ImmunoCult™ Human CD3/CD28/CD2 T Cell Activator

Human T cell activation and expansion reagent

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Human T cell activation and expansion reagent
From: 139 USD

Overview

ImmunoCult™ Human CD3/CD28/CD2 T Cell Activator is designed to activate and expand human T cells in the absence of magnetic beads, feeder cells or antigen. ImmunoCult™ Human CD3/CD28/CD2 T Cell Activator consists of soluble tetrameric antibody complexes that bind CD3, CD28 and CD2 cell surface ligands. Binding of the tetrameric antibody complexes results in the cross-linking of CD3, CD28, and CD2 cell surface ligands, thereby providing the required primary and co-stimulatory signals for T cell activation. Activated T cells can be expanded in ImmunoCult™-XF T Cell Expansion Medium or other media for culturing human T cells supplemented with cytokines.

This product is designed for cell therapy research applications following the recommendations of USP<1043> on Ancillary Materials, and we can currently work with you to qualify this reagent under an approved investigational new drug (IND) or clinical trial application (CTA).

This product aims to be developed as a cGMP-grade reagent for cellular therapy research. Learn more at www.stemcell.com/t-cell-therapy
Advantages:
• 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
Contains:
• Anti-human CD3 monospecific tetrameric antibody complex
• Anti-human CD28 monospecific tetrameric antibody complex
• Anti-human CD2 monospecific tetrameric antibody complex
Subtype:
Supplements
Cell Type:
T Cells; T Cells, CD4+; T Cells, CD8+
Species:
Human
Application:
Activation; Cell Culture; Expansion
Brand:
ImmunoCult
Area of Interest:
Immunology; Cell Therapy

Scientific Resources

Educational Materials

(18)
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Product Applications

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.

Data and Publications

Data

Activated Morphology of Human T Cells Stimulated With ImmunoCult™ Human CD3/CD28/CD2 T Cell Activator

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).

Activation of EasySep™ Isolated Human T Cells Stimulated With ImmunoCult™ Human CD3/CD28/CD2 T Cell Activator

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.

Robust Human T Cell Expansion 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).

Publications

(5)
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.

Abstract

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.
Stem Cell Research 2019 oct

Detection of all adult Tau isoforms in a 3D culture model of iPSC-derived neurons

L. Miguel et al.

Abstract

Tauopathies are a class of neurodegenerative diseases characterized by the presence of pathological intracellular deposits of Tau proteins. Six isoforms of Tau are expressed in the adult human brain, resulting from alternative splicing of the MAPT gene. Tau splicing is developmentally regulated such that only the smallest Tau isoform is expressed in fetal brain, contrary to the adult brain showing the expression of all 6 isoforms. Induced Pluripotent Stem Cell (iPSC) technology has opened up new perspectives in human disease modeling, including tauopathies. However, a major challenge to in vitro recapitulation of Tau pathology in iPSC-derived neurons is their relative immaturity. In this study, we examined the switch in Tau splicing from fetal-only to all adult Tau isoforms during the differentiation of iPSC-derived neurons in a new 3D culture system. First, we showed that iPSC-induced neurons inside Matrigel-coated alginate capsules were able to differentiate into cortical neurons. Then, using a new assay that allowed both the qualitative and the quantitative analysis of all adult MAPT mRNA isoforms individually, we demonstrated that BrainPhys-maintained neurons expressed the 6 adult MAPT mRNA transcripts from 25 weeks of maturation, making this model highly suitable for modeling Tau pathology and therapeutic purposes.
Scientific reports 2019 nov

PD-1+ melanocortin receptor dependent-Treg cells prevent autoimmune disease.

F. Muhammad et al.

Abstract

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.

Abstract

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.

Abstract

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.