Journal: bioRxiv

Article Title: Identification of Human Transferrin Receptor as an Entry Co-receptor for Parvovirus B19 Infection of Human Erythroid Progenitor Cells

doi: 10.64898/2026.04.02.715920

Figure Lengend Snippet: (A) Protein diagram. VP1u-APEX2 consists of APEX2 fused to the C-terminus of the unique region of B19V VP1 (VP1u) via a seven-residue glycine-serine linker (GGSGGSG), followed by a Flag tag and a 6 × Histidine (His) tag. APEX2 has a linker-Flag-His tag fused at the C-terminus. (B) Analysis of purified proteins. VP1u-APEX2 and APEX2 proteins were expressed in bacteria and purified. Approximately (∼) 1 µg of each protein was separated by SDS-PAGE, followed by Coomassie blue staining. M, molecular weight marker. (C) Confocal microscopy of VP1u-APEX2 entry. 1 × 10 6 UT7/Epo-S1 cells were incubated with 2 μM VP1u-APEX2 or APEX2 protein at 37°C for 2 h. The cells were then immunostained with α-Flag to visualize internalized proteins under a Leica STED confocal microscope. Scale bar = 10 μm. Nuclei were stained with DAPI (4’,6-diamidino-2-phenylindole). (D) Western blotting of APEX2-biotinylated proteins. 1 × 10 7 UT7/Epo-S1 cells were incubated with 2 μM VP1u-APEX2 or APEX2 protein at 37°C. After 2 h, APEX2-mediated biotinylation was then performed as described in the Materials and Methods and Figure S1 . Biotinylated host proteins were purified with streptavidin-conjugated magnetic beads. The supernatant was collected as the flow-through (FT), and the beads were further washed several times and eluted as the pull-down (PD). Both FT and PD samples were analyzed by SDS-PAGE and immunoblotting using Alexa Fluor 680-conjugated streptavidin. (E) Analysis of VP1u-APEX2-biotinylated/associated proteins using quantitative mass spectrometry (qMS). Three independent PD samples prepared from VP1u-APEX2 and APEX2 (control) treated cells were analyzed by on-bead digestion and qMS. MS data were processed and analyzed as described in the Materials and Methods. The bubble plot shows protein enrichment (log 2 fold change) in the VP1u-APEX2 group relative to the APEX control, with color indicating subcellular localization based on Gene Ontology (GO) annotation. TFRC denotes human transferrin receptor 1 (hTfR).

Article Snippet: Purified proteins: Recombinant hTfR ECD protein tagged with a His-tag at the C-terminus (#11020-H07H) and recombinant human ferritin heavy chain 1/FTH1 (#13217-HNAE) were purchased from SinoBiological (Paoli, PA).

Techniques: Residue, FLAG-tag, Purification, Bacteria, SDS Page, Staining, Molecular Weight, Marker, Confocal Microscopy, Incubation, Microscopy, Western Blot, Magnetic Beads, Mass Spectrometry, Control, Protein Enrichment

Journal:

Article Title: Survival of Aspergillus fumigatus in Serum Involves Removal of Iron from Transferrin: the Role of Siderophores

doi: 10.1128/IAI.72.3.1402-1408.2004

Figure Lengend Snippet: Degradation of transferrin by A. fumigatus in liquid cultures. A. fumigatus was incubated in MEM containing 10% human serum (A) or 2.5 μM holotransferrin (B). Supernatants were withdrawn from the cultures after the number of hours indicated above the lanes, and the presence of transferrin was determined by Western blotting following sodium dodecyl sulfate-PAGE. Controls (lanes C) were uninoculated samples incubated for 286 h. The band underneath transferrin in panel A is another protein that cross-reacted with the polyclonal antitransferrin antibody.

Article Snippet: Gels were silver stained or transferred to polyvinylidene difluoride membranes (Bio-Rad), blocked with 5% bovine serum albumin, probed with a rabbit immunoglobulin G fraction of anti-human transferrin (1:1,000 dilution; Rockland Inc., Gilbertsville, Pa.), and treated with goat anti-rabbit horseradish peroxidase.

Techniques: Incubation, Western Blot

Journal:

Article Title: Survival of Aspergillus fumigatus in Serum Involves Removal of Iron from Transferrin: the Role of Siderophores

doi: 10.1128/IAI.72.3.1402-1408.2004

Figure Lengend Snippet: Iron removal from transferrin by A. fumigatus. A. fumigatus was cultured in MEM containing 2.5 μM purified human holotransferrin (A) or 10% human serum (B). Culture media were withdrawn, and the iron saturation of transferrin was analyzed by urea-PAGE. Transferrin was visualized by Western blotting. The numbers above the lanes represent the hours of incubation with A. fumigatus. Fe2-Tf, holotransferrin; Apo-Tf, apotransferrin.

Article Snippet: Gels were silver stained or transferred to polyvinylidene difluoride membranes (Bio-Rad), blocked with 5% bovine serum albumin, probed with a rabbit immunoglobulin G fraction of anti-human transferrin (1:1,000 dilution; Rockland Inc., Gilbertsville, Pa.), and treated with goat anti-rabbit horseradish peroxidase.

Techniques: Cell Culture, Purification, Western Blot, Incubation

Journal:

Article Title: Survival of Aspergillus fumigatus in Serum Involves Removal of Iron from Transferrin: the Role of Siderophores

doi: 10.1128/IAI.72.3.1402-1408.2004

Figure Lengend Snippet: A. fumigatus can transport iron from transferrin across a dialysis membrane. A. fumigatus was inoculated into MEM in which a dialysis bag containing holotransferrin (25 μM) was suspended. A. fumigatus was incubated for 48 h, and then transferrin was withdrawn from the dialysis bag and analyzed by urea-PAGE (lane +). An uninoculated control flask containing MEM plus transferrin in a dialysis bag also was examined (lane −). Pure holotransferrin (Fe2-Tf) and apotransferrin (Apo-Tf) standards also were run.

Article Snippet: Gels were silver stained or transferred to polyvinylidene difluoride membranes (Bio-Rad), blocked with 5% bovine serum albumin, probed with a rabbit immunoglobulin G fraction of anti-human transferrin (1:1,000 dilution; Rockland Inc., Gilbertsville, Pa.), and treated with goat anti-rabbit horseradish peroxidase.

Techniques: Incubation

Journal:

Article Title: Survival of Aspergillus fumigatus in Serum Involves Removal of Iron from Transferrin: the Role of Siderophores

doi: 10.1128/IAI.72.3.1402-1408.2004

Figure Lengend Snippet: Iron saturation of transferrin following incubation with A. fumigatus siderophores. Purified desferrisiderophores were incubated with holotransferrin (25 μM) at 37°C for 16 h. Desferriferrichrome, desferriferricrocin, and desferritriacetylfusarinine C were serially diluted to final concentrations of 5 μM (lanes 1), 50 μM (lanes 2), 500 μM (lanes 3), and 5 mM (lanes 4). Controls containing holotransferrin alone also were run (lanes 0). holo-Tf, holotransferrin; Fe-Tf, monoferric transferrin; apo-Tf, apotransferrin.

Article Snippet: Gels were silver stained or transferred to polyvinylidene difluoride membranes (Bio-Rad), blocked with 5% bovine serum albumin, probed with a rabbit immunoglobulin G fraction of anti-human transferrin (1:1,000 dilution; Rockland Inc., Gilbertsville, Pa.), and treated with goat anti-rabbit horseradish peroxidase.

Techniques: Incubation, Purification

Journal: bioRxiv

Article Title: Dual Ligand Cooperation at the Plasma Membrane Drives Transport of Engineered Small Extracellular Vesicles Across Brain Endothelial Cells

doi: 10.64898/2026.01.21.700773

Figure Lengend Snippet: Preparation and characterization of engineered sEVs. (a) Scheme describing the strategy for engineering the surface of sEVs. (b.1) Quantification of available thiol groups on the surface of sEVs before and after conjugation with acrylated HA (HA-A). (b.2) HA-A immobilization on sEVs. The number of immobilized polymers was calculated based on the calibration of the fluorescently labelled polymer, normalized per number of sEVs. In b.1 and b.2, results are expressed as mean ± SEM (n=4 independent sEVs batches and a separate bioconjugation reaction) (b.3) Size distribution profile of sEVs and sEVs-HA evaluated by NTA, expressed in particle counts (percentage) as a function of particle size diameter (nm). Results are mean ± SEM (10 independent experiments). The standard error of the mean is represented in the colour filling. (c.1) Number of Transferrin molecules immobilized on the surface of sEVs at different protein:EV ratios. The number of immobilized proteins was calculated based on the fluorescently labelled protein, as described in the Methods section. The contribution of unspecific binding was evaluated using native sEVs, i.e. before conjugation with HA-A. Results are expressed as mean ± SEM (4-6 independent experiments). (c.2) Size distribution profile of transferrin sEVs conjugates, evaluated by NTA. Results are mean ± SEM (6 independent experiments regarding the highest ligand density tested). (c.3) TEM images of immunogold labelling of Transferrin molecules immobilized on the surface of EVs (15-nm gold particles). Scale bar = 100 nm. (d.1) Number of LDL molecules immobilized on the surface of sEVs at different protein:sEV ratios. Results are expressed as mean ± SEM (3-4 independent experiments) (d.2) Size distribution profile of sEV-HA-LDL, evaluated by NTA. Results are mean ± SEM (6 independent experiments regarding the highest ligand density tested). (e.1) Number of CD98hc antibodies immobilized on the surface of sEVs at different antibody:sEV ratios. Results are expressed as mean±SEM (3 independent experiments) (e.2) Size distribution profile of sEV-HA-CD98. Results are mean±SEM (5 independent experiments regarding the highest ligand density tested). (f) Zeta potential measurements of the sEVs conjugates. Results are mean ± SEM plotted for 3-5 independent experiments. An independent experiment is defined as a separate bioconjugation reaction performed using sEVs obtained from 1-2 isolations derived from pooled plasma of 2-4 individual donors. Statistical analyses were performed by One-way ANOVA followed by Tukey’s multiple comparisons test (p<0.05). In b.1 and e.1 * and ** denote statistical significance (p<0.05 and p<0.01).

Article Snippet: The membranes were then washed with TBS-T and left to incubate overnight at 4°C with the primary antibodies, diluted in 1% BSA/TBS-T: CD63 1:250 (BD Pharmingen, 556019), ApoA-1 1:1,000 (Affinity Biosciences, BF0578), GAPDH (G9 clone) 1:250 (Santa Cruz, sc-365062), Calnexin 1:1,000 (Santa Cruz, sc-23954), Alix 1:500 (Santa Cruz, sc-53540), CD9 1:250 (BD Biosciences 555370), CD81 1:250 (BD Biosciences, 555675), Hsp70 1:1,000 (BD Biosciences 554243) and Transferrin 1:1,000 (Santa Cruz, sc-52256).

Techniques: Conjugation Assay, Polymer, Binding Assay, Zeta Potential Analyzer, Derivative Assay, Clinical Proteomics

Journal: bioRxiv

Article Title: Dual Ligand Cooperation at the Plasma Membrane Drives Transport of Engineered Small Extracellular Vesicles Across Brain Endothelial Cells

doi: 10.64898/2026.01.21.700773

Figure Lengend Snippet: sEVs conjugated with ligands are internalized more efficiently by human BECs than native sEVs. (a) Scheme outlining the workflow of the internalization assay. (b) Internalization of sEVs-HA, following a 24 h kinetics. Fluorescence intensity per cell was normalized to the fluorescence of sEVs-HA at 24 h time-point. Results are expressed as mean ± SEM (n=7 independent experiments; for detailed data analysis refer to the Methods section). An independent experiment is defined as a separate bioconjugation reaction performed using sEVs obtained from 1-2 isolations derived from pooled plasma of 2-4 individual donors. Statistical analysis was performed by Two-way ANOVA followed by Bonferroni’s multiple comparisons test. **, *** and **** denote statistical significance between sEVs and sEVs-HA (p<0.01, p<0.001, p<0.0001). (c.1) Internalization kinetics of sEVs-HA engineered with low, medium and high densities of transferrin. (c.2) Internalization of sEVs-HA-Tf, after 24 h incubation. The observed increase in fluorescence signal corresponded to a higher number of internalized sEV clusters per cell (sEVs: 2, sEVs-HA: 4, sEVs-HA-Tf: 5.4 clusters/cell). Images were acquired in a high content fluorescence microscope. Scale bar: 40 μm. (d-e) Internalization kinetics of sEVs-HA engineered with low, medium and high densities of LDL (d) and CD98 antibody (e). These results were obtained without the need for apo-Transferrin pre-loading, as the concentration of Fe (III) in the culture medium was sufficient to ensure effective saturation of Transferrin with its ligand under the experimental conditions. In c.1, d and e, results are expressed as mean ± SEM (n=3-6 independent experiments). Statistical analysis was performed by Two-way ANOVA followed by Tukey’s multiple comparisons test. # and ## denote statistical significance between sEVs-HA and sEVs-HA-Tf (high) (p<0.05, p<0.01). *** and **** denote statistical significance between sEVs and sEVs-HA-Tf (high) (p<0.001, p<0.0001).

Article Snippet: The membranes were then washed with TBS-T and left to incubate overnight at 4°C with the primary antibodies, diluted in 1% BSA/TBS-T: CD63 1:250 (BD Pharmingen, 556019), ApoA-1 1:1,000 (Affinity Biosciences, BF0578), GAPDH (G9 clone) 1:250 (Santa Cruz, sc-365062), Calnexin 1:1,000 (Santa Cruz, sc-23954), Alix 1:500 (Santa Cruz, sc-53540), CD9 1:250 (BD Biosciences 555370), CD81 1:250 (BD Biosciences, 555675), Hsp70 1:1,000 (BD Biosciences 554243) and Transferrin 1:1,000 (Santa Cruz, sc-52256).

Techniques: Fluorescence, Derivative Assay, Clinical Proteomics, Incubation, Microscopy, Concentration Assay

Journal: bioRxiv

Article Title: Dual Ligand Cooperation at the Plasma Membrane Drives Transport of Engineered Small Extracellular Vesicles Across Brain Endothelial Cells

doi: 10.64898/2026.01.21.700773

Figure Lengend Snippet: sEVs conjugated with HA-Tf interact with CD44 and Tf receptors. (a.1) Real-time kinetic analysis using SPR for sequential binding of sEVs and sEVs-HA-Tf to the CD44 receptor and (a.2) Transferrin receptor, immobilized on a SPR sensor surface. RU, resonance units. (b.1) Scheme outlining the workflow of the internalization blocking assay. (b.2) Internalization of sEVs-HA, after antibody blocking of the CD44 receptors. Results are expressed as mean±SEM (n=3 independent experiments). (b.3) Internalization of sEVs-HA-Tf, after antibody blocking of the TfR, or CD44 and TfR, simultaneously. Fluorescence intensity per cell was normalized to the fluorescence of the condition sEVs-HA-Tf (control condition, without blocking the receptors). Results are expressed as mean ± SEM (n=6-9 independent experiments). An independent experiment is defined as a separate bioconjugation reaction performed using sEVs obtained from 1-2 isolations derived from pooled plasma of 2-4 individual donors. Statistical analyses in b.2 and b.3 was performed by One-way ANOVA followed by Tukey’s multiple comparisons test. *** denotes statistical significance (p<0.001) between the control condition and the CD44 blocking condition (b.2) or the dual blocking condition (b.3). (b.4) sEVs internalization following 24 h receptor blocking. Images were taken in a high content fluorescence microscope (INCell Analyzer, GE Healthcare). Scale bar: 40 μm.

Article Snippet: The membranes were then washed with TBS-T and left to incubate overnight at 4°C with the primary antibodies, diluted in 1% BSA/TBS-T: CD63 1:250 (BD Pharmingen, 556019), ApoA-1 1:1,000 (Affinity Biosciences, BF0578), GAPDH (G9 clone) 1:250 (Santa Cruz, sc-365062), Calnexin 1:1,000 (Santa Cruz, sc-23954), Alix 1:500 (Santa Cruz, sc-53540), CD9 1:250 (BD Biosciences 555370), CD81 1:250 (BD Biosciences, 555675), Hsp70 1:1,000 (BD Biosciences 554243) and Transferrin 1:1,000 (Santa Cruz, sc-52256).

Techniques: Binding Assay, Blocking Assay, Fluorescence, Control, Derivative Assay, Clinical Proteomics, Microscopy

Journal: bioRxiv

Article Title: Dual Ligand Cooperation at the Plasma Membrane Drives Transport of Engineered Small Extracellular Vesicles Across Brain Endothelial Cells

doi: 10.64898/2026.01.21.700773

Figure Lengend Snippet: sEVs-HA-Tf accumulate at the basolateral membrane of BECs. (a) Scheme illustrating the trancystosis steps of sEVs or sEVs-HA-Tf in BECs. (b.1) Expression of syntaxin-4 in human BECs along the z-axis. xy-slice at the level of the basolateral (z-stack:2/32) and apical (z-stack:17/32) membranes. Scale bar: 40 µm. (b.2) Number of Syntaxin-4 foci along the z-axis. (c.1) Representative image of Transferrin-594 conjugate, acquired at the bottom most plane of the glass slide, on STED mode using a single point scanning confocal Stellaris 8 (Leica) microscope. (c.2) Representative images of EVs, EVs-HA and EVs-HA-Tf, acquired with similar settings. Scale bar: 1 µm. (c.3) Measured area (μm2) of the encircled organelle structures depicted in c.1 and c.2. Results are expressed as mean±SEM (3 fields analyzed per experimental condition across 105-135 cells in a single experiment). (d.1) Overview of Transferrin and HSA co-localization with syntaxin-4 at the basolateral membrane. Arrowheads point to two-channel overlapping pixels. Scale bar: 20 µm. (d.2) Co-localization of transferrin and HSA with the t-SNARE protein syntaxin-4. Results are expressed as mean±SEM (5 fields analyzed per experimental condition across 175-225 cells in a single experiment). Results are given by the Mander’s co-localization coefficient M1, normalized to the control. Statistical analysis was performed by a Mann–Whitney test (**: p ≤ 0.01). In b.1, b.2, d.1 and d.2, images were acquired in a LSM710 confocal microscope (Zeiss). (e.1) Representative images of sEVs, sEVs-HA, and sEVs-HA-Tf interaction with Syntaxin-4, acquired on STED mode at the plane closest to the glass slide (corresponding to the basolateral side of the cell). Scale bar: 5 µm. Inset: Higher magnification images of EVs in contact with Syntaxin-4. Scale bar: 1 µm. (e.2) Co-localization of sEVs with syntaxin-4, given by the number of sEVs carrying organelles that colocalize with Syntaxin-4. Colocalization is defined as all Syntaxin-4 objects distancing ≤200 nm from sEVs carrying organelles. Results were normalized to the control. (f.) Number of basolateral sEVs carryring organelles, normalized to the control. Results in e.2 and f. are expressed as mean±SEM (11-13 fields analyzed per experimental condition across 25-50 cells in 2 independent experiments). An independent experiment is defined as a separate bioconjugation reaction performed using sEVs obtained from 2-3 isolations derived from pooled plasma of 4-6 individual donors. Statistical analyses were performed by One-way ANOVA, followed by Tukey’s multiple comparisons test (p<0.05).

Article Snippet: The membranes were then washed with TBS-T and left to incubate overnight at 4°C with the primary antibodies, diluted in 1% BSA/TBS-T: CD63 1:250 (BD Pharmingen, 556019), ApoA-1 1:1,000 (Affinity Biosciences, BF0578), GAPDH (G9 clone) 1:250 (Santa Cruz, sc-365062), Calnexin 1:1,000 (Santa Cruz, sc-23954), Alix 1:500 (Santa Cruz, sc-53540), CD9 1:250 (BD Biosciences 555370), CD81 1:250 (BD Biosciences, 555675), Hsp70 1:1,000 (BD Biosciences 554243) and Transferrin 1:1,000 (Santa Cruz, sc-52256).

Techniques: Membrane, Expressing, Microscopy, Control, MANN-WHITNEY, Derivative Assay, Clinical Proteomics

Journal:

Article Title: Phospholipase D2 Is Localized to the Rims of the Golgi Apparatus in Mammalian Cells

doi: 10.1091/mbc.02-04-0059

Figure Lengend Snippet: PLD2 localization with different organelles in rat NRK cells. Cells were prepared for immunofluorescence microscopy and incubated with rabbit PLD2 antibody PLD2-27 (A, D, G, and J) and costained with monoclonal antibodies to the ER marker BiP (B); the transferrin receptor (E), a marker of early endosomes and the plasma membrane; and lgp120 (H), a late endosome/lysosomal marker. (K) Cells were stained with caveolin-1, a marker for caveoli; the arrow corresponds to caveolin-1 localized to the plasma membrane. Images were merged to determine overlap between PLD2 (red) and the respective marker proteins (green; C, F, I, and L). Areas of maximal overlap are yellow. (L) Inset, enlargement of the region of overlap between PLD2 and caveolin-1 in the perinuclear Golgi apparatus. The arrow indicates areas where PLD2 puncta (red) either overlap completely with caveolin-1 (green) or are directly adjacent. Images are from projected Z-series. Bars, 10 μm.

Article Snippet: Purified monoclonal anti-rat transferrin receptor antibodies were purchased from Cedarlane Laboratories (Hornby, Ontario, Canada).

Techniques: Immunofluorescence, Microscopy, Incubation, Marker, Staining

Journal: Nutrients

Article Title: Construction and Evaluation of a Novel MAP Immunoassay for 9 Nutrition-and-Health-Related Protein Markers Based on Multiplex Liquid Protein Chip Technique

doi: 10.3390/nu15061522

Figure Lengend Snippet: Reagents used in this research.

Article Snippet: , sTfR detection antiboty , NB100-73092B , Novus Biologicals, Inc. (Centennial, CO, USA).

Techniques: Comparison, Enzyme-linked Immunosorbent Assay, Diagnostic Assay

Journal: Nutrients

Article Title: Construction and Evaluation of a Novel MAP Immunoassay for 9 Nutrition-and-Health-Related Protein Markers Based on Multiplex Liquid Protein Chip Technique

doi: 10.3390/nu15061522

Figure Lengend Snippet: The cross-reaction rates of 9 protein markers with each detection antibody (%).

Article Snippet: , sTfR detection antiboty , NB100-73092B , Novus Biologicals, Inc. (Centennial, CO, USA).

Techniques:

Journal: Nutrients

Article Title: Construction and Evaluation of a Novel MAP Immunoassay for 9 Nutrition-and-Health-Related Protein Markers Based on Multiplex Liquid Protein Chip Technique

doi: 10.3390/nu15061522

Figure Lengend Snippet: The cross-reaction rates of 9 protein markers with each capture antibody (%).

Article Snippet: , sTfR detection antiboty , NB100-73092B , Novus Biologicals, Inc. (Centennial, CO, USA).

Techniques:

Journal: Nutrients

Article Title: Construction and Evaluation of a Novel MAP Immunoassay for 9 Nutrition-and-Health-Related Protein Markers Based on Multiplex Liquid Protein Chip Technique

doi: 10.3390/nu15061522

Figure Lengend Snippet: The LLDs and BDLs of liquid protein chip for 9 protein markers (pg/mL).

Article Snippet: , sTfR detection antiboty , NB100-73092B , Novus Biologicals, Inc. (Centennial, CO, USA).

Techniques:

Journal: Nutrients

Article Title: Construction and Evaluation of a Novel MAP Immunoassay for 9 Nutrition-and-Health-Related Protein Markers Based on Multiplex Liquid Protein Chip Technique

doi: 10.3390/nu15061522

Figure Lengend Snippet: The S -curves of 9 protein markers in the same one detection by using liquid protein chip. ( A ): SF S -curve; ( B ): sTfR S -curve; ( C ): CRP S -curve; ( D ): RBP4 S -curve; ( E ): ApoB S -curve; ( F ): AFP S -curve; ( G ): PA S -curve; ( H ): CEA S -curve; ( I ): D-D S -curve.

Article Snippet: , sTfR detection antiboty , NB100-73092B , Novus Biologicals, Inc. (Centennial, CO, USA).

Techniques:

Journal: Nutrients

Article Title: Construction and Evaluation of a Novel MAP Immunoassay for 9 Nutrition-and-Health-Related Protein Markers Based on Multiplex Liquid Protein Chip Technique

doi: 10.3390/nu15061522

Figure Lengend Snippet: The regression equations and determination coefficients of 9 protein markers detected by the liquid protein chip.

Article Snippet: , sTfR detection antiboty , NB100-73092B , Novus Biologicals, Inc. (Centennial, CO, USA).

Techniques: Marker

Journal: Nutrients

Article Title: Construction and Evaluation of a Novel MAP Immunoassay for 9 Nutrition-and-Health-Related Protein Markers Based on Multiplex Liquid Protein Chip Technique

doi: 10.3390/nu15061522

Figure Lengend Snippet: The recovery rates of 9 protein markers detected by liquid protein chip simultaneously ( n = 3).

Article Snippet: , sTfR detection antiboty , NB100-73092B , Novus Biologicals, Inc. (Centennial, CO, USA).

Techniques:

Journal: Nutrients

Article Title: Construction and Evaluation of a Novel MAP Immunoassay for 9 Nutrition-and-Health-Related Protein Markers Based on Multiplex Liquid Protein Chip Technique

doi: 10.3390/nu15061522

Figure Lengend Snippet: The within-run precisions of 9 protein markers by liquid protein chip ( n = 10).

Article Snippet: , sTfR detection antiboty , NB100-73092B , Novus Biologicals, Inc. (Centennial, CO, USA).

Techniques: Chromatin Immunoprecipitation

Journal: Nutrients

Article Title: Construction and Evaluation of a Novel MAP Immunoassay for 9 Nutrition-and-Health-Related Protein Markers Based on Multiplex Liquid Protein Chip Technique

doi: 10.3390/nu15061522

Figure Lengend Snippet: The between-run precisions of 9 protein markers by liquid protein chip ( D = 6, n = 3).

Article Snippet: , sTfR detection antiboty , NB100-73092B , Novus Biologicals, Inc. (Centennial, CO, USA).

Techniques: Chromatin Immunoprecipitation

Journal: Nutrients

Article Title: Construction and Evaluation of a Novel MAP Immunoassay for 9 Nutrition-and-Health-Related Protein Markers Based on Multiplex Liquid Protein Chip Technique

doi: 10.3390/nu15061522

Figure Lengend Snippet: Correlation analysis between liquid protein chip method and other methods for detecting the 9 protein markers of the same 16 serum samples. ( A ): The correlation analysis of SF; ( B ): The correlation analysis of sTfR; ( C ): The correlation analysis of CRP; ( D ): The correlation analysis of RBP4; ( E ): The correlation analysis of ApoB; ( F ): The correlation analysis of AFP; ( G ): The correlation analysis of PA; ( H ): The correlation analysis of CEA; ( I ): The correlation analysis of D-D.

Article Snippet: , sTfR detection antiboty , NB100-73092B , Novus Biologicals, Inc. (Centennial, CO, USA).

Techniques:

Journal: Nutrients

Article Title: Construction and Evaluation of a Novel MAP Immunoassay for 9 Nutrition-and-Health-Related Protein Markers Based on Multiplex Liquid Protein Chip Technique

doi: 10.3390/nu15061522

Figure Lengend Snippet: The correlation analysis between the liquid protein chip method and other methods for the detection of 9 protein markers in the same 16 serums ( n = 16).

Article Snippet: , sTfR detection antiboty , NB100-73092B , Novus Biologicals, Inc. (Centennial, CO, USA).

Techniques: Enzyme-linked Immunosorbent Assay

Journal: Nutrients

Article Title: Construction and Evaluation of a Novel MAP Immunoassay for 9 Nutrition-and-Health-Related Protein Markers Based on Multiplex Liquid Protein Chip Technique

doi: 10.3390/nu15061522

Figure Lengend Snippet: The paired comparison between liquid protein chip method and other methods for the detection of 9 protein markers of serums ( n = 16).

Article Snippet: , sTfR detection antiboty , NB100-73092B , Novus Biologicals, Inc. (Centennial, CO, USA).

Techniques: Comparison, Enzyme-linked Immunosorbent Assay

Journal: Nutrients

Article Title: Construction and Evaluation of a Novel MAP Immunoassay for 9 Nutrition-and-Health-Related Protein Markers Based on Multiplex Liquid Protein Chip Technique

doi: 10.3390/nu15061522

Figure Lengend Snippet: The analytical specificities of different interferences for the liquid protein chip in detecting 9 protein markers (%).

Article Snippet: , sTfR detection antiboty , NB100-73092B , Novus Biologicals, Inc. (Centennial, CO, USA).

Techniques:

Journal: Nutrients

Article Title: Construction and Evaluation of a Novel MAP Immunoassay for 9 Nutrition-and-Health-Related Protein Markers Based on Multiplex Liquid Protein Chip Technique

doi: 10.3390/nu15061522

Figure Lengend Snippet: The comparison of the LLDs of 9 protein markers between liquid protein chip and other methods.

Article Snippet: , sTfR detection antiboty , NB100-73092B , Novus Biologicals, Inc. (Centennial, CO, USA).

Techniques: Comparison, Enzyme-linked Immunosorbent Assay