Cd163

Manufactured by R&D Systems

Sourced in United States

CD163 is a cell surface glycoprotein that functions as a scavenger receptor. It is primarily expressed on the surface of monocytes and macrophages. CD163 plays a role in the clearance of hemoglobin-haptoglobin complexes from the bloodstream.

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Lab products found in correlation

Recombinant human cd163, by R&D Systems (2 mentions) Cd163 immunoassay kit, by R&D Systems (2 mentions) Anti cd163, by R&D Systems (2 mentions) Ifn α, by PBL Assay Science (1 mentions) Luminex magpix, by Merck Group (1 mentions) Hemoglobin, by Merck Group (1 mentions) J774a 1 cells, by American Type Culture Collection (1 mentions) Cell culture media, by Merck Group (1 mentions) Fetal bovine serum (fbs), by Thermo Fisher Scientific (1 mentions) Anti cd56, by Beckman Coulter (1 mentions) Anti cd3, by Beckman Coulter (1 mentions) Anti cd19, by Beckman Coulter (1 mentions) Facsdiva software, by BD (1 mentions) Lsrii cytometer, by BD (1 mentions) Facsverse, by FlowJo (1 mentions) Facscalibur, by FlowJo (1 mentions) Jagged1, by R&D Systems (1 mentions) Accutase, by Innovative Cell Technologies (1 mentions) Cd206, by BD (1 mentions) Lsrfortessa flow cytometer, by BD (1 mentions)

10 protocols using cd163

Quantification of Inflammation Biomarkers in CVL

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Inflammation biomarkers were quantified in CVL from Group 2 women using a Milliplex 17-plex kit (Millipore) run on Luminex
MagPix (GM-CSF, IFN-γ, IL-10, IL-12p40, IL-12p70, IL-15, IL-1RA, IL-1α, IL-2, IL-4, IL-6, IL-8, IP10, MCP-1,
MIP-1β, RANTES, and TNFα). Five additional biomarkers were tested by ELISA: CD163 (R&D Systems), SLPI (R&D
Systems), IFN-α (PBL Assay Science), and beta-defensins 2 and 3 (Assay Biotech).

Nelson J.A., PARIS K.D., RAMIREZ C., EDMONDS A., MOLLAN K.R., BAY C.P., COMPLIMENT K., HEROLD B.C., ANASTOS K., MINKOFF H., KASSAYE S., SEIDMAN D.L., FRENCH A.L., GOLUB E.T., SHETH A.N., OCHSENBAUER C., SWANSTROM R., ERON J.J, & ADIMORA A.A. (2020). Female Genital Tract Shedding of HIV-1 is Rare in Women with Suppressed HIV-1 in Plasma. AIDS (London, England), 34(1), 39-46.

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Radiolabeled peptide characterization

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Cell culture media and hemoglobin were obtained from Sigma-Aldrich (St. Louis, MO, USA), fetal bovine serum (FBS) from Gibco (Rockville, MD, USA), bovine serum albumin (BSA) (Fraction V) from USB (Cleveland, OH, USA). J774A.1 cells were obtained from ATCC (catalog number TIB-67) and human coronary endothelial cells from Lonza (Basel, Switzerland). CD163 was obtained from R&D Systems, Inc. (Minneapolis, MN, USA). Common Laboratory Chemicals were purchased from Fisher Scientific or Sigma. Peptide was synthesized, per our amino acid sequence plan, by Chinese Peptides Company, (Hangzhou, China) and fully characterized by nuclear magnetic resonance (NMR), carbon, hydrogen and nitrogen (C,H,N) composition analyses and by MALDI/FAB mass spectrometry. ¹¹¹InCl₃ (Nordion Inc., Ottawa, ON, Canada) was supplied by Nuclear and Energy Research Institute (IPEN)/CNEN, (São Paulo, Brazil). HPLC analysis were performed in a Shimadzu VP series equipment (Shimadzu, Japan) connected to radiation detector Flow Scintillation Analyzer, Radiomatic 610RT (PerkinElmer, Boston, MA, USA).

Silva R.A., Giordano R.J., Gutierrez P.S., Rocha V.Z., Rudnicki M., Kee P., Abdalla D.S., Puech-Leão P., Caramelli B., Arap W., Pasqualini R., Meneghetti J.C., Marques F.L., Khoobchandani M., Katti K.V., Lugão A.B, & Kalil J. (2016). CTHRSSVVC Peptide as a Possible Early Molecular Imaging Target for Atherosclerosis. International Journal of Molecular Sciences, 17(9), 1383.

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Quantification of Der p1-CD163 Binding

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Plastic 96 well plates were coated with purified Der p1 and blocked with 1% bovine serum albumin dissolved in PBS. Recombinant human CD163 (R&D Systems, Inc., Minneapolis, MN) (120 ng) was added to the Der p1-coated plates overnight, washed 3 times with 0.05% Tween 20 in PBS, and the quantity of CD163 that bound to the immobilized Der p1 was quantified using a CD163 immunoassay kit (R&D Systems, Inc., Minneapolis, MN) with a horseradish peroxidase conjugated anti-CD163 antibody. Non-specific binding of the anti-CD163 antibody to Der p1-coated plates in the absence of CD163, as well as background related to the immobilized Der p1 protein in the absence of the anti-CD163 antibody were subtracted from the reported values.

Dai C., Yao X., Gordon E.M., Barochia A., Cuento R.A., Kaler M., Meyer K.S., Keeran K.J., Nugent G.Z., Jeffries K.R., Qu X., Yu Z.X., Aponte A., Gucek M., Dagur P.K., McCoy J.P, & Levine S.J. (2015). A CCL24-dependent Pathway Augments Eosinophilic Airway Inflammation in House Dust Mite-challenged Cd163−/− Mice. Mucosal immunology, 9(3), 702-717.

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Phenotyping of Mononuclear Cells

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Phenotyping of mononuclear cells was performed in 1% BSA and 3% human serum-PBS according to standard methods using a panel of antibodies directed against monocytes, T- and B-lymphocytes, natural killer cells and red cells. The following conjugated antibodies were used: anti-CD19 (Beckman Coulter Cat# IM1284U, RRID:AB_131011), anti-CD56 (Beckman Coulter Cat# IM2073U, RRID:AB_131195), anti-CD3 (Beckman Coulter Cat# IM1282U, RRID:AB_10640418), anti-CD14 (Beckman Coulter Cat# IM0645U, RRID:AB_130992), anti-CD16 (Beckman Coulter Cat# IM0814U, RRID:AB_10640417) were from Beckman Coulter (FL). FACS analysis was performed on a LSRII cytometer (BD Biosciences, CA). Mø phenotype was confirmed by flow cytometry targeting CD68 (R and D Systems Cat# IC20401P, RRID:AB_2074835) and CD80 (R and D Systems Cat# FAB140F, RRID:AB_357027), CD163 (R and D Systems Cat# FAB1607P, RRID:AB_2074536) and CD206 (R and D Systems Cat# FAB25342P, RRID:AB_10889015) antibodies all from R&D Systems (IN). Data were analyzed with Flowing Software (University of Turku, Finland) or FACSDiVa software (BD Biosciences) and represented, when required, with the logical display.

Pandruvada S.N., Ebersole J.L, & Huja S.S. (2019). Inhibition of osteoclastogenesis by opsonized Porphyromonas gingivalis. FASEB bioAdvances, 1(4), 213-226.

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Characterization of TLR2/1 activated Macrophages

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Cells were harvested after 48 hours incubation at 37°Celsius in 7%CO₂. Surface expression of protein was determined using specific antibodies: CD209 (Becton Dickinson), CD40 (Becton Dickinson), CD1a (Becton Dickinson), CD163 (R&D systems), Jagged1 (R&D systems), CD14 (Becton Dickinson) and IgG controls (Becton Dickinson). Phosphorylated STAT-1 levels were determined using Anti-Human phospho-STAT1 (eBiosciences). Cytometric Bead Arrays (CBA) were used to characterize TLR2/1R activated CD14⁺MΦ supernatants. CBAs were performed on 50μL of supernatant that was harvested after 24 hours of incubation. Supernatants were tested for the presence of MIP1-β, IL-6 and TNF-α. CBA Flex kits were obtained from Becton Dickinson and performed according to manufacturer’s recommendations. Samples were acquired using FacsCalibur and FacsVerse flow cytometers and FCS files were analyzed using FlowJo software.

Kibbie J., Teles R.M., Wang Z., Hong P., Montoya D., Krutzik S., Lee S., Kwon O., Modlin R.L, & Cruz D. (2016). Jagged1 Instructs Macrophage Differentiation in Leprosy. PLoS Pathogens, 12(8), e1005808.

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Quantification of Der p1-CD163 Binding

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Comprehensive Antibody Assay Protocol

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Antibody pairs were purchased as follows: IgM (GENWAY, San Diego, CA), lectin galactoside-binding soluble 3 binding protein (eBioScience, San Diego, CA), gastric inhibitory polypeptide (Millipore, Billerica, MA), CD5 molecule-like (CircuLex, Nagano, Japan), latent transforming growth factor beta binding protein 2 and haptoglobin-related protein (USCN Life Science, Hubei, China), CD163 (R&D Systems, Minneapolis, MN), cartilage acidic protein 1 and PDZ and LIM domain 1 (My BioSource, San Diego, CA), trefoil factor 2 (BioVendor, Asheville, NC), thioredoxin (Immuno-Biological Laboratories, Gunma, Japan), and heat shock protein 90kDa beta (Grp94), member 1 (Abcam, Cambridge, MA). ELISA assays were performed according to manufacturer’s protocols.

Inamoto Y., Martin P.J., Paczesny S., Tabellini L., Momin A.A., Mumaw C.L., Flowers M.E., Lee S.J., Carpenter P.A., Storer B.E., Hanash S, & Hansen J.A. (2017). Association of plasma CD163 concentration with de novo-onset chronic graft-versus-host disease. Biology of blood and marrow transplantation : journal of the American Society for Blood and Marrow Transplantation, 23(8), 1250-1256.

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Exosome-induced Macrophage Polarization

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To generate non-polarized (M0) macrophages, 4x10⁵ THP-1 monocytes were differentiated with PMA for 24 hours, after which the PMA-containing medium was replaced with 10% FBS-containing 1X RPMI growth medium and the cells were allowed to recover for 24 hours.
M0 macrophages were then treated with equivalent amounts of exosomes, based on 30 ug of exosomal protein. After 72 hours, cell culture medium was removed and stored at -80°C for analysis of secreted chemokines and cytokines (see below), and cells were detached using Accutase (Innovative Cell Technologies). After pre-treatment with Fc Block (BD Biosciences), 1x10⁵ cells were incubated for 30 minutes at 4°C with fluorochrome-conjugated primary antibodies against the following proteins: CD14 (ThermoFisher Scientific), HLA-DR (BD Biosciences), CD163 (R&D Systems), CD80 (Bio-Techne), and CD206 (BD Biosciences). Cells were washed twice with FACS buffer (0.8% BSA in PBS), resuspended in 0.5% PFA and stored at 4°C protected from light before being acquired on a LSRFortessa flow cytometer (BD Biosciences). Positive controls for M1 macrophage polarization were 20 ng/mL LPS and 20 ng/mL IFNɣ and for M2 macrophage polarization were 20 ng/mL IL-4 and 20 ng/mL IL-13. M1 and M2 polarization controls were treated for 24 hours. Data from at least 3 independent experiments were analyzed using FlowJo software (TreeStar).

Linton S.S., Abraham T., Liao J., Clawson G.A., Butler P.J., Fox T., Kester M, & Matters G.L. (2018). Tumor-promoting effects of pancreatic cancer cell exosomes on THP-1-derived macrophages. PLoS ONE, 13(11), e0206759.

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Immune Markers in Sarcoma and Cancer

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Scavenger receptor CD163 expression is associated with tumor R&D Systems CD163 cysteine-rich cell proliferation and progression in sarcomas receptors (29) (link) through the activation of macrophages (30) (link). CD163 is associated with a poorer disease-free survival in patients with breast cancer (54) (link) The function of CD34 is not clear. However, R&D Systems CD34 (756510) CD34 is often used as a marker for hematopoietic stem cells and hematopoietic progenitor cells (62) (link).
GISTs are CD34 positive in about 50-100% of the patients and are associated with the tumor location in the gastrointestinal tract (63) (link).
CD42a (GP9) Leucine-rich CD42a is a part of the GPIb-IX-V complex, LS Bio CD42a repeat family (34) (link) which is expressed on the platelet surface, binds the von Willebrand factor, and aids in the adhesion of platelets to endothelial cells (34) (link). Platelets play a role in tumor growth and metastasis (36) (link).

Brinch C.M., Hogdall E., Heer P., Penninga L., Bæk R., Jorgensen M.M., Engelmann B.E., Rossen P.B., Mortensen H.J., Krarup-Hansen A, & Aggerholm-Pedersen N. (2022). The Prognostic Value of Plasma Small Extracellular Vesicles' Phenotype in Patients With Gastrointestinal Stromal Tumor. Anticancer research, 42(12).

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Quantification of Inflammatory Markers

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IL1b, CD163, PGE2 (R&D systems, Minneapolis, USA) and S100A8, S100A9 (E Biosciences) concentrations were measured using sandwich ELISA. IL6, IL10, CCL3/MIP1a and TNFa were analyzed using multiplex bead-based sandwich immunoassay kits (BioRad Laboratories Inc., Segrate, Italy) following the manufacturer's instructions.

Manferdini C., Paolella F., Gabusi E., Gambari L., Piacentini A., Filardo G., Fleury-Cappellesso S., Barbero A., Murphy M, & Lisignoli G. (2017). Adipose stromal cells mediated switching of the pro-inflammatory profile of M1-like macrophages is facilitated by PGE2: in vitro evaluation. Osteoarthritis and cartilage, 25(7).

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