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Jurkat Cells

Jurkat cells are a widely used human T lymphocyte cell line derived from an acute T cell leukemia.
These cells have been instrumental in the study of T cell signaling, activation, and apoptosis.
Jurkat cells express a variety of T cell surface markers and exhibit many characteristics of immature T lymphocytes, making them a valuable model for investigating T cell biology and immunology.
Researhcers can leverage PubCompare.ai's AI-powered platform to easily locate the best Jurkat cell protocols from literature, preprints, and patents, optimizing their experimental workflows and taking the guesswork out of their research.

Most cited protocols related to «Jurkat Cells»

1
ChIP-Seq Analysis of NRSF, CTCF, and FoxA1
ChIP-Seq data for three factors, NRSF, CTCF, and FoxA1, were used in this study. ChIP-chip and ChIP-Seq (2.2 million ChIP and 2.8 million control uniquely mapped reads, simplified as 'tags') data for NRSF in Jurkat T cells were obtained from Gene Expression Omnibus (GSM210637) and Johnson et al. [8 (link)], respectively. ChIP-Seq (2.9 million ChIP tags) data for CTCF in CD4+ T cells were derived from Barski et al. [5 (link)].
ChIP-chip data for FoxA1 and controls in MCF7 cells were previously published [1 (link)], and their corresponding ChIP-Seq data were generated specifically for this study. Around 3 ng FoxA1 ChIP DNA and 3 ng control DNA were used for library preparation, each consisting of an equimolar mixture of DNA from three independent experiments. Libraries were prepared as described in [8 (link)] using a PCR preamplification step and size selection for DNA fragments between 150 and 400 bp. FoxA1 ChIP and control DNA were each sequenced with two lanes by the Illumina/Solexa 1G Genome Analyzer, and yielded 3.9 million and 5.2 million uniquely mapped tags, respectively.
Zhang Y., Liu T., Meyer C.A., Eeckhoute J., Johnson D.S., Bernstein B.E., Nusbaum C., Myers R.M., Brown M., Li W, & Liu X.S. (2008). Model-based Analysis of ChIP-Seq (MACS). Genome Biology, 9(9), R137.
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Publication 2008
CD4 Positive T Lymphocytes ChIP-Chip Chromatin Immunoprecipitation Sequencing CTCF protein, human DNA Chips DNA Library FOXA1 protein, human Gene Expression Genome Jurkat Cells MCF-7 Cells
2
Benchmarking Cell Deconvolution Algorithms
We performed two in silico experiments to assess the detection limits of different deconvolution algorithms. In the first experiment (Supplementary Fig. 6), we used the same cell line GEPs described above to compare CIBERSORT and RLR with five other GEP deconvolution methods4 (link)–8 (link). We evaluated detection limit using Jurkat cells (spike-in concentrations of 0.5%, 1%, 2.5%, 5%, 7.5%, and 10%), whose reference GEP (median of three replicates in GSE11103) was added into randomly created background mixtures of the other three blood cell lines. Five mixtures were created for each spike-in concentration. Predicted Jurkat fractions were assessed in the presence of differential tumor content, which we simulated by adding HCT116 (described above) in ten even increments, from 0% to 90%. Of note, we also used the same marker or signature genes described for simulated tumors (above). In a second experiment (Supplementary Fig. 7a), we compared CIBERSORT with QP5 (link), LLSR4 (link), PERT6 (link), and RLR. We spiked naïve B cell GEPs from the leukocyte signature matrix into four random background mixtures of the remaining 21 leukocyte subsets in the signature matrix. The same background mixtures were used for each spike-in. We also tested the addition of unknown content by adding defined proportions (0 to 90%) of randomly permuted expression values from a naïve B cell reference transcriptome (median expression profile from samples used to build LM22, Supplementary Table 1). We then repeated this analysis for each of the remaining leukocyte subsets in LM22 (Supplementary Fig. 7b).
Newman A.M., Liu C.L., Green M.R., Gentles A.J., Feng W., Xu Y., Hoang C.D., Diehn M, & Alizadeh A.A. (2015). Robust enumeration of cell subsets from tissue expression profiles. Nature methods, 12(5), 453-457.
Publication 2015
B-Lymphocytes BLOOD Cell Lines Cytosol Genes Jurkat Cells Leukocyte Count Leukocytes Neoplasms Transcriptome
3
Transcription Factor Binding Profiles
Data used in this study are summarized in Supplementary Table 1 online. The NRSF ChIP-chip data (GEO accession #: GSE8489) were obtained by analyzing the bound DNA fragments in Jurkat cells with Affymetrix Human Tiling 2.0R arrays. Two independent ChIP samples and two mock IPs were profiled. The NRSF ChIP-seq data were collected from a previous study4 (link). In that study, DNA fragments bound by NRSF in Jurkat cells were sequenced with the next generation sequencer made by Illumina/Solexa. These experiments involved sequencing a ChIP'd sample as well as a negative control sample generated from reverse-crosslinked genomic DNA that had not undergone immunoprecipitation. The Oct4 and Nanog ChIP-seq data were collected from [10].
Ji H., Jiang H., Ma W., Johnson D.S., Myers R.M, & Wong W.H. (2008). An integrated system CisGenome for analyzing ChIP-chip and ChIP-seq data. Nature biotechnology, 26(11), 1293-1300.
Publication 2008
ChIP-Chip Chromatin Immunoprecipitation Sequencing DNA Chips Genome Homo sapiens Immunoprecipitation Jurkat Cells POU5F1 protein, human
4
Transcription Factor Binding Profiles
Data used in this study are summarized in Supplementary Table 1 online. The NRSF ChIP-chip data (GEO accession #: GSE8489) were obtained by analyzing the bound DNA fragments in Jurkat cells with Affymetrix Human Tiling 2.0R arrays. Two independent ChIP samples and two mock IPs were profiled. The NRSF ChIP-seq data were collected from a previous study4 (link). In that study, DNA fragments bound by NRSF in Jurkat cells were sequenced with the next generation sequencer made by Illumina/Solexa. These experiments involved sequencing a ChIP'd sample as well as a negative control sample generated from reverse-crosslinked genomic DNA that had not undergone immunoprecipitation. The Oct4 and Nanog ChIP-seq data were collected from [10].
Ji H., Jiang H., Ma W., Johnson D.S., Myers R.M, & Wong W.H. (2008). An integrated system CisGenome for analyzing ChIP-chip and ChIP-seq data. Nature biotechnology, 26(11), 1293-1300.
Publication 2008
ChIP-Chip Chromatin Immunoprecipitation Sequencing DNA Chips Genome Homo sapiens Immunoprecipitation Jurkat Cells POU5F1 protein, human
5
High-Resolution Intracellular Ca2+ Imaging
Cultured cells were transfected using Lipofectamine 2000 (Invitrogen) 2 or 3 days before imaging. Jurkat T cells were electroporated using a MicroPorator (MP-100, Digital Bio) 1 day before imaging. For cytosolic Ca2+ imaging using fura-2, cells were loaded with 5 μM fura-2 AM (Molecular Probes, USA) at room temperature (22–24 °C) for 40–60 min in 0.1% BSA-supplemented physiological salt solution (PSS) containing (in mM) 150 NaCl, 4 KCl, 2 CaCl2, 1 MgCl2, 5.6 glucose and 25 HEPES (pH 7.4). Before imaging, the loading solution was replaced with PSS without BSA.
The images were captured using an inverted microscope (IX81, Olympus, Japan) equipped with a × 20 objective (numerical aperture (NA)=0.75, UPlanSApo, Olympus) or a × 40 objective (NA 0.90, UApo/340, Olympus), an electron-multiplying cooled-coupled device (EM-CCD) camera (ImagEM, Hamamatsu Photonics, Japan), a filter wheel (Lambda 10-3, Sutter Instrument, USA), a xenon lamp (ebx75) and a metal halide lamp (EL6000, Leica, Germany) at a rate of one frame per 2 or 3 s with the following excitation/emission filter settings: 472±15 nm/520±17.5 nm for G-GECO1.1, CEPIA1er, G-CEPIA1er, CEPIA2–4mt and EYFP-er; 562±20 nm/641±37.5 nm for R-GECO1, R-CEPIA1er and mCherry-STIM1; 377±25 nm/466±20 nm and 377±25 nm/520±17.5 nm for GEM-GECO1 and GEM-CEPIA1er; 340±13 nm/510±42 nm and 365±6 nm/510±42 nm for fura-2; 440±10.5 nm/480±15 nm and 440±10.5 nm/535±13 nm for D1ER19 (link)20 (link). For analysis of the ratiometric indicators, we calculated the fluorescence ratio (F466/F520 for GEM-GECO1 and GEM-CEPIA1er; F340/F365 for fura-2; F535/F480 for D1ER). Photobleaching was corrected for using a linear fit to the fluorescence intensity change before agonist stimulation. All images were analysed with ImageJ software.
To image subcellular ER Ca2+ dynamics during agonist-induced Ca2+ wave formation, we imaged HeLa cells expressing either G-CEPIA1er or R-CEPIA1er. Images were captured at a rate of one frame per 30–100 ms using a × 60 objective (NA 1.45, PlanApo TIRF, Olympus) and the metal halide lamp or an LED lamp (pE-100, CoolLED, UK). To evaluate Ca2+ wave velocity in the ER and cytosol, images were normalized by the resting intensity, and a linear region of interest (ROI) was defined along the direction of wave propagation. A line-scan image was created by averaging 30 adjacent linear ROIs parallel to the original ROI, and time derivative was obtained to detect the time point that showed maximal change during the scan duration. Then, the time points were plotted against the pixel, and the wave velocity was estimated by the slope of the least-squares regression line.
For mitochondrial Ca2+ imaging with ER and cytosolic Ca2+, mitochondrial inner membrane potential or mitochondrial pH at subcellular resolution, we imaged HeLa cells with a confocal microscope (TCS SP8, Leica) equipped with a × 63 objective (NA 1.40, HC PL APO, Leica) at a rate of one frame per 2 or 3 s with the following excitation/emission spectra: R-GECO1mt (552 nm/560–800nm), G-CEPIA1er (488 nm/500–550 nm) and GEM-GECO1 (405 nm/500–550 nm); GEM-GECO1mt (405 nm/500–550 nm), JC-1 (488 nm/500–550 nm and 488 nm/560–800nm); R-GECO1mt (552 nm/560–800nm), SypHer-dmito (405 nm/500–550 nm and 488 nm/500–550 nm). For analysis of JC-1 and SypHer-dmito, we calculated the fluorescence ratio (488 nm/560–800 nm over 488 nm/500–550 nm for JC-1 (ref. 55 (link)); 488 nm/500–550 nm over 405 nm/500–550 nm for SypHer-dmito62 (link)).
To perform in situ Ca2+ titration of CEPIA, we permeabilized the plasma membrane of HeLa cells with 150 μM β-escin (Nacalai Tesque, Japan) in a solution containing (in mM) 140 KCl, 10 NaCl, 1 MgCl2 and 20 HEPES (pH 7.2). After 4 min treatment with β-escin, we applied various Ca2+ concentrations in the presence of 3 μM ionomycin and 3 μM thapsigargin, and estimated the maximum and minimum fluorescent intensity (Rmax and Rmin), dynamic range (Rmax/Rmin), Kd and n.
For the estimation of [Ca2+]ER based on the ratiometric measurement using GEM-CEPIA1er (Figs 1e,f and 5b and Supplementary Fig. 5f), [Ca2+]ER was obtained by the following equation:

where R=(F at 466 nm)/(F at 510 nm), n=1.37 and Kd=558 μM.
To evaluate pH-dependent change of EYFP-er fluorescence (Supplementary Fig. 4a–d), we stimulated HeLa cells expressing EYFP-er in a PSS (adjusted to pH 6.8) containing monensin (10 μM, Wako) and nigericin (10 μM, Wako). Subsequently, the cells were alkalinized with a solution containing (in mM) 120 NaCl, 30 NH4Cl, 4 KCl, 2 CaCl2, 1 MgCl2, 5 HEPES and 5.6 Glucose (pH 7.4)67 (link).
Suzuki J., Kanemaru K., Ishii K., Ohkura M., Okubo Y, & Iino M. (2014). Imaging intraorganellar Ca2+ at subcellular resolution using CEPIA. Nature Communications, 5, 4153.
Publication 2014
Aftercare Cells Cultured Cells Cytosol Electrons Escin Fingers Fluorescence Fura-2 fura-2-am Glucose HeLa Cells HEPES Ionomycin Jurkat Cells lipofectamine 2000 Magnesium Chloride Medical Devices Membrane Potential, Mitochondrial Metals Microscopy Microscopy, Confocal Mitochondria Molecular Probes Monensin Nigericin physiology Plasma Radionuclide Imaging Reading Frames Reproduction Sodium Chloride STIM1 protein, human Thapsigargin Titrimetry Xenon

Most recents protocols related to «Jurkat Cells»

1
Characterization of Anti-CD25 Antibodies
Not available on PMC !

Example 8

Antibody-dependent cell-mediated cytotoxicity assays (ADCC assays) were performed for the characterization of anti-human CD25 antibodies using CD25-expressing SR786 cells, herein called target (T) cells, incubated for 20 minutes at 37 C with different concentrations of anti-human CD25 antibodies in a low-IgG FBS-supplemented medium (4% FBS in RPMI). ADCC effector (E) cells are then added to the cell-mAbs mixture at an E:T ratio of 1:1. The effector cells are Jurkat cells stably transfected with a luciferase reporter system and over-expressing CD16/FcgammaRIIIA (Promega). After overnight incubation at 37 C, the cells are lysed and luciferase activity is measured by mean of luminescence release from the hydrolysis of a specific luciferase substrate, following manufacturer instruction (Promega Bio-Glow protocol). Graphs of the raw data are produced using Graphpad Prism v7 to generate dose response curves. The Relative Luminescences Units (RLU) are plotted on a XY chart against the log of the antibody concentration, and the data fir to a non-linear regression curve from which the EC50 is calculated.

US11873341B2. Anti-CD25 for tumour specific cell depletion (2024-01-16). Tusk Therapeutics Ltd. [GB], Cancer Research Technology Limited [GB]. Inventors: Anne Goubier [GB], Beatriz Goyenechea Corzo [GB], Josephine Salimu [GB], Kevin Moulder [GB], Pascal Merchiers [GB], Sergio Quezada [GB].
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Patent 2024
Anti-Antibodies anti-c antibody Biological Assay Cells Cytotoxicities, Antibody-Dependent Cell FCGR3A protein, human Homo sapiens Hydrolysis IL2RA protein, human Immunoglobulins Jurkat Cells Luciferases Luminescence Monoclonal Antibodies prisma Promega T-Lymphocyte
2
Lentiviral Transduction of Jurkat Cells
Not available on PMC !

Example 2

CAR-T constructs in pLenti6.3/V5-DEST were purified using the PureLink HQ plasmid purification kit (Life Technology). CAR-T plasmids were lipofected into 293-FT cells with ViraPower packaging plasmids (Life Technologies) according to the manufacturer's protocol. After 48-72 hours, cell supernatant containing live Lentivirus was harvested. Optionally, the virus was concentrated using Lenti-X Concentrator (Clontech), according to the manufacturer's protocol.

Jurkat E6.1 cells were grown in RPMI (Sigma), 10% foetal bovine serum, 2 mM L-glutamine

Jurkat E6.1 cells were transduced for 48-72 hours with viral supernatant in a 50:50 mix of HEK cell supernatant:Jurkat medium: cells at a final concentration of 5×105/ml.

A non-CAR-T construct containing the open reading frame of the Green Fluorescent Protein (GFP) was included as a control. Note that this construct gives cytoplasmic expression.

US11866510B2. Chimeric antigen receptor with single domain antibody (2024-01-09). CRESCENDO BIOLOGICS LIMITED [GB]. Inventors: Brian McGuinness [GB], Colette Johnston [GB].
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Patent 2024
Cells Cytoplasm Fetal Bovine Serum Glutamine Green Fluorescent Proteins Jurkat Cells Lentivirus Plasmids Virus
3
Cytotoxicity and Anti-Tumor Efficacy of Chimeric Protein
Not available on PMC !

Example 5

In Vitro Cytotoxicity Assay

Cells from the Jurkat cell line were treated with different doses of chimera. The result was that the chimera is toxic to Jurkat cells in a dose-dependent manner as can be seen in FIG. 10. Almost all the cells undergo apoptotic death with a chimera concentration of 6 μM.

HT29 cells were treated with different doses of GRNLY and chimera. The result was that both GRNLY and the chimera are toxic to HT29 cells in a dose-dependent manner as can be seen in FIG. 11. GRNLY or chimera concentrations of 4 or 5 μM seem to have a similar effect, but the chimera is more cytolytic than GRNLY at a concentration of 6 μM, achieving a percentage of growth of 30% with respect to the control, i.e., 70% cytotoxicity. To match said effect, a GRNLY concentration of about 20 μM must be used.

Furthermore, labeling was also performed with Alexa-46-conjugated annexin-V showing phosphatidylserine exposure and with 7AAD showing membrane integrity on HT29 cells treated with different concentrations of chimera for analyzing the type of induced cell death. By increasing the concentration of chimera, an increase in cells labeled with annexin which still have not lost membrane integrity is observed, indicating that cell death is caused by apoptosis (FIG. 12). Furthermore, a significant increase in cytotoxicity is observed when incubating the cells with a chimera concentration of 6 μM, as shown in FIG. 16. The maximum dose of chimera used was 6 μM, whereas in the case of GRNLY, a concentration of up to 20 μM was reached.

In Vivo Assay with HELA-CEA Cells

Five mice per group (control group, granulysin group, and MFE group (with the chimera) were assayed. Although there was a mouse in the MFE group that died after the sixth injection, the other 4 mice, however, reached the end of the experiment in good conditions state. The tumor was subcutaneously injected with Matrigel at 2 million cells. Treatments began when the tumors reached a size of 150 mm3. The treatments were systemic intraperitoneal treatments performed every two days (injections):

    • Control group, 500 ul of PBS.
    • Granulysin group, 220 ul of a stock at 500 ug/ml (40 uM), i.e., 110 ug per injection, which yields a concentration of about 5 uM in 2 ml of total blood.
    • MFE group, 500 ul of stocks of about 900 ug/ml (25 uM), i.e., 425 ug per injection, which yields a concentration of about 5 uM in 2 ml of total blood.

Ten injections were performed and the mice were sacrificed 2 days after the last injection.

The results are illustrated in FIGS. 13 to 19. FIG. 13 shows that if the control group is compared with MFE group (chimera), significant differences can be seen after the 7th injection, with the difference being very significant in the last injections. It can be seen how tumor growth in treated mice is somehow contained or attenuated. FIG. 14 shows that if the control group is compared with the (non-chimeric) granulysin group, there are no significant differences, although the granulysin curve is below the control curve for all the points. FIG. 15 shows all the results shown in FIG. 13 and FIG. 14. FIG. 16 shows the means±SD of the sizes of the tumors once removed and subjected to different treatments, a smaller tumor size with granulysin treatment, and an even smaller size when the chimera is used, being shown. FIG. 16 shows the means±SD of the weights of the tumors once removed and subjected to different treatments, a lower tumor weight with granulysin treatment, and an even lower weight when the chimera is used, being shown.

US11858973B2. Granulysin, method of obtaining same, and uses (2024-01-02). UNIVERSIDAD DE ZARAGOZA [ES], FUNDACIÓN AGENCIA ARAGONESA PARA LA INVESTIGACIÓN Y EL DESARROLLO (ARAID) [ES], FUNDACIÓN PARA LA INVESTIGACIÓN BIOMÉDICA HOSPITAL UNIVERSITARIO PUERTA DE HIERRO MAJADAHONDA [ES]. Inventors: Luis Alberto Anel Bernal [ES], Raquel Ibañez Perez [ES], Patricia Guerrero Ochoa [ES], Luis Martinez Lostao [ES], Blanca Conde Guerri [ES], Ramón Hurtado Guerrero [ES], Ana Laura Sanz Alcober [ES], Rocio Navarro Ortiz [ES].
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Patent 2024
7-aminoactinomycin D Annexin A5 Annexins Apoptosis BLOOD Cell Death Cell Lines Cells Chimera Cytotoxin GNLY protein, human HeLa Cells HT29 Cells Injections, Intraperitoneal Jurkat Cells matrigel Mus Neoplasms Phosphatidylserines Plasma Membrane Tissue, Membrane Vision
4
Lenti-GFP Transduction and CART Surface Expression
Not available on PMC !

Example 3

Cells transduced with Lenti-GFP as explained above were analysed on a Sony SH800Z flow cytometer with 488 laser. Signal from GFP transduced cells was compared with untransduced cells. The results are shown in FIG. 5. This demonstrates that transduction works.

Constructs expressing irrelevant VH with a HIS tag were shown by flow cytometry to have surface expression on Jurkat cells using anti-His detection agents. This shows that the leader sequence directs the CART to the surface of the cell as expected.

US11866510B2. Chimeric antigen receptor with single domain antibody (2024-01-09). CRESCENDO BIOLOGICS LIMITED [GB]. Inventors: Brian McGuinness [GB], Colette Johnston [GB].
Full text: Click here
Patent 2024
CART protein, human Flow Cytometry Jurkat Cells Lentivirus Signal Peptides Signal Transduction T-Lymphocyte
5
CD28 Binding Nanobody Verification
Not available on PMC !

EXAMPLE 41

To verify if the CD28-Fc binding clones could also bind to the native form of the CD28 antigen, serial dilutions of purified protein preparations of such clones were allowed to bind to the human Jurkat T-cell line, which expresses human CD28. Binding of putative CD28 reactive Nanobodies clones was detected using unlabeled anti-c-myc tag mouse monoclonal antibody 9E10, followed by a phycoerythrin conjugated F(ab′)2 derived from goat-anti-mouse IgG (human and bovine crossabsorbed), and read on a BD FACSarray instrument. Dead cells were excluded from the analysis by gating out TOPRO3 vital dye positive scoring cells. Binding of the Nanobodies to cells was evaluated in BD FACS array control software as PE channel histograms. Based on these FACS experiments, all CD28-Fc binding Nanobody clones bound cell expressed CD28. Results of a representative experiment are depicted in FIG. 23.

US11858997B2. Amino acid sequences that modulate the interaction between cells of the immune system (2024-01-02). Ablynx N.V. [BE]. Inventors: Guy Hermans [BE], Peter Verheesen [BE], Edward Dolk [NL], Hendricus Renerus Jacobus Mattheus Hoogenboom [NL], Michael John Scott Saunders [BE], Hans De Haard [NL], Renee de Bruin [NL].
Full text: Click here
Patent 2024
anti-c antibody anti-IgG Bos taurus CD28 Antigens Cell Lines Cells Clone Cells Goat Homo sapiens Jurkat Cells Mus Phycoerythrin Proteins T-Lymphocyte Technique, Dilution VHH Immunoglobulin Fragments

Top products related to «Jurkat Cells»

1
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.
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RPMI 1640 medium is a commonly used cell culture medium developed at Roswell Park Memorial Institute. It is a balanced salt solution that provides essential nutrients, vitamins, and amino acids to support the growth and maintenance of a variety of cell types in vitro.
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RPMI 1640 is a common cell culture medium used for the in vitro cultivation of a variety of cells, including human and animal cells. It provides a balanced salt solution and a source of essential nutrients and growth factors to support cell growth and proliferation.
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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.
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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.
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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.
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Lipofectamine 2000 by Thermo Fisher Scientific
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Lipofectamine 2000 is a cationic lipid-based transfection reagent designed for efficient and reliable delivery of nucleic acids, such as plasmid DNA and small interfering RNA (siRNA), into a wide range of eukaryotic cell types. It facilitates the formation of complexes between the nucleic acid and the lipid components, which can then be introduced into cells to enable gene expression or gene silencing studies.
9
Jurkat cell by American Type Culture Collection
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Jurkat cells are a human T lymphocyte cell line derived from the peripheral blood of a patient with T cell leukemia. They are widely used in research for their ability to rapidly proliferate and express T cell markers.
10
L glutamine by Thermo Fisher Scientific
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L-glutamine is an amino acid that is commonly used as a dietary supplement and in cell culture media. It serves as a source of nitrogen and supports cellular growth and metabolism.

More about "Jurkat Cells"

Jurkat cells are a widely utilized human T lymphocyte cell line that originated from an acute T cell leukemia.
These immortalized cells have been instrumental in the study of T cell signaling, activation, and apoptosis (programmed cell death).
Jurkat cells express a variety of T cell surface markers and exhibit many characteristics of immature T lymphocytes, making them a valuable model for investigating T cell biology and immunology.
Researchers can leverage the power of PubCompare.ai's AI-driven platform to easily locate the best Jurkat cell protocols from the published literature, preprints, and patents.
This optimizes experimental workflows and takes the guesswork out of Jurkat cell research.
The platform's comparison tools allow researchers to quickly identify the most effective Jurkat cell methods, from cell culture techniques to experimental assays.
When culturing Jurkat cells, it is common to use RPMI 1640 medium, which is a standard cell culture medium that provides the necessary nutrients and supplements for cell growth and maintenance.
Fetal bovine serum (FBS) is often added to the RPMI 1640 medium to further support cell proliferation and survival.
Antibiotics, such as penicillin and streptomycin, are also commonly included to prevent bacterial contamination.
In addition to RPMI 1640, researchers may also use other cell culture media, such as Dulbecco's Modified Eagle Medium (DMEM), depending on the specific requirements of their experiments.
Transfection reagents, like Lipofectamine 2000, are often utilized to introduce genetic material into Jurkat cells for various studies, such as gene expression analysis or gene silencing experiments.
By leveraging the comprehensive resources and advanced comparison tools provided by PubCompare.ai, researchers can streamline their Jurkat cell research, optimize their experimental protocols, and gain valuable insights into T cell biology and immunology.