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> Living Beings > Mammal > Equus caballus

Equus caballus

Equus caballus, commonly known as the domestic horse, is a large, hoofed mammal species that has been domesticated for centuries.
It is a member of the family Equidae and is one of the most widely recognized and utilized animals in human history.
Horses are known for their strength, speed, and versatility, and have been used for transportation, agriculture, warfare, and recreation.
They are herbivores, grazing on grasses and other vegetation, and are found in a variety of habitats, from open grasslands to forested areas.
Equus caballus research is an important field, as it helps us better understand the biology, behavior, and evolution of this iconic animal.
With the help of tools like PubCompare.ai, researchers can streamline their studies and enhance the reproducibility and accuracy of their findings.

Most cited protocols related to «Equus caballus»

1
Immunohistochemical Staining of Tumor Tissue
Standard IHC protocol was followed to stain the tumor tissue samples using the mouse monoclonal antibody against hNIS (human Sodium Iodide Symporter) (Abcam, ab17795), ER (Estrogen Receptor) (Abcam, ab16660, ab288). Briefly, 5 µm sized paraffin embedded tissue sections were de-paraffinized with xylene and endogenous peroxidase activity was quenched with 3% H2O2 in methanol for 30 minutes in the dark. Tissue sections were dehydrated through graded alcohols and subjected to antigen retrieval using 10mM sodium citrate. Sections were washed with TBST (Tris Borate Saline Tween-20) and then blocked with 5% BSA (Bovine Serum Albumin) for one hour. Slides were incubated with the respective mouse monoclonal primary antibody diluted with TBS. Slides were then washed for 5 minutes in TBST and incubated for 1 hour with the respective HRP (Horse Raddish Peroxidase) conjugated anti-mouse secondary antibody diluted with TBS in a ratio of 1∶200. After washing, slides were incubated with DAB (3,3′-diaminobenzidine tetrahydrochloride) (Sigma) and immediately washed under tap water after color development. Slides were then counter stained with hematoxylin. Slides were mounted with DPX (dibutyl phthalate xylene) and were then observed under a light microscope (Carl Zeiss).
Varghese F., Bukhari A.B., Malhotra R, & De A. (2014). IHC Profiler: An Open Source Plugin for the Quantitative Evaluation and Automated Scoring of Immunohistochemistry Images of Human Tissue Samples. PLoS ONE, 9(5), e96801.
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Publication 2014
Antibodies, Anti-Idiotypic Antigens Borates Equus caballus estrogen receptor alpha, human Ethanol Homo sapiens Light Microscopy Methanol Monoclonal Antibodies Mus Neoplasms Paraffin Peroxidase Peroxide, Hydrogen Phthalate, Dibutyl Saline Solution Serum Albumin, Bovine SLC5A5 protein, human Sodium Citrate Stains Tissues Tromethamine Tween 20 Xylene
2
Comprehensive Analysis of MHC Class I Ligand Elution Data
Data on all class I MHC ligand elution assays available in IEDB database (www.iedb.org) were collected including the ligand sequence, details of the source protein, position of the ligand in the source protein and the restricting allele of the ligand. There were 160,527 distinct assays in total and the length of the ligands ranged from 4–37. All lengths with a count of ligands at least 0.5% of total ligands were selected for further analysis which included lengths 8–15 and comprised of 99% of the assay entries.
The restricting MHC molecule of the ligands were analyzed and entries with alleles listed unambiguously were selected. For example, some entries where the HLA alleles are listed as just the gene name and alleles from chicken, horse, cow and mouse for which we did not have binding prediction algorithms were excluded. Representative alleles were assigned for entries where only supertypes were listed (e.g. HLA-A*26:01 for HLA-A26). Thus there were 127 class I molecules from human and mouse in the selected data set. Redundant entries with same ligand sequence and MHC molecule were removed and MHC molecules with at least 50 ligand entries were selected. This included 55 class I molecules and the number of available ligands per molecule varied widely from 50 to 9500.
We hypothesized that some of the ligands could be artefacts of the elution assays and therefore their source proteins could be false positive as antigens. A protocol was designed to identify such false positive antigens and exclude them from the final data selected. The protocol identified proteins that had significantly lesser number of predicted binders among ligands than expected of random peptides using binomial probability distribution. Five sets of random peptides were generated from the ligand sequences by shuffling the amino acid residues within the ligands. Binding affinity was then predicted for the original ligands and random peptide sets for their corresponding alleles. The median of the predicted percentile ranks of the five random sets was estimated and assigned as the binding affinity of the random peptides. Based on a predicted binding affinity cut-off of percentile rank 1.0, the number of predicted binders among the original ligands and the random peptide sets were estimated. Five proteins were thus identified as false positives and ligand entries from these proteins were excluded from the data set.
The final data set had 85,217 entries in total with ligand length ranging from 8 to 15. The ligands originated from 14,797 source antigens and were restricted by 55 unique HLA molecules.
Random artificial negatives were generated for each MHC molecule covered by eluted ligand data by sampling randomly 10*N peptides of each length 8–15 amino acids from the antigen source protein sequences, where N is the number of 9mer ligands for the given MHC molecule.
Jurtz V., Paul S., Andreatta M., Marcatili P., Peters B, & Nielsen M. (2017). NetMHCpan 4.0: Improved peptide-MHC class I interaction predictions integrating eluted ligand and peptide binding affinity data. Journal of immunology (Baltimore, Md. : 1950), 199(9), 3360-3368.
Publication 2017
Alleles Amino Acids Amino Acid Sequence Antigens Biological Assay Chickens Equus caballus Genes Genes, MHC Class I HLA-A*26 antigen Homo sapiens Ligands Mice, House Peptides Proteins
3
Influenza Virus Plaque Assay Optimization
One hour after infecting the cell monolayers with 30–50 plaque forming units of the virus in 1 ml of maintenance medium without trypsin, we removed the virus inoculum, covered the cells with 3 ml of the different overlay media and incubated cultures at 35°C in 5% CO2 atmosphere. In the case of MC and Avicel overlays, care was taken not to disturb the plates during the incubation period in order to avoid formation of non-even plaques. After three days of incubation, we removed the overlays and fixed the cells. Agar overlay was removed using metal spatula; MC, Avicel, and liquid overlays were removed by suction. The cells were fixed with 4% paraformaldehyde solution in MEM for 30 min at 4°C and washed with PBS. All subsequent treatments of the cells were performed at room temperature. We permeabilized the cells and simultaneously blocked residual aldehyde groups by incubating the cells for 10–20 min with 1 ml/well of solution containing 0.5 % Triton-X-100 and 20 mM glycine in PBS. We immuno-stained virus-infected cells by incubating for 1 hr with monoclonal antibodies specific for the influenza A virus nucleoprotein (kindly provided by Dr. Alexander Klimov at Centers for Disease Control, USA) followed by 1 hr incubation with peroxidase-labeled anti-mouse antibodies (DAKO, Denmark) and 30 min incubation with precipitate-forming peroxidase substrates. Solution of 10% normal horse serum and 0.05% Tween-80 in PBS was used for the preparation of working dilutions of immuno-reagents. We washed the cells after the primary and secondary antibodies by incubating them three times for 3–5 min with 0.05% Tween-80 in PBS. As peroxidase substrates, we employed either ready to use True Blue™ (KPL) or solution of aminoethylcarbazole (AEC, Sigma) (0.4 mg/ml) prepared in 0.05 M sodium acetate buffer, pH 5.5 and containing 0.03% H2O2. Stained plates were washed with tap water to stop the reaction and dried. In the case of True Blue staining, which is relatively unstable in water solutions, plates were dried inverted in order to minimize bleaching. Stained plates were scanned on a flat bed scanner and the data were acquired by Adobe Photoshop 7.0 software.
As an alternative to immuno-staining, in some experiments we revealed plaques as areas of destroyed cells. To this end, after removing the overlays, we stained the cells with 1% crystal violet solution in 20% methanol in water.
Matrosovich M., Matrosovich T., Garten W, & Klenk H.D. (2006). New low-viscosity overlay medium for viral plaque assays. Virology Journal, 3, 63.
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Publication 2006
Agar Aldehydes Anti-Antibodies Antibodies Atmosphere Avicel Buffers Dental Plaque Equus caballus Glycine Metals Methanol Monoclonal Antibodies Mus NP protein, Influenza A virus paraform Peroxidase Peroxide, Hydrogen Senile Plaques Serum Sodium Acetate Suction Drainage Technique, Dilution Triton X-100 true blue Trypsin Tween 80 Violet, Gentian Virus
4
Whole-mount in situ hybridization of planarians
Unless otherwise noted, asexual planarians 1–5 mm in length were processed for WISH essentially as described [21 (link)] with the following significant modifications: the reduction step prior to dehydration was omitted. Bleaching was performed for 2 hours in formamide bleaching solution (1.2% H2O2, 5% formamide, and 0.5xSSC [32 ]). For regenerating planarians, the Proteinase K/post fixation steps were replaced with a 10 minute boiling step in 10 mM sodium citrate pH 6.0 with 0.05% Tween20, followed by a 20 minute room temperature incubation in PBSTx (Phosphate Buffered Saline [32 ], 0.3% Triton X-100) with 1% SDS. Blocking and antibody incubation for peroxidase-conjugated anti-digoxigenin (1:2,000 [Roche]), anti-fluorescein (1:2,000 [Roche]), and anti-dinitrophenol (1:300 [PerkinElmer]) were performed with 5% horse serum and 0.5% RWBR in TNTx (100 mM Tris pH 7.5, 150 mM NaCl, 0.3% Triton X-100). For chromogenic detection using alkaline phosphatase-conjugated anti-digoxigenin antibody (1:2,000 [Roche]), antibody incubation and blocking were performed with 5% horse serum in TNTx, and post-antibody washes were with TNTx prior to development as described in [21 (link)].
King R.S, & Newmark P.A. (2013). In situ hybridization protocol for enhanced detection of gene expression in the planarian Schmidtea mediterranea. BMC Developmental Biology, 13, 8.
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Publication 2013
Alkaline Phosphatase Antibodies, Anti-Idiotypic azo rubin S Dehydration Digoxigenin Dinitrophenols Endopeptidase K Equus caballus Fluorescein formamide Immunoglobulins Peroxidase Peroxide, Hydrogen Phosphates Planarians Saline Solution Serum Sodium Chloride Sodium Citrate Triton X-100 Tromethamine Tween 20
5
Fractionation of Breast Epithelial Cell Proteome
Human breast epithelial cells (MCF10A) were transfected with a pQCXIH vector and were cultured in DMEM/F12 (Invitrogen, Carlsbad, CA) supplemented with 5% horse serum (Invitrogen), 20 ng/mL EGF, 0.5 μg/mL hydro-cortisone, 100 ng/mL cholera toxin, 10 μg/mL insulin, and 50 μg/mL penicillin/streptomycin until 70–80% confluence was reached. The cells were then lysed in a buffer containing 8 M urea, 2.5 mM sodium pyrophosphate, 1 mM β-glycerophosphate, 50 mM ammonium bicarbonate, one-third tablet of protease inhibitor, and 2 mM sodium ortho-vanadate. Proteins were denatured, reduced, and alkylated after which tryptic digestions were performed at an enzyme/substrate ratio of 1:50. For method comparison between SCX and RP, digested peptides were cleaned by flowing through a 1 mL solid-phase extraction C18 column (Discovery DSC-18, SUPELCO, Bellefonte, PA). Samples were concentrated using a Speed-Vac SC 250 Express (Thermo Savant, Holbrook, NY) and stored at −80°C until time for analysis. A 300.0 μg desalted peptide sample was used for each SCX, low-pH RPLC, and high-pH RPLC fractionation. A 300.0 μg nondesalted protein digest was used to evaluate the potential of high-pH approach for desalting.
Wang Y., Yang F., Gritsenko M.A., Wang Y., Clauss T., Liu T., Shen Y., Monroe M.E., Lopez-Ferrer D., Reno T., Moore R.J., Klemke R.L., Camp DG I.I, & Smith R.D. (2011). Reversed-phase chromatography with multiple fraction concatenation strategy for proteome profiling of human MCF10A cells. Proteomics, 11(10), 2019-2026.
Publication 2011
ammonium bicarbonate beta-glycerol phosphate Breast Buffers Cells Cholera Toxin Cloning Vectors Cortisone Digestion Enzymes Epithelial Cells Equus caballus Fractionation, Chemical Homo sapiens Insulin Penicillins Peptides Protease Inhibitors Proteins Serum sodium pyrophosphate Sodium Vanadate Solid Phase Extraction Streptomycin Tablet Trypsin Urea

Most recents protocols related to «Equus caballus»

1
Conserved Amino Acid Substitutions in Canine H3N8 Influenza Viruses
Not available on PMC !

Example 10

There were conserved amino acid substitutions in all 6 canine isolates that differentiated them from contemporary equine influenza viruses (Table 9). These conserved substitutions were 115M, N83S, W222L, I328T, and N483T. Phylogenetic comparisons of the mature HA protein showed that the canine/Jax/05, canine/Miami/05, and canine/Iowa/05 viruses formed a subgroup with the canine/TX/04 isolate (FIG. 4). There were 3 amino acid changes (L118V, K261N, and G479E) that differentiated this subgroup from the other canine viruses (Table 9). There were 2 amino acid changes (F79L and G218E) that differentiated the 2005 isolates from their canine/TX/04 root. Furthermore, the 2005 isolates from non-greyhound dogs, canine/Jax/05 and canine/Miami/05, differed from the canine/Iowa/05 greyhound isolate by one amino acid change, R492K. Finally, canine/Jax/05 differed from canine/Miami/05 at a single amino acid, S107P. In all other H3N8 equine and canine viruses, S is conserved at position 107 except for A/Equine/Jilin/1/89 which has a T (Guo Y. et al., 1992).

US11865172B2. Materials and methods for respiratory disease control in canines (2024-01-09). UNIVERSITY OF FLORIDA RESEARCH FOUNDATION, INC. [US], CORNELL RESEARCH FOUNDATION, INC. [US], The Government of The United States of America as represented by The Secretary of the Department of [US]. Inventors: Patti Cynthia Crawford [US], Paul J. Gibbs [US], Edward J. Dubovi [US], Ruben Omar Donis [US], Jacqueline Katz [US], Alexander I. Klimov [US], Nallakannu P. Lakshmanan [US], Melissa Anne Lum [US], Daniel Ghislena Emiel Goovaerts [NL], Mark William Mellencamp [US], Nancy J. Cox [US], William L. Castleman [US].
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Patent 2024
Amino Acids Amino Acid Substitution Canis familiaris Equus caballus Influenza Orthomyxoviridae Plant Roots Proteins Virus
2
Expansion and Differentiation of Pluripotent Cells
Not available on PMC !

Example 5

Selected cells can be expanded/grown in Dulbecco's modified Minimal Essential Medium (DMEM) supplemented with glutamine, beta.-mercaptoethanol, 10% (by volume) horse serum, and human recombinant Leukemia Inhibitory Factor (LIF). LIF replaces the need for maintaining selected cells on feeder layers of cells, (which may also be employed) and is essential for maintaining selected cells in an undifferentiated, multipotent, or pluripotent state, such cells can be maintained in Dulbecco's modified Minimal Essential Medium (DMEM) supplemented with glutamine, beta.-mercaptoethanol, 10% (by volume) horse serum, and human recombinant Leukemia Inhibitory Factor (LIF). The LIF replaces the need for maintaining cells on feeder layers of cells, (which may also be employed) and is essential for maintaining cells in an undifferentiated state (per U.S. Pat. No. 6,432,711).

In order to initiate the differentiation of the selected cells into neuronal cells, the cells are trypsinized and washed free of LIF, and placed in DMEM supplemented with 10% fetal bovine serum (FBS). After resuspension in DMEM and 10% FBS, 1×106 cells are plated in 5 ml DMEM, 10% FBS, 0.5 microM retinoic acid in a 60 mm Fisher bacteriological grade Petri dishes, where the cells are expected to form small aggregates. Aggregation aids in proper cell differentiation. High efficiency transfection with (or overexpression of) appropriate neuronal transcription factors and small RNAs can occur before or after plating in DMEM, FBS, and retinoic acid. (See U.S. Pat. Nos. 6,432,711 and 5,453,357 for additional details).

US11859168B2. Electroporation, developmentally-activated cells, pluripotent-like cells, cell reprogramming and regenerative medicine (2024-01-02). None [US]. Inventors: Christopher B. Reid [US], Melissa Braga [US], Lilian N. Santamaria [US], Ashley N. Wickrema [US], Marinne D. Wickrema [US], Anthony Hao Dinh [US], Yaman Eksioglu [US], Mat Hoang Ho [US].
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Patent 2024
2-Mercaptoethanol Acquired Immunodeficiency Syndrome Cells Differentiations, Cell Equus caballus Feeder Layer Cells Fetal Bovine Serum Glutamine Hyperostosis, Diffuse Idiopathic Skeletal LIF protein, human Neurons RNA Serum Transcription Factor Transfection Tretinoin
3
Increasing Oil Content in Forage Crops
Not available on PMC !

Example 6

Oil content in the dicotyledonous plant species Trifolium repens (clover), a legume commonly used as a pasture species, was increased by expressing the combination of WRI1, DGAT and Oleosin genes in vegetative parts. The construct pJP3502 was used to transform T. repens by Agrobacterium-mediated transformation (Larkin et al., 1996). Briefly, the genetic construct pJP3502 was introduced into A. tumefaciens via a standard electroporation procedure. The binary vector also contained a 35S:NptII selectable marker gene within the T-DNA. The transformed Agrobacterium cells were grown on solid LB media supplemented with kanamycin (50 mg/L) and rifampicin (25 mg/L) and incubated at 28° C. for two days. A single colony was used to initiate a fresh culture. Following 48 hours vigorous culture, the Agrobacterium cells was used to treat T. repens (cv. Haifa) cotyledons that had been dissected from imbibed seed as described by Larkin et al. (1996). Following co-cultivation for three days the explants were exposed to 25 mg/L kanamycin to select transformed shoots and then transferred to rooting medium to form roots, before transfer to soil.

Six transformed plants containing the T-DNA from pJP3502 were obtained and transferred to soil in the glasshouse. Increased oil content was observed in the non-seed tissue of some of the plants, with one plant showing greater than 4-fold increase in TAG levels in the leaves. Such plants are useful as animal feed, for example by growing the plants in pastures, providing feed with an increased energy content per unit weight (energy density) and resulting in increased growth rates in the animals.

The construct pJP3502 is also used to transform other leguminous plants such as alfalfa (Medicago sativa) and barrel medic (Medicago truncatula) by the method of Wright et al. (2006) to obtain transgenic plants which have increased TAG content in vegetative parts. The transgenic plants are useful as pasture species or as hay or silage as a source of feed for animals such as, for example, cattle, sheep and horses, providing an increased energy density in the feed.

US11859193B2. Plants with modified traits (2024-01-02). Commonwealth Scientific and Industrial Research Organisation [AU]. Inventors: XueRong Zhou [AU], Qing Liu [AU], Anna El Tahchy [AU], Srinivas Belide [AU], Madeline Claire Mitchell [AU], Uday Kumar Divi [AU], Thomas Vanhercke [AU], James Robertson Petrie [AU], Surinder Pal Singh [AU], Allan Graham Green [AU].
Full text: Click here
Patent 2024
Agrobacterium Alfalfa Animals Cattle Cells Cloning Vectors Cotyledon Domestic Sheep Electroporation Equus caballus Fabaceae Genes Kanamycin Magnoliopsida Markers, DNA Medicago truncatula Plant Embryos Plant Oils Plant Roots Plants Plants, Transgenic Reproduction Rifampin Silage Tissues Trifolium Trifolium repens
4
Generating Resistant Target Cells
Not available on PMC !

Example 19

In order to obtain large numbers of target cells that are relatively resistant to 1) HIV infection and/or 2) HIV replication and/or 3) HIV transcription, progenitor/stem cells can be grown in Dulbecco's modified Minimal Essential Medium (DMEM) supplemented with glutamine, beta.-mercaptoethanol, 10% (by volume) horse serum, and human recombinant Leukemia Inhibitory Factor (LIF). The LIF replaces the need for maintaining progenitor/stem cells on feeder layers of cells, (which may also be employed) and is essential for maintaining progenitor/stem cells in an undifferentiated state.

US11859168B2. Electroporation, developmentally-activated cells, pluripotent-like cells, cell reprogramming and regenerative medicine (2024-01-02). None [US]. Inventors: Christopher B. Reid [US], Melissa Braga [US], Lilian N. Santamaria [US], Ashley N. Wickrema [US], Marinne D. Wickrema [US], Anthony Hao Dinh [US], Yaman Eksioglu [US], Mat Hoang Ho [US].
Full text: Click here
Patent 2024
2-Mercaptoethanol DNA Replication Equus caballus Feeder Layer Cells Glutamine HIV Infections LIF protein, human Serum Stem, Plant Stem Cells Transcription, Genetic
5
Single-Cell RNA-Seq of Rat Skeletal Muscle
Cell isolations were performed as previously described in mice [37 (link)] and modified slightly for rats [28 (link)]. Briefly, the gastrocnemius muscles from WB and HS male rats were excised and placed in muscle dissociation media (MDM) (Hams F-10 (Gibco, USA), 10% Horse Serum (Thermo Fisher), 1% penicillin/streptomycin (Gibco), 800 U/ml Collagenase II (Gibco)), and minced using sterilized surgical equipment. The muscle homogenate was then incubated in MDM for 1 h at 37 °C with gentle agitation. Following incubation, samples underwent further incubation in 1000 U/ml Collagenase II (Gibco) and 11 U/ml dispase (Gibco) for 30 min at 37 °C. The single-cell suspension was passed through an 18-gauge needle approximately 10 times prior to 0.2-μm filtration. Single cells were incubated in propidium iodide to identify dying/dead cells for removal via fluorescence-activated cell sorting (Sony Biotechnology, USA). Single-cell suspensions from each group were added to a Chromium Controller (10X Genomics, USA) using the Single Cell 3’ Reagent Kit per manufacturer’s instructions and sequenced on an Illumina HiSeq platform (Novogene, USA), yielding 200 million reads/sample.
Ismaeel A., Van Pelt D.W., Hettinger Z.R., Fu X., Richards C.I., Butterfield T.A., Petrocelli J.J., Vechetti I.J., Confides A.L., Drummond M.J, & Dupont-Versteegden E.E. (2023). Extracellular vesicle distribution and localization in skeletal muscle at rest and following disuse atrophy. Skeletal Muscle, 13, 6.
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Publication 2023
ATF7IP protein, human Cell Separation Chromium Collagenase dispase Equus caballus Filtration Males Mus Muscle, Gastrocnemius Muscle Tissue Needles Penicillins Propidium Iodide Rattus norvegicus Serum Streptomycin Surgical Equipment Type II Mucolipidosis

Top products related to «Equus caballus»

1
Horse serum by Thermo Fisher Scientific
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Horse serum is a biological fluid derived from the blood of horses. It contains a complex mixture of proteins, including immunoglobulins, hormones, and other biomolecules. Horse serum is commonly used as a supplement in cell culture media to support the growth and maintenance of various cell types.
2
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.
3
Dulbecco modified eagle medium (dmem) by Thermo Fisher Scientific
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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.
4
Penicillin streptomycin by Thermo Fisher Scientific
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Penicillin/streptomycin is a commonly used antibiotic solution for cell culture applications. It contains a combination of penicillin and streptomycin, which are broad-spectrum antibiotics that inhibit the growth of both Gram-positive and Gram-negative bacteria.
5
Hydrocortisone by Merck Group
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Hydrocortisone is a laboratory-grade reagent used in various research and analytical applications. It is a synthetic corticosteroid compound with anti-inflammatory and immunosuppressant properties. Hydrocortisone is commonly utilized as a standard or reference material in analytical procedures, such as assays and chromatographic techniques, to quantify and identify related compounds.
6
Insulin by Merck Group
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Insulin is a lab equipment product designed to measure and analyze insulin levels. It provides accurate and reliable results for research and diagnostic purposes.
7
Cholera toxin by Merck Group
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Cholera toxin is a bacterial protein produced by the bacterium Vibrio cholerae. It has a well-documented function as a potent activator of the adenylate cyclase enzyme, leading to increased levels of cyclic AMP (cAMP) in target cells. This property makes cholera toxin a valuable tool in various areas of biological research, such as cell signaling studies and the investigation of cellular regulatory mechanisms.
8
Penicillin by Thermo Fisher Scientific
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Penicillin is a type of antibiotic used in laboratory settings. It is a broad-spectrum antimicrobial agent effective against a variety of bacteria. Penicillin functions by disrupting the bacterial cell wall, leading to cell death.
9
Streptomycin by Thermo Fisher Scientific
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Streptomycin is a broad-spectrum antibiotic used in laboratory settings. It functions as a protein synthesis inhibitor, targeting the 30S subunit of bacterial ribosomes, which plays a crucial role in the translation of genetic information into proteins. Streptomycin is commonly used in microbiological research and applications that require selective inhibition of bacterial growth.
10
Dmem f12 by Thermo Fisher Scientific
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DMEM/F12 is a cell culture medium developed by Thermo Fisher Scientific. It is a balanced salt solution that provides nutrients and growth factors essential for the cultivation of a variety of cell types, including adherent and suspension cells. The medium is formulated to support the proliferation and maintenance of cells in vitro.

More about "Equus caballus"

Discover the fascinating world of Equus caballus, the domestic horse, a majestic and versatile species that has captivated humanity for centuries.
This large, hoofed mammal from the Equidae family is renowned for its strength, speed, and adaptability, making it a crucial part of human history.
Explore the rich biology, behavior, and evolution of Equs caballus through comprehensive research.
Leverage cutting-edge tools like PubCompare.ai to streamline your studies and enhance the reproducibility and accuracy of your findings.
Identify optimal research approaches and products by leveraging intelligent comparisons and accessing a wealth of protocols from literature, pre-prints, and patents.
Delve into the diverse applications of Equus caballus, from transportation and agriculture to warfare and recreation.
Understand the importance of key components like Horse serum, FBS, DMEM, Penicillin/streptomycin, Hydrocortisone, Insulin, and Cholera toxin in supporting your research.
Whether you're studying the domestication, genetics, or behavior of these iconic animals, PubCompare.ai can help you navigate the vast landscape of Equus caballus research with ease.
Embark on your equine journey and uncover new insights that will expand our understanding of this remarkable species.
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