Achieve robust activation and expansion of T cells in the absence of magnetic beads, feeder cells, or antigens.
This product’s gentle activation stimulus ensures a high viability of activated T cells, which can be further expanded in ImmunoCult™-XF T Cell Expansion Medium (Catalog #10981) or other media for culturing human T cells. ImmunoCult™ Human CD3/CD28/CD2 T Cell Activator consists of soluble antibody complexes that bind to and cross-link CD3, CD28, and CD2 cell surface ligands, thereby providing the required primary and co-stimulatory signals for T cell activation.
This product is designed for cell therapy research applications, but may be qualified for use as an ancillary material (AM) following the framework outlined in USP<1043>. STEMCELL can work with you to qualify this reagent as an AM under an approved investigational new drug (IND) or clinical trial application (CTA). Learn more about how we can support your regulatory needs here.
• Robust activation and expansion of human T cells without the use of magnetic beads, feeder cells, or antigen
• Provides a gentle activation stimulus that maintains high viability of activated and expanded T cells
• Highly stable, filter-sterilized soluble reagent
T Cell Reagents for Your Cellular Therapy Research
Optimization of Human T Cell Expansion Protocol: Effects of Early Cell Dilution
Human Immune Cytokines
Antigen Processing and Presentation
The Immune Response to HIV Poster
Production of Chimeric Antigen Receptor T Cells
Frequencies of Cell Types in Human Peripheral Blood
How EasySep™ Magnetic Cell Separation Technology Works: Fast and Easy Cell Isolation
CAR T Cell Manufacturing Workflow: Isolation, Activation and Expansion
How to Isolate PBMCs from Whole Blood Using Density Gradient Centrifugation (Ficoll™ or Lymphoprep™)
How to Isolate Cells Directly from Whole Blood Using the EasySep™ Purple/Silver Magnets
Qualification of Ancillary/Raw Materials for Clinical Use
T Cell Differentiation and Cancer Immunity
Online Immunology Journal Club: Human In Vitro T Cell Development
Rapid Expansion of Functional Human T Cells Using a Novel Serum-Free and Xeno-Free Culture Medium
Optimization of Human T Cell Activation and Expansion Protocols Improves Efficiency of Genetic Modification and Overall Cell Yield
Workflow Solutions for Human T Cell Isolation and Expansion
Load More Educational Materials
This product is designed for use in the following research area(s) as part of the highlighted workflow stage(s). Explore these workflows to learn more about the other products we offer to support each research area.
Figure 1. Activated Morphology of Human T Cells Stimulated With ImmunoCult™ Human CD3/CD28/CD2 T Cell Activator
Image of human T cells isolated using the EasySep™ Human T Cell Isolation Kit (Catalog #17951), stimulated with ImmunoCult™ Human CD3/CD28/CD2 T Cell Activator, and cultured in ImmunoCult™-XF T Cell Expansion Medium (Catalog #10981).
Figure 2. Activation of EasySep™ Isolated Human T Cells Stimulated With ImmunoCult™ Human CD3/CD28/CD2 T Cell Activator
EasySep™-isolated human T cells were stimulated with ImmunoCult™ Human CD3/CD28/CD2 T Cell Activator and cultured in ImmunoCult™-XF T Cell Expansion Medium. Activation of viable CD3+ T cells was assessed by CD25 expression using flow cytometry. On day 0, the frequency of CD25 positive cells was (A) 5.6 ± 2.4% (mean ± SD). Following 3 days of culture, the frequency of CD25 positive cells was (B) 88.8 ± 3.2% (mean ± SD) when stimulated with ImmunoCult™ Human CD3/CD28/CD2 T Cell Activator.
Figure 3. Robust Human T Cell Expansion with ImmunoCult™ Human CD3/CD28/CD2 T Cell Activator
EasySep™-isolated human T cells were expanded over 12 days with ImmunoCult™ Human CD3/CD28/CD2 T Cell Activator in ImmunoCult™-XF T Cell
Expansion Medium supplemented with Human Recombinant IL-2. On day 0, 1 x 10^6 EasySep™-isolated human T cells were stimulated with 25 μL of
ImmunoCult™ Human CD3/CD28/CD2 T Cell Activator in ImmunoCult™-XF T Cell Expansion Medium supplemented with 10 ng/mL Human Recombinant
IL-2. On days 3, 5, 7, and 10, viable cells were counted and fresh medium supplemented with IL-2 was added. No additional ImmunoCult™ Human
CD3/CD28/CD2 T Cell Activator was added during the 12-day culture period (mean ± SD in 6 experiments with 3 donors).
Cancer research 2020 sep
Plasma Gelsolin Inhibits CD8+ T-cell Function and Regulates Glutathione Production to Confer Chemoresistance in Ovarian Cancer.
M. Asare-Werehene et al.
Although initial treatment of ovarian cancer is successful, tumors typically relapse and become resistant to treatment. Because of poor infiltration of effector T cells, patients are mostly unresponsive to immunotherapy. Plasma gelsolin (pGSN) is transported by exosomes (small extracellular vesicle, sEV) and plays a key role in ovarian cancer chemoresistance, yet little is known about its role in immunosurveillance. Here, we report the immunomodulatory roles of sEV-pGSN in ovarian cancer chemoresistance. In chemosensitive conditions, secretion of sEV-pGSN was low, allowing for optimal CD8+ T-cell function. This resulted in increased T-cell secretion of IFN$\gamma$, which reduced intracellular glutathione (GSH) production and sensitized chemosensitive cells to cis-diaminedichloroplatinum (CDDP)-induced apoptosis. In chemoresistant conditions, increased secretion of sEV-pGSN by ovarian cancer cells induced apoptosis in CD8+ T cells. IFN$\gamma$ secretion was therefore reduced, resulting in high GSH production and resistance to CDDP-induced death in ovarian cancer cells. These findings support our hypothesis that sEV-pGSN attenuates immunosurveillance and regulates GSH biosynthesis, a phenomenon that contributes to chemoresistance in ovarian cancer. SIGNIFICANCE: These findings provide new insight into pGSN-mediated immune cell dysfunction in ovarian cancer chemoresistance and demonstrate how this dysfunction can be exploited to enhance immunotherapy.
Science advances 2020 may
Competition between PAF1 and MLL1/COMPASS confers the opposing function of LEDGF/p75 in HIV latency and proviral reactivation.
R. Gao et al.
Transcriptional status determines the HIV replicative state in infected patients. However, the transcriptional mechanisms for proviral replication control remain unclear. In this study, we show that, apart from its function in HIV integration, LEDGF/p75 differentially regulates HIV transcription in latency and proviral reactivation. During latency, LEDGF/p75 suppresses proviral transcription via promoter-proximal pausing of RNA polymerase II (Pol II) by recruiting PAF1 complex to the provirus. Following latency reversal, MLL1 complex competitively displaces PAF1 from the provirus through casein kinase II (CKII)-dependent association with LEDGF/p75. Depleting or pharmacologically inhibiting CKII prevents PAF1 dissociation and abrogates the recruitment of both MLL1 and Super Elongation Complex (SEC) to the provirus, thereby impairing transcriptional reactivation for latency reversal. These findings, therefore, provide a mechanistic understanding of how LEDGF/p75 coordinates its distinct regulatory functions at different stages of the post-integrated HIV life cycles. Targeting these mechanisms may have a therapeutic potential to eradicate HIV infection.
Scientific reports 2019 nov
PD-1+ melanocortin receptor dependent-Treg cells prevent autoimmune disease.
F. Muhammad et al.
Experimental autoimmune uveoretinitis (EAU) is a mouse model of human autoimmune uveitis marked by ocular autoantigen-specific regulatory immunity in the spleen. The melanocortin 5 receptor (MC5r) and adenosine 2 A receptor (A2Ar) are required for induction of post-EAU regulatory T cells (Tregs) which provide resistance to EAU. We show that blocking the PD-1/PD-L1 pathway prevented suppression of EAU by post-EAU Tregs. A2Ar induction of PD-1+FoxP3+ Tregs in uveitis patients was similar compared to healthy controls, but was significantly reduced with melanocortin stimulation. Further, lower body mass index correlated with responsiveness to stimulation of this pathway. These observations indicate an importance of the PD-1/PD-L1 pathway to provide resistance to relapsing uveitis and shows a reduced capacity of uveitis patients to induce Tregs when stimulated through melanocortin receptors, but that it is possible to bypass this part of the pathway through direct stimulation of A2Ar.
The Journal of clinical investigation 2019 dec
Myalgic encephalomyelitis/chronic fatigue syndrome patients exhibit altered T cell metabolism and cytokine associations.
A. H. Mandarano et al.
Myalgic encephalomyelitis/chronic fatigue syndrome (ME/CFS) is a complex disease with no known cause or mechanism. There is an increasing appreciation for the role of immune and metabolic dysfunction in the disease. ME/CFS has historically presented in outbreaks, often has a flu-like onset, and results in inflammatory symptoms. Patients suffer from severe fatigue and post-exertional malaise. There is little known about the metabolism of specific immune cells in ME/CFS patients. To investigate immune metabolism in ME/CFS, we isolated CD4+ and CD8+ T cells from 53 ME/CFS patients and 45 healthy controls. We analyzed glycolysis and mitochondrial respiration in resting and activated T cells, along with markers related to cellular metabolism, and plasma cytokines. We found that ME/CFS CD8+ T cells have reduced mitochondrial membrane potential compared to healthy controls. Both CD4+ and CD8+ T cells from ME/CFS patients had reduced glycolysis at rest, while CD8+ T cells also had reduced glycolysis following activation. ME/CFS patients had significant correlations between measures of T cell metabolism and plasma cytokine abundance that differed from healthy control subjects. Our data indicate that patients have impaired T cell metabolism consistent with ongoing immune alterations in ME/CFS that may illuminate the mechanism behind this disease.
Blood 2016 JUL
LFA-1 integrin antibodies inhibit leukocyte α4β1-mediated adhesion by intracellular signaling.
Grö et al.
Binding of ICAM-1 (intercellular adhesion molecule-1) to the β2-integrin LFA-1 (leukocyte function associated antigen-1) is known to induce crosstalk to the α4β1 integrin. Using different LFA-1 monoclonal antibodies we have been able to study the requirement and mechanism of action for the crosstalk in considerable detail. LFA-1 activating antibodies and those inhibitory antibodies that signal to α4β1 induce phosphorylation of Thr-758 on the β2-chain, which is followed by binding of 14-3-3 proteins and signaling through the G protein exchange factor Tiam1. This results in dephosphorylation of Thr-788/789 on the β1-chain of α4β1 and loss of binding to its ligand VCAM-1 (vascular cell adhesion molecule-1). The results show that with LFA-1 antibodies, we can either 1) activate LFA-1 and inhibit α4β1, 2) inhibit both LFA-1 and α4β1, 3) inhibit LFA-1 but not α4β1 or 4) not affect LFA-1 or α4β1 These findings are important for the understanding of integrin regulation and for the interpretation of the effect of integrin antibodies and their use in clinical applications.
PRODUCTS ARE FOR RESEARCH USE ONLY AND NOT INTENDED FOR HUMAN OR ANIMAL DIAGNOSTIC OR THERAPEUTIC USES UNLESS OTHERWISE STATED. FOR ADDITIONAL INFORMATION ON QUALITY AT STEMCELL, REFER TO WWW.STEMCELL.COM/COMPLIANCE.
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