Human Peripheral Blood Mononuclear Cells, Frozen

Primary human cells, frozen

Human Peripheral Blood Mononuclear Cells, Frozen

Primary human cells, frozen

From: 155 USD
Catalog #
70025_C
Primary human cells, frozen

Overview

Streamline your assays with ready-to-use, ethically sourced, primary human mononuclear cells. With personalized service, custom products, flexible delivery times, and the option to reserve entire lots to prescreen cells for applications, we help you get the cells you need.

Isolated from peripheral blood leukapheresis samples using density gradient separation and/or red blood cell lysis and cryopreserved in animal component-free CryoStor®CS10 medium (Catalog #07930), cells are collected using Institutional Review Board (IRB)-approved consent forms and protocols. Additional documentation and high-resolution HLA typing (Class I and Class II alleles and CMV status) are available upon request. Acid-citrate-dextrose solution A (ACDA) is added during collection as an anticoagulant. Donor specifications (e.g. BMI category, smoking status, ethnicity, etc.) can be requested in the comment box above, after selecting from the product options. Donors are screened for HIV-1, HIV-2, hepatitis B, and hepatitis C.

Certain products are only available in select territories. Please contact your local sales representative or Product & Scientific Support at techsupport@stemcell.com for further information.

Browse our Frequently Asked Questions (FAQs) on Primary Cells.
Contains
• CryoStor® CS10
Subtype
Frozen
Cell Type
Mononuclear Cells
Species
Human
Cell and Tissue Source
Peripheral Blood
Donor Status
Normal

Protocols and Documentation

Find supporting information and directions for use in the Product Information Sheet or explore additional protocols below.

Document Type
Product Name
Catalog #
Lot #
Language
Catalog #
70025, 70025.1, 70025.2, 70025.3
Lot #
All
Language
English

Resources and Publications

Publications (12)

Eradication of Triple-Negative Breast Cancer Cells by Targeting Glycosylated PD-L1. C.-W. Li et al. Cancer cell 2018 FEB

Abstract

Protein glycosylation provides proteomic diversity in regulating protein localization, stability, and activity; it remains largely unknown whether the sugar moiety contributes to immunosuppression. In the study of immune receptor glycosylation, we showed that EGF induces programmed death ligand 1 (PD-L1) and receptor programmed cell death protein 1 (PD-1) interaction, requiring beta$-1,3-N-acetylglucosaminyl transferase (B3GNT3) expression in triple-negative breast cancer. Downregulation of B3GNT3 enhances cytotoxic T cell-mediated anti-tumor immunity. A monoclonal antibody targeting glycosylated PD-L1 (gPD-L1) blocks PD-L1/PD-1 interaction and promotes PD-L1 internalization and degradation. In addition to immune reactivation, drug-conjugated gPD-L1 antibody induces a potent cell-killing effect as well as a bystander-killing effect on adjacent cancer cells lacking PD-L1 expression without any detectable toxicity. Our work suggests targeting protein glycosylation as a potential strategy to enhance immune checkpoint therapy.
Dendritic Cells but Not Macrophages Sense Tumor Mitochondrial DNA for Cross-priming through Signal Regulatory Protein α Signaling. Xu MM et al. Immunity 2017 AUG

Abstract

Inhibition of cytosolic DNA sensing represents a strategy that tumor cells use for immune evasion, but the underlying mechanisms are unclear. Here we have shown that CD47-signal regulatory protein α (SIRPα) axis dictates the fate of ingested DNA in DCs for immune evasion. Although macrophages were more potent in uptaking tumor DNA, increase of DNA sensing by blocking the interaction of SIRPα with CD47 preferentially occurred in dendritic cells (DCs) but not in macrophages. Mechanistically, CD47 blockade enabled the activation of NADPH oxidase NOX2 in DCs, which in turn inhibited phagosomal acidification and reduced the degradation of tumor mitochondrial DNA (mtDNA) in DCs. mtDNA was recognized by cyclic-GMP-AMP synthase (cGAS) in the DC cytosol, contributing to type I interferon (IFN) production and antitumor adaptive immunity. Thus, our findings have demonstrated how tumor cells inhibit innate sensing in DCs and suggested that the CD47-SIRPα axis is critical for DC-driven antitumor immunity.
Phosphorylation of NEUROG3 Links Endocrine Differentiation to the Cell Cycle in Pancreatic Progenitors. Krentz NAJ et al. Developmental cell 2017 APR

Abstract

During pancreatic development, proliferating pancreatic progenitors activate the proendocrine transcription factor neurogenin 3 (NEUROG3), exit the cell cycle, and differentiate into islet cells. The mechanisms that direct robust NEUROG3 expression within a subset of progenitor cells control the size of the endocrine population. Here we demonstrate that NEUROG3 is phosphorylated within the nucleus on serine 183, which catalyzes its hyperphosphorylation and proteosomal degradation. During progression through the progenitor cell cycle, NEUROG3 phosphorylation is driven by the actions of cyclin-dependent kinases 2 and 4/6 at G1/S cell-cycle checkpoint. Using models of mouse and human pancreas development, we show that lengthening of the G1 phase of the pancreatic progenitor cell cycle is essential for proper induction of NEUROG3 and initiation of endocrine cell differentiation. In sum, these studies demonstrate that progenitor cell-cycle G1 lengthening, through its actions on stabilization of NEUROG3, is an essential variable in normal endocrine cell genesis.

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