham, MA, USA), and 1X sodium orthovanadate phosphatase inhibitor (Cat# 13721-39-6, ThermoFisher Scientific, Waltham, MA, USA). The total protein concentrations of cell lysates were determined using Pierce BCA Protein Assay Kit (Cat# 23225, ThermoFisher Scientific, Waltham, MA, USA). Equal protein amounts (10 µg) were prepared in Sample Buffer (Cat# B0007, ThermoFisher Scientific, Waltham, MA, USA) and loaded onto SDS-PAGE gels using the Bolt system from ThermoFisher Scientific according to the manufacturer’s protocol with the following reagents: 1. Bolt 4-12% Bis-Tris Plus gels (Cat# NW04120) 2. Bolt MES SDS Running buffer (Cat# B0002) 3. Bolt Antioxidant (Cat# BT0005). SDS-PAGE was performed. Proteins were transferred onto nitrocellulose membranes (Cat# 10600015, Cytiva, Marlborough, MA, USA) at 300 mA for 2 h before blocking in 5% non-fat dry milk (Carnation) in TBS-Tween-20 for one hour at room temperature. Blots were placed in primary antibody dilutions at 4 °C on a rotator overnight. All antibodies utilized are listed in Table S4. Blots were washed in TBS-Tween-20 the next day, placed in secondary antibody dilutions for one hour at room temperature, washed again, and imaged using SignalFire Plus ECL reagent (Cat#12630S, Cell Signaling, Danvers, MA, USA) or SuperSignal West Pico Plus (Cat# 34578, ThermoFisher Scientific, Waltham, MA, USA) on the FluorChem R imaging system (ProteinSimple, San Jose, CA, USA). Densitometry was performed using ImageJ software [140 (link)] and analyzed on GraphPad Prism version 9.4.0 (GraphPad Software Inc., La Jolla, CA, USA).
Renaud L., Waldrep K.M., da Silveira W.A., Pilewski J.M, & Feghali-Bostwick C.A. (2023). First Characterization of the Transcriptome of Lung Fibroblasts of SSc Patients and Healthy Donors of African Ancestry. International Journal of Molecular Sciences, 24(4), 3645.
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Publication 2023
Antibodies Antioxidants Biological Assay Bistris Buffers Carnation Densitometry Edetic Acid Gels Immunoglobulins Milk, Cow's Nitrocellulose Orthovanadate Phosphoric Monoester Hydrolases prisma Protease Inhibitors Proteins Radioimmunoprecipitation Assay SDS-PAGE Sodium Technique, Dilution Tissue, Membrane Tween 20
5
Fusarium Identification in Maize Samples
Climate is an important factor that modify fungal development and leads to variable levels of mycotoxins [11 (link)]. In temperate regions, colonization of maize by Fusarium species and consequent contamination with fumonisins are expected [11 (link)]. In this way, and following our previous studies [6 (link),7 (link)], the mycological analyses were focused on Fusarium spp. detection and identification. The preparation of samples was performed as described by Carbas and co-workers [6 (link)]. Briefly, 50 grains per sample were surface disinfected and plated aseptically on Malachite Green Agar 2.5 [37 (link)] at the rate of five grains per 90 mm Petri-dish: one in the centre and one in each quadrant. Plates were incubated at 25 °C for 12 h under near UV light and 12 h darkness [38 (link)]. After 7 days, the quantification of maize grains contaminated with Fusarium was performed, and the Fusarium specimens were isolated by the single spore technique [5 ] onto Potato Dextrose Agar (PDA), BD Difco™, (Fisher Scientific, Porto Salvo, Portugal) and incubated for 7 days. Fungal culture from each diseased grain represents an independent isolate. The isolates were grouped by morphotypes, picked to Carnation Leaf-piece Agar (CLA) and Spezieller Nährstoffarmer Agar (SNA) media, and after 10 days of incubation, were identified until species level by macro and microscopic (100× and 400×) morphology, following Leslie and Summerell (2006) [5 ].
Simões D., Carbas B., Soares A., Freitas A., Silva A.S., Brites C, & de Andrade E. (2023). Assessment of Agricultural Practices for Controlling Fusarium and Mycotoxins Contamination on Maize Grains: Exploratory Study in Maize Farms. Toxins, 15(2), 136.
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Publication 2023
Agar Carnation Cereals Climate Darkness Fumonisins Fusarium Glucose Hyperostosis, Diffuse Idiopathic Skeletal Maize malachite green Microscopy Mycotoxins Plant Leaves Solanum tuberosum Spores Ultraviolet Rays Workers

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More about "Carnation"

Dianthus, the genus of carnations, encompasses a wide array of fragrant, vibrant flowers.
These perennial plants, thriving in USDA hardiness zones 5-9, are renowned for their ruffled, frilly petals and long, slender stems.
Carnations come in a diverse palette of colors, including red, white, pink, yellow, and purple, making them a popular choice for cut flower arrangements, bouquets, and corsages.
The carnation's importance extends beyond its aesthetic appeal.
As a crucial horticultural crop, global production and trade of these blooms support a sizable industry.
Researchers harness the power of tools like the DS-Ri2 camera, RNeasy Plant Mini Kit, Eclipse 80i microscope, and StepOnePlus Real-Time PCR System to study the plant's biology, genetics, and cultivation practices.
This research aims to enhance quality, yield, and disease resistance, elevating the carnation's role in the floral landscape.
Whether you're a florist, horticulturist, or simply a lover of these fragrant blooms, understanding the nuances of carnation cultivation and research can unlock new possibilities.
Leverage the insights of PubCompare.ai's innovative AI-powered tools to optimize your workflow, identify the best protocols and products, and drive reproducibility in your carnation-related experiments.
Embark on a journey of discovery and unlock the full potential of this iconic flower.