anti sars cov 2 n protein monoclonal antibodies  (Sino Biological)

Journal: Cancers

Article Title: Optimizing Sequential Targeted Therapies in Advanced Renal Cell Carcinoma Using Patient-Derived Orthotopic Xenograft Mouse Avatars

doi: 10.3390/cancers18101615

Figure Lengend Snippet: Histopathological comparison of tumor architecture and proliferation between patient renal cell carcinoma (RCC) specimens and corresponding patient-derived xenograft models. Formalin-fixed, paraffin-embedded sections from primary patient tumors (KiCa-Pt58 and KiCa-Pt118), matched subcutaneous xenografts, and intra-renal patient-derived orthotopic xenograft (PDOX) tumors were analyzed to assess preservation of tumor histology and proliferative characteristics. ( A , C ) Representative images of KiCa-Pt58 ( A ) and KiCa-Pt118 ( C ) tissues stained with hematoxylin and eosin (H&E) for tissue architecture or were subjected to immunohistochemistry (IHC) for human CD44 (tumor cell marker) and human Ki67 (proliferation marker). Brown staining indicates positive immunoreactivity. Images were captured at 100× original magnification using an Axiovert 200M deconvolution microscope and SlideBook 6.0 software (Intelligent Imaging Innovations, Denver, CO, USA). ( B , D ) Quantitative analysis of Ki67-positive area (%) in KiCa-Pt58 ( B ) and KiCa-Pt118 ( D ) tissues. Positive (brown) staining areas were quantified digitally using Adobe Photoshop 7.0, with the percentage of immunoreactive area calculated per field. Data are presented as mean ± SEM (multiple fields per sample). Comparisons among patient biopsy specimens, subcutaneous xenografts, and orthotopic PDOX tumors were performed using unpaired Student’s t -test. No significant differences were observed (ns, p > 0.05), demonstrating faithful recapitulation of the parental tumor proliferative index across model passages. Abbreviations: RCC, renal cell carcinoma; PDOX, patient-derived orthotopic xenograft; H&E, hematoxylin and eosin; IHC, immunohistochemistry.

Article Snippet: Paraffin-embedded sections (5 μm) were stained with H&E or subjected to immunohistochemistry using primary antibodies against human Ki67 (proliferation marker; Thermo Fisher Scientific, Waltham, MA, USA; 1:200), human CD44 (tumor cell marker; Acris Antibodies, Rockville, MD, USA; 1:75), mouse CD31 (angiogenesis marker; Abcam, Cambridge, MA, USA; 1:200), and human PD-L1 (programmed death-ligand 1, immune checkpoint ligand; BioLegend, San Diego, CA, USA; 1:200) [ ].

Techniques: Comparison, Derivative Assay, Formalin-fixed Paraffin-Embedded, Preserving, Staining, Immunohistochemistry, Marker, Microscopy, Software, Imaging

Journal: Cancers

Article Title: Optimizing Sequential Targeted Therapies in Advanced Renal Cell Carcinoma Using Patient-Derived Orthotopic Xenograft Mouse Avatars

doi: 10.3390/cancers18101615

Figure Lengend Snippet: Histopathological and immunohistochemical evaluation of targeted therapy responses in the KiCa-Pt58 patient-derived orthotopic xenograft (PDOX) model. ( A ) Representative images of left kidney tumors from KiCa-Pt58 PDOX mice after vehicle control or sequential targeted therapy (Everolimus→Sunitinib [E→S], Pazopanib→Sunitinib [P→S], Sunitinib→Everolimus [S→E], Pazopanib→Everolimus [P→E]). Formalin-fixed, paraffin-embedded sections were stained with hematoxylin and eosin (H&E) for tumor architecture or subjected to immunohistochemistry (IHC) for human CD44 (tumor cell marker), human Ki67 (proliferation marker), mouse CD31 (angiogenesis/endothelial marker), and human PD-L1 (immune checkpoint ligand). Brown staining indicates positive immunoreactivity. Images were acquired at 100× original magnification using an Axiovert 200M deconvolution microscope and SlideBook 6.0 software (Intelligent Imaging Innovations, Denver, CO, USA). ( B – D ) Quantitative analysis of positive staining area (%) for Ki67 ( B ), CD31 ( C ), and PD-L1 ( D ) across treatment groups. Positive (brown) areas were quantified digitally using Adobe Photoshop 7.0 (percentage immunoreactive area per field). Data are presented as mean ± SEM (multiple fields per sample; n = 7–9 mice per group). Statistical comparisons vs. control were performed using one-way ANOVA followed by Dunnett’s or Tukey’s post hoc tests (GraphPad Prism v7). Asterisks indicate significance: * p < 0.05; ** p < 0.01; *** p < 0.001. Effective regimens (particularly P→E and S→E) significantly reduced Ki67+ proliferation, CD31+ vascularity, and PD-L1 expression compared to control, consistent with antitumor and potential immunomodulatory effects. Abbreviations: PDOX, patient-derived orthotopic xenograft; IHC, immunohistochemistry; E, everolimus; S, sunitinib; P, pazopanib.

Article Snippet: Paraffin-embedded sections (5 μm) were stained with H&E or subjected to immunohistochemistry using primary antibodies against human Ki67 (proliferation marker; Thermo Fisher Scientific, Waltham, MA, USA; 1:200), human CD44 (tumor cell marker; Acris Antibodies, Rockville, MD, USA; 1:75), mouse CD31 (angiogenesis marker; Abcam, Cambridge, MA, USA; 1:200), and human PD-L1 (programmed death-ligand 1, immune checkpoint ligand; BioLegend, San Diego, CA, USA; 1:200) [ ].

Techniques: Immunohistochemical staining, Derivative Assay, Control, Formalin-fixed Paraffin-Embedded, Staining, Immunohistochemistry, Marker, Microscopy, Software, Imaging, Expressing

Journal: Cancers

Article Title: Optimizing Sequential Targeted Therapies in Advanced Renal Cell Carcinoma Using Patient-Derived Orthotopic Xenograft Mouse Avatars

doi: 10.3390/cancers18101615

Figure Lengend Snippet: Histopathological and immunohistochemical assessment of targeted therapy responses in the KiCa-Pt118 patient-derived orthotopic xenograft (PDOX) model. ( A ) Representative images of left kidney tumors from KiCa-Pt118 PDOX mice after vehicle control or sequential targeted therapy (Everolimus→Sunitinib [E→S], Pazopanib→Sunitinib [P→S], Sunitinib→Everolimus [S→E], Pazopanib→Everolimus [P→E]). Formalin-fixed, paraffin-embedded sections were stained with hematoxylin and eosin (H&E) for tumor architecture or subjected to immunohistochemistry (IHC) for human CD44 (tumor cell marker), human Ki67 (proliferation marker), mouse CD31 (angiogenesis/endothelial marker), and human PD-L1 (immune checkpoint ligand). Brown staining indicates positive immunoreactivity. Images were acquired at 100× original magnification using an Axiovert 200M deconvolution microscope and SlideBook 6.0 software (Intelligent Imaging Innovations, Denver, CO, USA). ( B – D ) Quantitative analysis of positive staining area (%) for Ki67 ( B ), CD31 ( C ), and PD-L1 ( D ) across treatment groups. Positive (brown) areas were quantified digitally using Adobe Photoshop 7.0 (percentage immunoreactive area per field), as described in . Data are presented as mean ± SEM (multiple fields per sample; n = 7–9 mice per group). Statistical comparisons vs. control were performed using one-way ANOVA followed by Dunnett’s or Tukey’s post hoc tests (GraphPad Prism v7). Asterisks indicate significance: * p < 0.05; ** p < 0.01; *** p < 0.001. Effective regimens (particularly S→E) significantly reduced Ki67+ proliferation, CD31+ vascularity, and PD-L1 expression compared to control, consistent with antitumor activity in this indolent, non-metastatic model. Abbreviations: PDOX, patient-derived orthotopic xenograft; IHC, immunohistochemistry; E, everolimus; S, sunitinib; P, pazopanib.

Article Snippet: Paraffin-embedded sections (5 μm) were stained with H&E or subjected to immunohistochemistry using primary antibodies against human Ki67 (proliferation marker; Thermo Fisher Scientific, Waltham, MA, USA; 1:200), human CD44 (tumor cell marker; Acris Antibodies, Rockville, MD, USA; 1:75), mouse CD31 (angiogenesis marker; Abcam, Cambridge, MA, USA; 1:200), and human PD-L1 (programmed death-ligand 1, immune checkpoint ligand; BioLegend, San Diego, CA, USA; 1:200) [ ].

Techniques: Immunohistochemical staining, Derivative Assay, Control, Formalin-fixed Paraffin-Embedded, Staining, Immunohistochemistry, Marker, Microscopy, Software, Imaging, Expressing, Activity Assay

Journal: bioRxiv

Article Title: Desmoglein-3 modulates p38MAPK and ERK signaling responses through the mechano-sensitive channel Piezo1

doi: 10.64898/2026.05.11.723746

Figure Lengend Snippet: A . Immunofluorescence staining for DSG3 and desmoplakin (DSP) of CTRL and DSG3-KO HaCaT keratinocytes. Scale bar 10 μm. B . Quantification of DSP intensity over the corresponding membrane length (μm), Mann-Whitney test. Each data point represents one cell from three independent experiments in total. C . Immunofluorescence staining for Pan-cytokeratin (pan-CK) of CTRL and DSG3-KO HaCaT keratinocytes. Scale bar 10 μm. D . Analysis of pan-CK staining by quantifying the intensity (a.u) perpendicular to cell borders over a distance of 10 µm. E . Dispase-based dissociation assay of CTRL and DSG3-KO cells. Representative images and quantifications of N = 3 are shown, Welch’s t-test. F-G . Western blot and representative quantification of phosphorylated p38MAPK (p-p38MAPK) and ERK (pERK) in CTRL and DSG3-KO HaCaT keratinocytes. Each dot represents biological replicates. Welch’s t-test.

Article Snippet: The following primary antibodies were diluted with Odyssey blocking buffer in TBS containing 0.1% Tween 20 (Thermo Fisher Scientific) and incubated overnight at 4°C, with rotation: mouse GAPDH mAb (Santa Cruz Biotechnology, #sc-47724), rabbit phospho-p38MAPK Thr180/Tyr182 (Cell Signaling Technology, #4511S), rabbit p38MAPK (Cell Signaling Technology, #9212S), rabbit ERK 1/2 (p44/42) (Cell Signaling Technology, #9102), phospho-ERK (Santa Cruz, sc-7383), mouse plakoglobin (Progen, #61005), mouse desmoplakin 1/2 (Progen, #61003), rabbit Piezo1 (Proteintech, # 15939-1-AP), rabbit Desmoglein-3 (5G11, Santa Cruz Biotechnology, # sc-53487), Desmoglein-2 (10G11, Acris OriGene, #BM5016), mouse Pan Cytokeratin mAb (Thermo Fisher, #41-9003-82), Phalloidin (Thermo Fisher, #21833).

Techniques: Immunofluorescence, Staining, Membrane, MANN-WHITNEY, Western Blot

Journal: The Journal of Pathology: Clinical Research

Article Title: The prognostic significance of the IASLC grading system in ALK ‐positive invasive non‐mucinous adenocarcinoma of the lung: correlation with clinicopathological features

doi: 10.1002/2056-4538.70093

Figure Lengend Snippet: Increased IASLC grade association with elevated immune cell infiltration. (A) H&E staining showing increased TILs with grade elevation. (B) Higher IASLC grades exhibited a rise in intratumoral CD4+ T‐cell accumulation. (C) Correlation of advanced IASLC grades with a prominent rise in CD8+ T‐lymphocytes. (D) Lack of significant difference in FoxP3 + lymphocyte count across grades. (E) Quantitative analysis of CD4+, CD8+, and FoxP3+ cells by IHC. (F) CD4:CD8 and CD8:FoxP3 ratios across IASLC grades (bar = 50 μm). H&E, hematoxylin and eosin; IASLC, International Association for the Study of Lung Cancer; TILs, tumor‐infiltrating lymphocytes.

Article Snippet: The antibodies used included: ALK (790‐4797, ready‐to‐use, Ventana®), TTF‐1 (11833669A, 1:100, Zhongshan Golden Bridge Biotechnology, Beijing, China), p40 (25081519, 1:100, Dako, Carpinteria, CA, USA), Ki‐67 ( GT209429 , 1:100, Gene Tech Company Limited, Shanghai, China), PD‐L1 (SK006, ready‐to‐use, Dako, Carpinteria, CA, USA), CD4 (IR649, 1:100, Dako, Carpinteria, CA, USA), CD8 (ZA‐0508, 1:100, Zhongshan Golden Bridge Biotechnology, Beijing, China), and FoxP3 (sc‐53876, 1:100, Santa Cruz, Dallas, TX, USA).

Techniques: Staining

Journal: Genes & Diseases

Article Title: Dual-mode aptamer-driven biosensing platform for ultrasensitive and mutation-resilient detection of the SARS-CoV-2 nucleocapsid protein

doi: 10.1016/j.gendis.2025.101943

Figure Lengend Snippet: Workflow of NP14 aptamer screening and development of the MD ELAAA detection platform. (A) Schematic illustration of the X-aptamer protein SELEX process for isolating aptamers. (B) Schematic illustration of the ultrasensitive detection of the SARS-CoV-2 N protein via the MD ELAAA platform.

Article Snippet: X-Aptamer libraries were acquired from AM Biotechnologies (Houston, Texas, USA); His-Tag magnetic beads (Invitrogen, DynabeadsTM His-Tag Isolation & Pulldown, 10103D), SARS-CoV-2 N protein, and anti-SARS-CoV-2 N protein monoclonal antibodies (anti-SARS-CoV-2 N protein mAb, Cat: 40143-MM05, 40588-R001) were purchased from Sino Biological.

Techniques:

Journal: Genes & Diseases

Article Title: Dual-mode aptamer-driven biosensing platform for ultrasensitive and mutation-resilient detection of the SARS-CoV-2 nucleocapsid protein

doi: 10.1016/j.gendis.2025.101943

Figure Lengend Snippet: Binding affinity and stability characterization of the NP14 aptamer. (A) Magnetic bead (12.5 mg/mL, 3 μL) flow assay for the binding of the aptamer to the His-tag SARS-CoV-2 N protein (1 μg). (B) Flow cytometry analysis of the binding of 300 nM FAM-labeled aptamer NP14 to magnetic beads coated with the SARS-CoV-2 N protein. (C) Flow cytometry analysis of the binding of 300 nM FAM-labeled NP14 to magnetic beads coated with the SARS-CoV-2 N protein at different temperatures (4 °C, 25 °C, and 37 °C). (D) The binding affinity of NP14 for the SARS-CoV-2 N protein was validated via the use of 2 μg/mL SARS-CoV-2 N protein and biotin-labeled NP14 at different concentrations (0, 2.5, 5, 10, 20, 50, 100, 150, and 200 nM). (E) Determination of the Kd value of aptamer NP14 (15.625, 31.25, 62.5, 125, 250, and 500 nM) via surface plasmon resonance. (F) Confocal analysis of 300 nM FAM-labeled aptamer NP14 with SARS-CoV-2 N protein-coated magnetic beads (scale bar = 30 μm).

Article Snippet: X-Aptamer libraries were acquired from AM Biotechnologies (Houston, Texas, USA); His-Tag magnetic beads (Invitrogen, DynabeadsTM His-Tag Isolation & Pulldown, 10103D), SARS-CoV-2 N protein, and anti-SARS-CoV-2 N protein monoclonal antibodies (anti-SARS-CoV-2 N protein mAb, Cat: 40143-MM05, 40588-R001) were purchased from Sino Biological.

Techniques: Binding Assay, Flow Cytometry, Labeling, Magnetic Beads, SPR Assay

Journal: Genes & Diseases

Article Title: Dual-mode aptamer-driven biosensing platform for ultrasensitive and mutation-resilient detection of the SARS-CoV-2 nucleocapsid protein

doi: 10.1016/j.gendis.2025.101943

Figure Lengend Snippet: Structural basis and binding mechanism of NP14 interaction with the SARS-CoV-2 N protein. (A) Molecular simulation of the binding mode between aptamer NP14 and the SARS-CoV-2 N protein ( http://www.rcsb.org , ID:6VYO) via AutoDock. (B) Enlarged view of the presumed binding area. (C) Nucleic acid sequences and corresponding amino acids involved in the docking model. (D) Secondary structure simulation of aptamer NP14 via the Nupack web server at 37 °C. (E) Secondary structure simulation of the truncated chains NP14a via the Nupack web server at 37 °C. (F) Secondary structure simulation of the truncated chains NP14b via the Nupack web server at 37 °C. (G) Binding analysis of NP14 with truncated NP14a, NP14b, and base-mutated 400 nM NP14a1, NP14a2, NP14a3, NP14a4, NP14b1, NP14b2, NP14b3, NP14b4, and NP14b5 to the SARS-CoV-2 N protein by ELONA. Data were presented as mean ± standard deviation of triplicate results ( n = 3). The NP14 control: ns, not significant; ∗ p < 0.05, ∗∗ p < 0.01, and ∗∗∗ p < 0.001. (H) Circular dichroism spectroscopy of AS1411 (20 μM) and NP14 (10 μM) was performed in PBS buffer (0.01 M, pH = 7.4) at wavelengths ranging from 220 to 320 nm. (I) Domain organization of the SARS-CoV-2 N protein, with numbers indicating domain boundaries. (J) Immunomagnetic beads (40 μL, 10 mg/mL) labeled with Flag antibodies against the truncated overexpressed protein were reacted with 300 nM biotin-labeled NP14 to assess binding. Data were presented as mean ± standard deviation of triplicate results ( n = 3). Compared with the blank control: ∗∗∗∗ p < 0.0001. (K) 250 nM biotin-labeled NP14 was mixed with 250 nM unlabeled N1, A58, A61 and competitive binding was analyzed by ELONA. Data were presented as mean ± standard deviation of four replicate results ( n = 4). Compared with the NP14: ns, not significant; ∗∗∗ p < 0.001. (L) Evaluation of the binding affinity for truncated proteins containing the NTD region at different concentrations of NP14 (0, 2, 5, 10, 20, 50, and 100 nM). Data were presented as mean ± standard deviation of triplicate results ( n = 3).

Article Snippet: X-Aptamer libraries were acquired from AM Biotechnologies (Houston, Texas, USA); His-Tag magnetic beads (Invitrogen, DynabeadsTM His-Tag Isolation & Pulldown, 10103D), SARS-CoV-2 N protein, and anti-SARS-CoV-2 N protein monoclonal antibodies (anti-SARS-CoV-2 N protein mAb, Cat: 40143-MM05, 40588-R001) were purchased from Sino Biological.

Techniques: Binding Assay, Standard Deviation, Control, Circular Dichroism, Spectroscopy, Labeling

Journal: Genes & Diseases

Article Title: Dual-mode aptamer-driven biosensing platform for ultrasensitive and mutation-resilient detection of the SARS-CoV-2 nucleocapsid protein

doi: 10.1016/j.gendis.2025.101943

Figure Lengend Snippet: Specificity and cross-variant recognition of NP14 for the SARS-CoV-2 N protein. (A) ELONA method detection mode diagram. (B) NP14 labeled with 400 nM biotin was used with various proteins (1 μg/mL): SARS-CoV N protein, human coronavirus (HCoV) 229E, OC43, HKU1, SARS-CoV-2 receptor-binding domain (RBD), alpha-fetoprotein (AFP), interleukin-4 (IL-4), bovine serum albumin (BSA), and influenza (InFlu) A and B proteins, to validate the specificity of NP14 via ELISA. Data were presented as mean ± standard deviation of triplicate results ( n = 3). Compared with the SARS-CoV-2 N protein: ns, not significant; ∗∗∗∗ p < 0.0001. (C) Direct detection of SARS-CoV-2 N protein binding activity at various concentrations (0, 0.5, 1, 5, 10, 20, 50, 100, 200, 500, 800, and 1000 ng/mL) via the ELONA platform. Data were presented as mean ± standard deviation of triplicate results ( n = 3). (D – L) Detection of NP14 (biotin-labeled, 400 nM) binding to N recombinant proteins from SARS-CoV-2 variants at different concentrations (0, 5, 10, 20, 50, 100, 200, 500, and 1000 ng/mL) on the direct ELONA platform. Variants included (D) alpha, (E) beta, (F) gamma, (G) delta, (H) omicron B.1.640, (I) omicron BA.2, (J) lambda, (K) omicron BA.1, and (L) omicron BA.4.

Article Snippet: X-Aptamer libraries were acquired from AM Biotechnologies (Houston, Texas, USA); His-Tag magnetic beads (Invitrogen, DynabeadsTM His-Tag Isolation & Pulldown, 10103D), SARS-CoV-2 N protein, and anti-SARS-CoV-2 N protein monoclonal antibodies (anti-SARS-CoV-2 N protein mAb, Cat: 40143-MM05, 40588-R001) were purchased from Sino Biological.

Techniques: Variant Assay, Labeling, Binding Assay, Enzyme-linked Immunosorbent Assay, Standard Deviation, Protein Binding, Activity Assay, Recombinant

Journal: Genes & Diseases

Article Title: Dual-mode aptamer-driven biosensing platform for ultrasensitive and mutation-resilient detection of the SARS-CoV-2 nucleocapsid protein

doi: 10.1016/j.gendis.2025.101943

Figure Lengend Snippet: Comparative sensitivity and specificity of antibody–antibody versus antibody–aptamer sandwich assays. (A) Standard curve for the sandwich assay (1 μg/mL antibody) using the SARS-CoV-2 N protein at various concentrations (0, 0.1, 0.5, 1, 5, 10, 20, 50, 100, 200, 500, and 1000 ng/mL). Data were presented as mean ± standard deviation of triplicate results ( n = 3). (B) Standard curve of the SARS-CoV-2 N protein in the antibody‒aptamer sandwich mode using SARS-CoV-2 N protein at various concentrations (0, 0.2, 0.5, 1, 5, 10, 20, 50, 100, 200, 500, and 1000 ng/mL). Data were presented as mean ± standard deviation of triplicate results ( n = 3). (C) Specificity validation with multiple proteins (1 μg/mL), including: SARS-CoV-2 receptor-binding domain (RBD), alpha-fetoprotein (AFP), interleukin-4 (IL-4), bovine serum albumin (BSA), influenza (InFlu) A and B proteins, to validate the specificity of the antibody–antibody (1 μg/mL) sandwich assay. Data were presented as mean ± standard deviation of triplicate results ( n = 3). Compared with the blank control: ns, not significant; ∗∗ p < 0.01 and ∗∗∗∗ p < 0.0001. (D) Validation was performed using multiple proteins at a concentration of 1 μg/mL, including: SARS-CoV-2 RBD, AFP, IL-4, BSA, InFlu A and B proteins, to validate the specificity of the antibody (1 μg/mL)-aptamer (200 nM) sandwich assay. Data were presented as mean ± standard deviation of triplicate results ( n = 3). Compared with the blank control: ns, not significant; ∗∗∗∗ p < 0.0001.

Article Snippet: X-Aptamer libraries were acquired from AM Biotechnologies (Houston, Texas, USA); His-Tag magnetic beads (Invitrogen, DynabeadsTM His-Tag Isolation & Pulldown, 10103D), SARS-CoV-2 N protein, and anti-SARS-CoV-2 N protein monoclonal antibodies (anti-SARS-CoV-2 N protein mAb, Cat: 40143-MM05, 40588-R001) were purchased from Sino Biological.

Techniques: Standard Deviation, Biomarker Discovery, Binding Assay, Control, Concentration Assay

Journal: Genes & Diseases

Article Title: Dual-mode aptamer-driven biosensing platform for ultrasensitive and mutation-resilient detection of the SARS-CoV-2 nucleocapsid protein

doi: 10.1016/j.gendis.2025.101943

Figure Lengend Snippet: Analytical performance of the MD ELAAA platform in detecting the SARS-CoV-2 N protein and viral cultures. (A) Schematic illustration of the modulation of the Ag shell layer thickness in core–shell AuNFs@Ag nanostructures leading to changes in the localized surface plasmon resonance (LSPR) and light scattering intensity. (B) Standard curve of the MD ELAAA method for different SARS-CoV-2 N proteins (0, 0.005, 0.01, 0.02, 0.05, 0.1, 0.5, 1, 2, and 5 ng/mL). Data were presented as mean ± standard deviation of triplicate results ( n = 3). (C) Validation was performed using multiple proteins at a concentration of 1 ng/mL, including: SARS-CoV-2 receptor-binding domain (RBD), alpha-fetoprotein (AFP), interleukin-4 (IL-4), bovine serum albumin (BSA), influenza (InFlu) A and B proteins, to validate the specificity of the MD ELAAA platform. Data were presented as mean ± standard deviation of triplicate results ( n = 3). The blank control: ns, not significant; ∗∗∗∗ p < 0.0001. (D) Standard curve of the MD ELAAA method for SARS-CoV-2 virus cultures at different concentrations (0, 1, 2, 5, 10, 20, 50, 100, and 200 TCID 50 /mL). Data were presented as mean ± standard deviation of triplicate results ( n = 3). (E) Standard curve of the ELAAA method for SARS-CoV-2 virus cultures at different concentrations (0, 10, 20, 50, 100, 200, 300, 500, and 1000 TCID 50 /mL). Data were presented as mean ± standard deviation of triplicate results ( n = 3).

Article Snippet: X-Aptamer libraries were acquired from AM Biotechnologies (Houston, Texas, USA); His-Tag magnetic beads (Invitrogen, DynabeadsTM His-Tag Isolation & Pulldown, 10103D), SARS-CoV-2 N protein, and anti-SARS-CoV-2 N protein monoclonal antibodies (anti-SARS-CoV-2 N protein mAb, Cat: 40143-MM05, 40588-R001) were purchased from Sino Biological.

Techniques: SPR Assay, Standard Deviation, Biomarker Discovery, Concentration Assay, Binding Assay, Control, Virus