R&D Systems recombinant cd36 fc
Recombinant Cd36 Fc, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/recombinant+cd36+fc/bio_rxiv__2024__02__21__581431-167-17-19?v=R%26D+Systems
Average 94 stars, based on 1 article reviews

recombinant cd36 fc - by Bioz Stars, 2026-07

94/100 stars

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cd36 (R&D Systems)

R&D Systems cd36

Inhibition of sRAGE, Gal‐3, <t>CD36</t> and SR‐AI by BLG and whey proteins measured in competition ELISA. BLG (A) and WP (B), non‐treated or heated in the absence of sugar (BLG‐H) or in the presence of lactose or glucose (BLG‐Glu, BLG‐Lac) were pre‐incubated with the recombinant forms of sRAGE, Gal‐3, CD36 and SR‐AI prior adding to the ELISA plate coated with glycated soy protein extract. The data are expressed as percentage of inhibition by the use of non‐inhibited signal as the maximum value. Positive control: highly glycated soy protein extract; Negative control: ovalbumin. Data shown as mean ± SD of triplicate wells and are representative of three independent experiments on three different batches of processed BLG. Significant differences analyzed with one‐way ANOVA with Tukey post hoc comparison test (GraphPad Prism); * p < 0.05; ** p < 0.01, *** p < 0.001.

Cd36, supplied by R&D Systems, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/recombinant+cd36+fc/pmc08244112-189-54-57?v=R%26D+Systems
Average 91 stars, based on 1 article reviews

cd36 - by Bioz Stars, 2026-07

91/100 stars

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recombinant human cd36 sr b3 fc chimera protein cf (R&D Systems)

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The Recombinant Human CD36 SR B3 Fc Chimera Protein from R D Systems is derived from Sf 21 baculovirus The Recombinant Human CD36 SR B3 Fc Chimera Protein has been validated for the following applications

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recombinant human platelet membrane glycoprotein iv/cd36/sr-b3 fc chimera protein (Elabscience Biotechnology)

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Platelet Glycoprotein 4 (CD36) is an integral membrane glycoprotein that has multiple physiological functions. It is broadly expressed on a variety of cell types including microvascular endothelium, adipocytes, skeletal muscle, epithelial cells of the retina,

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recombinant human cd36/platelet membrane glycoprotein iv/sr-b3 fc chimera protein (Beijing Solarbio Science)

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recombinant cynomolgus cd36, fc tagged (Creative BioMart)

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Recombinant Cynomolgus CD36 (Q6J512) (Gly30-Asn439), fused with the Fc region of human IgG1 at the C-terminus, was produced in Human Cells.http://www.creativebiomart.net/description_388178_12.htm

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recombinant mouse cd36, fc-his tagged (Creative BioMart)

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Recombinant Mouse Cd36 (NP_001153030.1) extracellular domain (Gly 30-Lys 439), fused with the polyhistidine-tagged Fc region of human IgG1 at the C-terminus, was produced in Human Cell.http://www.creativebiomart.net/description_9406_12.htm

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recombinant rat cd36, fc tagged (Creative BioMart)

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Recombinant Rat Cd36 (Gly30-Lys439), fused with the Fc region of human IgG1 at the C-terminus, was produced in Human Cell.http://www.creativebiomart.net/description_382886_12.htm

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cd36 recombinant protein c-fc tag lyophilized (Innovative Research Inc)

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CD36 Recombinant Protein C-Fc Tag Lyophilized from Innovative Research has been recombinantly produced in Human Cells. The protein formulation is lyophilized from a 0.2 ?m filtered solution of PBS, pH 7.4. with a purity of

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recombinant mouse cd36 sr b3 fc chimera protein cf (R&D Systems)

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The Recombinant Mouse CD36 SR B3 Fc Chimera Protein from R D Systems is derived from CHO The Recombinant Mouse CD36 SR B3 Fc Chimera Protein has been validated for the following applications Binding Activity

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Inhibition of sRAGE, Gal‐3, CD36 and SR‐AI by BLG and whey proteins measured in competition ELISA. BLG (A) and WP (B), non‐treated or heated in the absence of sugar (BLG‐H) or in the presence of lactose or glucose (BLG‐Glu, BLG‐Lac) were pre‐incubated with the recombinant forms of sRAGE, Gal‐3, CD36 and SR‐AI prior adding to the ELISA plate coated with glycated soy protein extract. The data are expressed as percentage of inhibition by the use of non‐inhibited signal as the maximum value. Positive control: highly glycated soy protein extract; Negative control: ovalbumin. Data shown as mean ± SD of triplicate wells and are representative of three independent experiments on three different batches of processed BLG. Significant differences analyzed with one‐way ANOVA with Tukey post hoc comparison test (GraphPad Prism); * p < 0.05; ** p < 0.01, *** p < 0.001.

Journal: Molecular Nutrition & Food Research

Article Title: Enhanced Uptake of Processed Bovine β‐Lactoglobulin by Antigen Presenting Cells: Identification of Receptors and Implications for Allergenicity

doi: 10.1002/mnfr.202000834

Figure Lengend Snippet: Inhibition of sRAGE, Gal‐3, CD36 and SR‐AI by BLG and whey proteins measured in competition ELISA. BLG (A) and WP (B), non‐treated or heated in the absence of sugar (BLG‐H) or in the presence of lactose or glucose (BLG‐Glu, BLG‐Lac) were pre‐incubated with the recombinant forms of sRAGE, Gal‐3, CD36 and SR‐AI prior adding to the ELISA plate coated with glycated soy protein extract. The data are expressed as percentage of inhibition by the use of non‐inhibited signal as the maximum value. Positive control: highly glycated soy protein extract; Negative control: ovalbumin. Data shown as mean ± SD of triplicate wells and are representative of three independent experiments on three different batches of processed BLG. Significant differences analyzed with one‐way ANOVA with Tukey post hoc comparison test (GraphPad Prism); * p < 0.05; ** p < 0.01, *** p < 0.001.

Article Snippet: Inhibition ELISA was conducted as a screening tool to determine the binding strength of the processed BLG to the following receptors: soluble RAGE (# RD172116100, BioVendor, Brno, Czech Republic), galectin‐3 (# 1154‐DC, R&D Systems, Minneapolis, United States) and two receptors from the scavenger receptor family: SR‐AI (# 1154‐DC, R&D Systems, Minneapolis, United States) and CD36 (# 1955‐CD, R&D Systems, Minneapolis, United States) according to the protocol described by Zenker et al. [ ] The detailed information about antibodies used in the assay are displayed in Table , Supporting Information.

Techniques: Inhibition, Enzyme-linked Immunosorbent Assay, Incubation, Recombinant, Positive Control, Negative Control, Comparison

Inhibition of binding and internalization of processed BLG by human THP‐1 macrophages. PMA differentiated THP‐1 macrophages were pre‐incubated with endocytosis inhibitors: dynasore and cytochalasin D (Cyt D) or inhibitors of specific receptors: amyloid‐β and FPS‐ZM1 for RAGE; Oxidized low‐density lipoprotein (Ox‐LDL) for CD36; fucoidan for SR‐AI, short peptides 33‐DFTG and G3‐C12 for Gal‐3. Followed by pre‐incubation with inhibitor the cells were incubated in a presence or absence of BLG: non‐treated (BLG‐NT), heated (BLG‐H), heated with lactose (BLG‐Lac) or heated with glucose (BLG‐Glu) and stained extracellularly (A) or intracellularly (B) with Alexa Fluor 647 conjugated anti‐BLG antibodies. The level of fluorescence was measured by flow cytometry and expressed as a relative to non‐inhibited THP‐1 cells. Data shown as mean ± SD of triplicate wells and are representative of three independent experiments. Significant differences analyzed with one‐way ANOVA with Tukey post hoc comparison test (GraphPad Prism); * p < 0.05; ** p < 0.01, *** p < 0.001.

Journal: Molecular Nutrition & Food Research

Article Title: Enhanced Uptake of Processed Bovine β‐Lactoglobulin by Antigen Presenting Cells: Identification of Receptors and Implications for Allergenicity

doi: 10.1002/mnfr.202000834

Figure Lengend Snippet: Inhibition of binding and internalization of processed BLG by human THP‐1 macrophages. PMA differentiated THP‐1 macrophages were pre‐incubated with endocytosis inhibitors: dynasore and cytochalasin D (Cyt D) or inhibitors of specific receptors: amyloid‐β and FPS‐ZM1 for RAGE; Oxidized low‐density lipoprotein (Ox‐LDL) for CD36; fucoidan for SR‐AI, short peptides 33‐DFTG and G3‐C12 for Gal‐3. Followed by pre‐incubation with inhibitor the cells were incubated in a presence or absence of BLG: non‐treated (BLG‐NT), heated (BLG‐H), heated with lactose (BLG‐Lac) or heated with glucose (BLG‐Glu) and stained extracellularly (A) or intracellularly (B) with Alexa Fluor 647 conjugated anti‐BLG antibodies. The level of fluorescence was measured by flow cytometry and expressed as a relative to non‐inhibited THP‐1 cells. Data shown as mean ± SD of triplicate wells and are representative of three independent experiments. Significant differences analyzed with one‐way ANOVA with Tukey post hoc comparison test (GraphPad Prism); * p < 0.05; ** p < 0.01, *** p < 0.001.

Techniques: Inhibition, Binding Assay, Incubation, Staining, Fluorescence, Flow Cytometry, Comparison

Immunoreactivity of heated and glycated BLG after enzymatic digestion in infant gastrointestinal static in vitro model. BLG: Non‐treated, heated (BLG‐H), heated with lactose (BLG‐Lac) or heated with glucose (BLG‐Glu) were subjected to gastric and intestinal phase of enzymatic digestion and immunogenicity of digested samples was measured as (A) binding to sRAGE, Gal‐3, CD36 and SR‐AI in inhibition ELISAs; following positive controls were used: amyloid‐β for sRAGE and CD36, fucoidan for SRAI and soy protein extract glycated with glucose for Gal‐3. B) binding assay to THP‐1 macrophages using Alexa Fluor 647 conjugated anti‐BLG antibodies for flow cytometry detection. Digestion blank (dBlank) – sample containing all digestive enzymes but no BLG. Data shown as mean ± SD of triplicate wells and are representative of at three (A) or two (B) independent experiments. Significant differences analyzed with one‐way ANOVA with Tukey post hoc comparison test (GraphPad Prism); * p < 0.05; ** p < 0.01, *** p < 0.001.

Journal: Molecular Nutrition & Food Research

Article Title: Enhanced Uptake of Processed Bovine β‐Lactoglobulin by Antigen Presenting Cells: Identification of Receptors and Implications for Allergenicity

doi: 10.1002/mnfr.202000834

Figure Lengend Snippet: Immunoreactivity of heated and glycated BLG after enzymatic digestion in infant gastrointestinal static in vitro model. BLG: Non‐treated, heated (BLG‐H), heated with lactose (BLG‐Lac) or heated with glucose (BLG‐Glu) were subjected to gastric and intestinal phase of enzymatic digestion and immunogenicity of digested samples was measured as (A) binding to sRAGE, Gal‐3, CD36 and SR‐AI in inhibition ELISAs; following positive controls were used: amyloid‐β for sRAGE and CD36, fucoidan for SRAI and soy protein extract glycated with glucose for Gal‐3. B) binding assay to THP‐1 macrophages using Alexa Fluor 647 conjugated anti‐BLG antibodies for flow cytometry detection. Digestion blank (dBlank) – sample containing all digestive enzymes but no BLG. Data shown as mean ± SD of triplicate wells and are representative of at three (A) or two (B) independent experiments. Significant differences analyzed with one‐way ANOVA with Tukey post hoc comparison test (GraphPad Prism); * p < 0.05; ** p < 0.01, *** p < 0.001.

Techniques: In Vitro, Immunopeptidomics, Binding Assay, Inhibition, Flow Cytometry, Comparison

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