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EasySep? RBC Depletion Reagent

Immunomagnetic depletion of RBCs

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EasySep? RBC Depletion Reagent

Immunomagnetic depletion of RBCs

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Immunomagnetic depletion of RBCs
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Product Advantages


  • 99.9% RBC depletion without the need for density gradient centrifugation, sedimentation or lysis

  • Fast, easy-to-use and column-free

  • Isolated cells are untouched

What's Included

  • EasySep? RBC Depletion Reagent (Catalog #18170)
    • EasySep? RBC Depletion Reagent, 10 mL
  • EasySep? RBC Depletion Reagent for RoboSep? (Catalog #18170RF)
    • EasySep? RBC Depletion Reagent for RoboSep?, 4 x 2.5 mL
    • RoboSep? Buffer (Catalog #20104) x 2
    • RoboSep? Filter Tips (Catalog #20125) x 2

Overview

The EasySep? RBC Depletion Reagent is designed to immunomagnetically deplete red blood cells (RBCs) from fresh human peripheral blood, umbilical cord blood, bone marrow, or leukapheresis samples by negative selection. RBCs are labeled with antibody complexes recognizing Glycophorin A and magnetic particles. Labeled cells are separated using an EasySep? magnet without the use of columns. Unwanted cells remain in the tube while desired cells are poured off.

This product replaces the EasySep? Human Glycophorin A Depletion Kit (Catalog #18352) for even faster cell isolations.

Learn more about how immunomagnetic EasySep? technology works. Explore additional products optimized for your workflow, including culture media, supplements, antibodies, and more.
Magnet Compatibility
? EasySep? Magnet (Catalog #18000)
? “The Big Easy” EasySep? Magnet (Catalog #18001)
? EasyEights? EasySep? Magnet (Catalog #18103)
? Easy 50 EasySep? Magnet (Catalog #18002)
? EasyPlate? EasySep? Magnet (Catalog #18102)
Species
Human
Sample Source
Whole Blood
Selection Method
Negative
Brand
EasySep, RoboSep
Area of Interest
Chimerism, Drug Discovery and Toxicity Testing, HLA, Immunology

Data Figures

Figure 1. EasySep? RBC Depletion Reagent Provides Superior RBC Depletion Compared to Ammonium Chloride Lysis

Different types of RBC-containing samples from normal healthy donors were processed to remove RBCs by using either ammonium chloride (NH4Cl) lysis or immunomagnetic depletion with EasySep? RBC Depletion Reagent. After RBC removal, samples were stained with fluorochrome-conjugated anti-CD45 and anti-Glycophorin A antibodies and analyzed by flow cytometry. Residual RBCs were identified as Glycophorin A+/CD45? events. (A) The percentages of residual RBCs in various samples following use of EasySep? RBC Depletion Reagent was significantly lower compared to samples treated with ammonium chloride (mean ± SD; n = 31). (B) Both, RBC lysis with ammonium chloride and RBC removal using EasySep? RBC Depletion Reagent resulted in an equivalent total number of white blood cells recovered from whole blood samples (mean ± SD; n = 37).

Figure 2. Typical RBC Removal Using EasySep? RBC Depletion Reagent With Human Whole Blood Samples

Starting with human whole blood from normal healthy donors, the percentage of residual RBCs (Glycophorin A+/CD45-) following use of EasySep? RBC Depletion Reagent is typically 2 ± 3 (mean ± SD; n = 31). In the above example, the residual RBC content is 0.05%.

Figure 3. Typical RBC Removal Using EasySep? RBC Depletion Reagent With Human Bone Marrow Samples

Starting with human bone marrow, the percentage of residual RBCs (Glycophorin A+/CD45-) following use of EasySep? RBC Depletion Reagent is typically 0.39 ± 0.34 (mean ± SD; n = 5). In the above example, the residual RBC content is 0.57%.

Figure 4. Typical RBC Removal Using EasySep? RBC Depletion Reagent With Buffy Coat Samples

Starting with buffy coat, the percentage of residual RBCs (Glycophorin A+/CD45-) following use of EasySep? RBC Depletion Reagent is typically 0.12 ± 0.08 (mean ± SD; n = 6). In the above example, the residual RBC content is 0.26%.

Figure 5. Typical RBC Removal Using EasySep? RBC Depletion Reagent With Cord Blood Samples

Starting with cord blood, the percentage of residual RBCs (Glycophorin A+/CD45-) following use of EasySep? RBC Depletion Reagent is typically 1.7 ± 2.2 (mean ± SD; n = 16). In the above example, the residual RBC content is 0.08%.

Figure 6. Typical RBC Removal Using EasySep? RBC Depletion Reagent With Leukapheresis Samples

Starting with leukapheresis samples, the percentage of residual RBCs (Glycophorin A+/CD45-) following use of EasySep? RBC Depletion Reagent is typically 0.5 ± 0.8 (mean ± SD; n = 15). In the above example, the residual RBC content is 0.6%.

Protocols and Documentation

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

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18170RF
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18170RF
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18170RF
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18170
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English
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18170RF
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18170RF
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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.

Resources and Publications

Publications (7)

Cellular interactions within the immune microenvironment underpins resistance to cell cycle inhibition in breast cancers Nature Communications 2025 Mar

Abstract

Immune evasion by cancer cells involves reshaping the tumor microenvironment (TME) via communication with non-malignant cells. However, resistance-promoting interactions during treatment remain lesser known. Here we examine the composition, communication, and phenotypes of tumor-associated cells in serial biopsies from stage II and III high-risk estrogen receptor positive (ER+?) breast cancers of patients receiving endocrine therapy (letrozole) as single agent or in combination with ribociclib, a CDK4/6-targeting cell cycle inhibitor. Single-cell RNA sequencing analyses on longitudinally collected samples show that in tumors overcoming the growth suppressive effects of ribociclib, first cancer cells upregulate cytokines and growth factors that stimulate immune-suppressive myeloid differentiation, resulting in reduced myeloid cell- CD8?+?T-cell crosstalk via IL-15/18 signaling. Subsequently, tumors growing during treatment show diminished T-cell activation and recruitment. In vitro, ribociclib does not only inhibit cancer cell growth but also T cell proliferation and activation upon co-culturing. Exogenous IL-15 improves CDK4/6 inhibitor efficacy by augmenting T-cell proliferation and cancer cell killing by T cells. In summary, response to ribociclib in stage II and III high-risk ER?+? breast cancer depends on the composition, activation phenotypes and communication network of immune cells. The CDK4/6 inhibitor ribociclib holds promise in cancer therapy but how cell cycle inhibitory drugs affect the anti-tumor immune response remains a question. Here authors show that poor response of early-stage estrogen receptor positive breast cancers to ribociclib is caused by changes in the immune cell composition and cancer-cell-immune-cell communication in the tumors rather than intrinsic cancer cell resistance to cell cycle inhibition.
A cell atlas of the human fallopian tube throughout the menstrual cycle and menopause Nature Communications 2025 Jan

Abstract

The fallopian tube undergoes extensive molecular changes during the menstrual cycle and menopause. We use single-cell RNA and ATAC sequencing to construct a comprehensive cell atlas of healthy human fallopian tubes during the menstrual cycle and menopause. Our scRNA-seq comparison of 85,107 pre- and 46,111 post-menopausal fallopian tube cells reveals substantial shifts in cell type frequencies, gene expression, transcription factor activity, and cell-to-cell communications during menopause and menstrual cycle. Menstrual cycle dependent hormonal changes regulate distinct molecular states in fallopian tube secretory epithelial cells. Postmenopausal fallopian tubes show high chromatin accessibility in transcription factors associated with aging such as Jun, Fos, and BACH1/2, while hormone receptors were generally downregulated, a small proportion of secretory epithelial cells had high expression of ESR2, IGF1R, and LEPR. While a pre-menopausal secretory epithelial gene cluster is enriched in the immunoreactive molecular subtype, a subset of genes expressed in post-menopausal secretory epithelial cells show enrichment in the mesenchymal molecular type of high-grade serous ovarian cancer. The fallopian tube undergoes extensive cellular and molecular changes during the menstrual cycle and aging. Here, Weigert et al. present a single-cell atlas of the normal human fallopian tube revealing the transition of secretory epithelial cells throughout the menstrual cycle and menopause.
Proteasome localization and activity in pig brain and Frontiers in Cellular Neuroscience 2024 Feb

Abstract

IntroductionLoss of proteasome function, proteinopathy, and proteotoxicity may cause neurodegeneration across the human lifespan in several forms of brain injury and disease. Drugs that activate brain proteasomes in vivo could thus have a broad therapeutic impact in neurology.MethodsUsing pigs, a clinically relevant large animal with a functionally compartmental gyrencephalic cerebral cortex, we evaluated the localization and biochemical activity of brain proteasomes and tested the ability of small molecules to activate brain proteasomes.ResultsBy Western blotting, proteasome protein subunit PSMB5 and PSMA3 levels were similar in different pig brain regions. Immunohistochemistry for PSMB5 showed localization in the cytoplasm (diffuse and particulate) and nucleus (cytoplasm < nucleus). Some PSMB5 immunoreactivity was colocalized with mitochondrial (voltage-gated anion channel and cyclophilin D) and cell death (Aven) proteins in the neuronal soma and neuropil in the neocortex of pig and human brains. In the nucleus, PSMB5 immunoreactivity was diffuse, particulate, and clustered, including perinucleolar decorations. By fluorogenic assay, proteasome chymotrypsin-like activities (CTL) in crude tissue soluble fractions were generally similar within eight different pig brain regions. Proteasome CTL activity in the hippocampus was correlated with activity in nasal mucosa biopsies. In pilot analyses of subcellular fractions of pig cerebral cortex, proteasome CTL activity was highest in the cytosol and then ~50% lower in nuclear fractions; ~15–20% of total CTL activity was in pure mitochondrial fractions. With in-gel activity assay, 26S-singly and -doubly capped proteasomes were the dominant forms in the pig cerebral cortex. With a novel in situ histochemical activity assay, MG132-inhibitable proteasome CTL activity was localized to the neuropil, as a mosaic, and to cell bodies, nuclei, and centrosome-like perinuclear satellites. In piglets treated intravenously with pyrazolone derivative and chlorpromazine over 24 h, brain proteasome CTL activity was modestly increased.DiscussionThis study shows that the proteasome in the pig brain has relative regional uniformity, prominent nuclear and perinuclear presence with catalytic activity, a mitochondrial association with activity, 26S-single cap dominance, and indications from small molecule systemic administration of pyrazolone derivative and chlorpromazine that brain proteasome function appears safely activable.
New look, same high quality and support! You may notice that your instrument or reagent packaging looks slightly different from images displayed on the website, or from previous orders. We are updating our look but rest assured, the products themselves and how you should use them have not changed. Learn more