Human Peripheral Blood CD34+ Cells, Frozen

Primary human cells, frozen

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Human Peripheral Blood CD34+ Cells, Frozen

Primary human cells, frozen

2 x 105 cells

Please select one of the preferences above when ordering multiple quantities

Catalog #70040
988 USD

Human Peripheral Blood CD34+ Cells, Frozen

Primary human cells, frozen

5 x 105 cells

Please select one of the preferences above when ordering multiple quantities

Catalog #70040.1
2,328 USD

Human Peripheral Blood CD34+ Cells, Frozen

Primary human cells, frozen

1 x 106 cells

Please select one of the preferences above when ordering multiple quantities

Catalog #70040.2
3,864 USD

Overview

Primary human CD34+ cells were isolated from peripheral blood (PB) mononuclear cells (MNCs) using positive immunomagnetic separation techniques. PB was collected using one of the following anticoagulants: acid-citrate-dextrose (ACD), acid-citrate-dextrose solution A (ACDA), citrate-phosphate-dextrose (CPD), citrate-phosphate-double-dextrose (CP2D), or citrate-phosphate-dextrose-adenine (CPDA). CD34 is expressed on hematopoietic stem and progenitor cells.

Cells were obtained using Institutional Review Board (IRB)-approved consent forms and protocols.

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Contains:
• Serum-free cryopreservation medium
• 10% dimethyl sulfoxide (DMSO)
Subtype:
Frozen
Cell Type:
Hematopoietic Stem and Progenitor Cells
Species:
Human
Cell and Tissue Source:
Peripheral Blood
Donor Status:
Normal
Purity:
The purity of CD34+ cells is ≥ 85% by flow cytometry.

Scientific Resources

Product Documentation

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Educational Materials

(2)

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

Publications

(2)
PloS one 2014 MAY

Stimulus-selective regulation of human mast cell gene expression, degranulation and leukotriene production by fluticasone and salmeterol.

Catalli A et al.

Abstract

Despite the fact that glucocorticoids and long acting beta agonists are effective treatments for asthma, their effects on human mast cells (MC) appear to be modest. Although MC are one of the major effector cells in the underlying inflammatory reactions associated with asthma, their regulation by these drugs is not yet fully understood and, in some cases, controversial. Using a human immortalized MC line (LAD2), we studied the effects of fluticasone propionate (FP) and salmeterol (SM), on the release of early and late phase mediators. LAD2 cells were pretreated with FP (100 nM), SM (1 µM), alone and in combination, at various incubation times and subsequently stimulated with agonists substance P, C3a and IgE/anti-IgE. Degranulation was measured by the release of β-hexosaminidase. Cytokine and chemokine expression were measured using quantitative PCR, ELISA and cytometric bead array (CBA) assays. The combination of FP and SM synergistically inhibited degranulation of MC stimulated with substance P (33% inhibition compared to control, n = 3, P>05). Degranulation was inhibited by FP alone, but not SM, when MC were stimulated with C3a (48% inhibition, n = 3, P>05). As previously reported, FP and SM did not inhibit degranulation when MC were stimulated with IgE/anti-IgE. FP and SM in combination inhibited substance P-induced release of tumor necrosis factor (TNF), CCL2, and CXCL8 (98%, 99% and 92% inhibition, respectively, n = 4, P>05). Fluticasone and salmeterol synergistically inhibited mediator production by human MC stimulated with the neuropeptide substance P. This synergistic effect on mast cell signaling may be relevant to the therapeutic benefit of combination therapy in asthma.
PloS one 2013 JUL

Epo receptors are not detectable in primary human tumor tissue samples.

Elliott S et al.

Abstract

Erythropoietin (Epo) is a cytokine that binds and activates an Epo receptor (EpoR) expressed on the surface of erythroid progenitor cells to promote erythropoiesis. While early studies suggested EpoR transcripts were expressed exclusively in the erythroid compartment, low-level EpoR transcripts were detected in nonhematopoietic tissues and tumor cell lines using sensitive RT-PCR methods. However due to the widespread use of nonspecific anti-EpoR antibodies there are conflicting data on EpoR protein expression. In tumor cell lines and normal human tissues examined with a specific and sensitive monoclonal antibody to human EpoR (A82), little/no EpoR protein was detected and it was not functional. In contrast, EpoR protein was reportedly detectable in a breast tumor cell line (MCF-7) and breast cancer tissues with an anti-EpoR polyclonal antibody (M-20), and functional responses to rHuEpo were reported with MCF-7 cells. In another study, a functional response was reported with the lung tumor cell line (NCI-H838) at physiological levels of rHuEpo. However, the specificity of M-20 is in question and the absence of appropriate negative controls raise questions about possible false-positive effects. Here we show that with A82, no EpoR protein was detectable in normal human and matching cancer tissues from breast, lung, colon, ovary and skin with little/no EpoR in MCF-7 and most other breast and lung tumor cell lines. We show further that M-20 provides false positive staining with tissues and it binds to a non-EpoR protein that migrates at the same size as EpoR with MCF-7 lysates. EpoR protein was detectable with NCI-H838 cells, but no rHuEpo-induced phosphorylation of AKT, STAT3, pS6RP or STAT5 was observed suggesting the EpoR was not functional. Taken together these results raise questions about the hypothesis that most tumors express high levels of functional EpoR protein.
STEMCELL TECHNOLOGIES INC.’S QUALITY MANAGEMENT SYSTEM IS CERTIFIED TO ISO 13485. PRODUCTS ARE FOR RESEARCH USE ONLY AND NOT INTENDED FOR HUMAN OR ANIMAL DIAGNOSTIC OR THERAPEUTIC USES UNLESS OTHERWISE STATED.