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recombinant wild type sars cov 2  (Sino Biological)


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    Sino Biological recombinant wild type sars cov 2
    Dual mechanism of human ATG10S in suppressing MEF2A-driven pro-inflammatory responses. First, ATG10S directly binds to MEF2A and promotes its targeting to autolysosomes for degradation. Second, in the nucleus, ATG10S competes with MAPK7 for binding to MEF2A, thereby disrupting the TLR4-MAPK7-MEF2A signaling axis and suppressing MEF2A transcriptional activity. Together, these dual mechanisms effectively suppress the overexpression of pro-inflammatory cytokines (IFNA, IFNG, IL1B, IL6, TNF, IL8, and CCL2) <t>induced</t> <t>by</t> <t>SARS-CoV-2</t> S protein or LPS. This diagram was generated using BioRender.com.
    Recombinant Wild Type Sars Cov 2, supplied by Sino Biological, used in various techniques. Bioz Stars score: 95/100, based on 153 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/recombinant+s1/SARS-CoV-2+(2019-nCoV)+Spike+S1-His+Recombinant+Protein/pmc13618858-462-0-11
    Average 95 stars, based on 153 article reviews
    recombinant wild type sars cov 2 - by Bioz Stars, 2026-10
    95/100 stars

    Images

    1) Product Images from "Dual mechanism of human ATG10S in suppressing MEF2A-Driven pro-inflammatory responses"

    Article Title: Dual mechanism of human ATG10S in suppressing MEF2A-Driven pro-inflammatory responses

    Journal: Autophagy

    doi: 10.1080/15548627.2026.2676074

    Dual mechanism of human ATG10S in suppressing MEF2A-driven pro-inflammatory responses. First, ATG10S directly binds to MEF2A and promotes its targeting to autolysosomes for degradation. Second, in the nucleus, ATG10S competes with MAPK7 for binding to MEF2A, thereby disrupting the TLR4-MAPK7-MEF2A signaling axis and suppressing MEF2A transcriptional activity. Together, these dual mechanisms effectively suppress the overexpression of pro-inflammatory cytokines (IFNA, IFNG, IL1B, IL6, TNF, IL8, and CCL2) induced by SARS-CoV-2 S protein or LPS. This diagram was generated using BioRender.com.
    Figure Legend Snippet: Dual mechanism of human ATG10S in suppressing MEF2A-driven pro-inflammatory responses. First, ATG10S directly binds to MEF2A and promotes its targeting to autolysosomes for degradation. Second, in the nucleus, ATG10S competes with MAPK7 for binding to MEF2A, thereby disrupting the TLR4-MAPK7-MEF2A signaling axis and suppressing MEF2A transcriptional activity. Together, these dual mechanisms effectively suppress the overexpression of pro-inflammatory cytokines (IFNA, IFNG, IL1B, IL6, TNF, IL8, and CCL2) induced by SARS-CoV-2 S protein or LPS. This diagram was generated using BioRender.com.

    Techniques Used: Binding Assay, Activity Assay, Over Expression, Generated

    Related Articles

    Recombinant:

    Article Title: SARS-CoV-2 Seroprevalence of Surinamese Children and Determinants of Seropositivity in the CCREOH/MeKiTamara Cohort.
    Article Snippet: .. A total of 50 μL of recombinant NP of SARS-CoV-2 (RayBiotech, cat# 230–30164–100, Peachtree Corners, GA, USA) or recombinant S1 (Sino Biological, cat# 40591-V08H, Houston, TX, USA) at 2 μg/mL in carbonate/bicarbonate buffer was used to coat 96-well plates and incubated in a humid chamber at 4 ◦C overnight. ..

    Article Title: Robust immune responses after one dose of BNT162b2 mRNA vaccine dose in SARS-CoV-2 experienced individuals
    Article Snippet: A direct enzyme-linked immunospot (ELISpot) assay was used to determine the number of SARS-CoV-2 spike protein subunit S1-, S2-, and receptor-binding domain (RBD)-specific IgG, IgA, and IgM ASCs in fresh PBMCs. .. Ninety-six well ELISpot filter plates (Millipore, MSHAN4B50) were coated overnight with 2 μg/mL recombinant S1, S2, or RBD (Sino Biological Inc., 40591-V08H, 40590-V08B, and 40592-V08H), or 10 μg/mL of goat anti-human IgG/A/M capture antibody (Jackson ImmunoResearch Laboratory Inc., 109-005-064). .. Plates were washed 4 times with 200 μL PBS-T and blocked for 2 hours at 37°C with 200 μL RPMI 1640 containing 10% fetal calf serum (FCS), 100 units/mL of penicillin G, and 100 μg/mL of streptomycin (Gibco), referred to as complete medium.

    Article Title: Robust immune responses are observed after one dose of BNT162b2 mRNA vaccine dose in SARS-CoV-2 experienced individuals
    Article Snippet: A direct enzyme-linked immunospot (ELISpot) assay was used to determine the number of SARS-CoV-2 spike protein subunit S1-, S2-, and RBD-specific IgG, IgA, and IgM ASCs in fresh PBMCs. .. Ninety-six well ELISpot filter plates (Millipore, MSHAN4B50) were coated overnight with 2 μg/mL recombinant S1, S2, or RBD (Sino Biological Inc., 40591-V08H, 40590-V08B, and 40592-V08H), or 10 μg/mL of goat anti-human IgG/A/M capture antibody (Jackson ImmunoResearch Laboratory Inc., 109-005-064). .. Plates were washed four times with 200 μL PBS-T and blocked for 2 hours at 37°C with 200 μL RPMI-1640 containing 10% fetal calf serum (FCS), 100 units/mL of penicillin G, and 100 μg/mL of streptomycin (Gibco), referred to as complete medium.

    Article Title: Optimizing SARS-CoV-2 Immunoassays for Specificity in Dengue-Co-Endemic Areas
    Article Snippet: Preparation of in-house S1-IgG, RBD-IgG, and N-IgG ELISA assays and characterization of samples Assay development was performed in the 96-well microtiter plates (ExtraGene, Taichung City Taiwan) as previously described [ - ]. .. Briefly, recombinant S1 (Cat. No. 40591-V08H), RBD (Cat. No. 40592-V08H), and N (Cat. No. 40588-V08B) proteins specific to SARS-CoV-2 were purchased from a commercial source (Sino Biologicals, Beijing, China) and used as capturing agents. .. The presence or absence of anti-SARS-CoV-2 human IgGs in panels P1-P4 was carried out on these S1-IgG, RBD-IgG, and N-IgG ELISA assays (Figure ).

    Article Title: Circulating Spike Protein Detected in Post–COVID-19 mRNA Vaccine Myocarditis
    Article Snippet: .. Recombinant S1 (V0591-V08H, Sino Biological) and a stabilized ectodomain of the spike protein, encoding residues 1-1208 39 were used as the protein standards for S1 and full spike, respectively. .. Simoa antigen assays are performed in an automated three-step assay format onboard the HDX Analyzer (Quanterix), as previously described 42.


    Incubation:

    Article Title: SARS-CoV-2 Seroprevalence of Surinamese Children and Determinants of Seropositivity in the CCREOH/MeKiTamara Cohort.
    Article Snippet: .. A total of 50 μL of recombinant NP of SARS-CoV-2 (RayBiotech, cat# 230–30164–100, Peachtree Corners, GA, USA) or recombinant S1 (Sino Biological, cat# 40591-V08H, Houston, TX, USA) at 2 μg/mL in carbonate/bicarbonate buffer was used to coat 96-well plates and incubated in a humid chamber at 4 ◦C overnight. ..


    Enzyme-linked Immunospot:

    Article Title: Robust immune responses after one dose of BNT162b2 mRNA vaccine dose in SARS-CoV-2 experienced individuals
    Article Snippet: A direct enzyme-linked immunospot (ELISpot) assay was used to determine the number of SARS-CoV-2 spike protein subunit S1-, S2-, and receptor-binding domain (RBD)-specific IgG, IgA, and IgM ASCs in fresh PBMCs. .. Ninety-six well ELISpot filter plates (Millipore, MSHAN4B50) were coated overnight with 2 μg/mL recombinant S1, S2, or RBD (Sino Biological Inc., 40591-V08H, 40590-V08B, and 40592-V08H), or 10 μg/mL of goat anti-human IgG/A/M capture antibody (Jackson ImmunoResearch Laboratory Inc., 109-005-064). .. Plates were washed 4 times with 200 μL PBS-T and blocked for 2 hours at 37°C with 200 μL RPMI 1640 containing 10% fetal calf serum (FCS), 100 units/mL of penicillin G, and 100 μg/mL of streptomycin (Gibco), referred to as complete medium.

    Article Title: Robust immune responses are observed after one dose of BNT162b2 mRNA vaccine dose in SARS-CoV-2 experienced individuals
    Article Snippet: A direct enzyme-linked immunospot (ELISpot) assay was used to determine the number of SARS-CoV-2 spike protein subunit S1-, S2-, and RBD-specific IgG, IgA, and IgM ASCs in fresh PBMCs. .. Ninety-six well ELISpot filter plates (Millipore, MSHAN4B50) were coated overnight with 2 μg/mL recombinant S1, S2, or RBD (Sino Biological Inc., 40591-V08H, 40590-V08B, and 40592-V08H), or 10 μg/mL of goat anti-human IgG/A/M capture antibody (Jackson ImmunoResearch Laboratory Inc., 109-005-064). .. Plates were washed four times with 200 μL PBS-T and blocked for 2 hours at 37°C with 200 μL RPMI-1640 containing 10% fetal calf serum (FCS), 100 units/mL of penicillin G, and 100 μg/mL of streptomycin (Gibco), referred to as complete medium.



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    Dual mechanism of human ATG10S in suppressing MEF2A-driven pro-inflammatory responses. First, ATG10S directly binds to MEF2A and promotes its targeting to autolysosomes for degradation. Second, in the nucleus, ATG10S competes with MAPK7 for binding to MEF2A, thereby disrupting the TLR4-MAPK7-MEF2A signaling axis and suppressing MEF2A transcriptional activity. Together, these dual mechanisms effectively suppress the overexpression of pro-inflammatory cytokines (IFNA, IFNG, IL1B, IL6, TNF, IL8, and CCL2) <t>induced</t> <t>by</t> <t>SARS-CoV-2</t> S protein or LPS. This diagram was generated using BioRender.com.
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    Image Search Results


    Dual mechanism of human ATG10S in suppressing MEF2A-driven pro-inflammatory responses. First, ATG10S directly binds to MEF2A and promotes its targeting to autolysosomes for degradation. Second, in the nucleus, ATG10S competes with MAPK7 for binding to MEF2A, thereby disrupting the TLR4-MAPK7-MEF2A signaling axis and suppressing MEF2A transcriptional activity. Together, these dual mechanisms effectively suppress the overexpression of pro-inflammatory cytokines (IFNA, IFNG, IL1B, IL6, TNF, IL8, and CCL2) induced by SARS-CoV-2 S protein or LPS. This diagram was generated using BioRender.com.

    Journal: Autophagy

    Article Title: Dual mechanism of human ATG10S in suppressing MEF2A-Driven pro-inflammatory responses

    doi: 10.1080/15548627.2026.2676074

    Figure Lengend Snippet: Dual mechanism of human ATG10S in suppressing MEF2A-driven pro-inflammatory responses. First, ATG10S directly binds to MEF2A and promotes its targeting to autolysosomes for degradation. Second, in the nucleus, ATG10S competes with MAPK7 for binding to MEF2A, thereby disrupting the TLR4-MAPK7-MEF2A signaling axis and suppressing MEF2A transcriptional activity. Together, these dual mechanisms effectively suppress the overexpression of pro-inflammatory cytokines (IFNA, IFNG, IL1B, IL6, TNF, IL8, and CCL2) induced by SARS-CoV-2 S protein or LPS. This diagram was generated using BioRender.com.

    Article Snippet: Recombinant wild-type SARS-CoV-2 S protein (isolate: 2019-nCoV, 40,591-V08B1) was obtained from Sino Biological (Beijing, China).

    Techniques: Binding Assay, Activity Assay, Over Expression, Generated

    Schematic design and proposed therapeutic mechanism of the dual‐membrane biomimetic nanoplatform [A&T]MLN. (A) Fabrication process of [A&T]MLN. Cell membranes isolated from ACE2‐overexpressing HEK293T cells and THP‐1‐derived macrophages are fused and subsequently coated onto siRNA‐loaded lipid nanoparticles (prepared by thin‐film hydration) to generate the final nanoconstruct. (B) Proposed triple‐modal therapeutic action against SARS‐CoV‐2 infection: (i) neutralization of free virions via high‐affinity binding of surface‐displayed ACE2; (ii) attenuation of the cytokine storm through scavenging of key inflammatory mediators (e.g., IL‐6, TNF‐α) by macrophage‐derived membrane receptors; and (iii) intracellular delivery of therapeutic siRNA to suppress viral replication.

    Journal: Advanced Science

    Article Title: A Dual‐Membrane Biomimetic Nanoplatform Enables Triple‐Modal Therapy Against SARS‐CoV‐2 Through Viral Decoy, Inflammation Neutralizing, and Intracellular RNAi

    doi: 10.1002/advs.77581

    Figure Lengend Snippet: Schematic design and proposed therapeutic mechanism of the dual‐membrane biomimetic nanoplatform [A&T]MLN. (A) Fabrication process of [A&T]MLN. Cell membranes isolated from ACE2‐overexpressing HEK293T cells and THP‐1‐derived macrophages are fused and subsequently coated onto siRNA‐loaded lipid nanoparticles (prepared by thin‐film hydration) to generate the final nanoconstruct. (B) Proposed triple‐modal therapeutic action against SARS‐CoV‐2 infection: (i) neutralization of free virions via high‐affinity binding of surface‐displayed ACE2; (ii) attenuation of the cytokine storm through scavenging of key inflammatory mediators (e.g., IL‐6, TNF‐α) by macrophage‐derived membrane receptors; and (iii) intracellular delivery of therapeutic siRNA to suppress viral replication.

    Article Snippet: Male K18‐hACE2‐2A‐CreERT2 mice (6–8 weeks old; Saiye Model Biological Research Center Co., Ltd., China) were anesthetized and administered 50 μL of SARS‐CoV‐2 S1SP (RayBiotech, USA) via intratracheal instillation at a dose of 400 mg/kg, followed by an air bolus (150 μL) to promote distribution.

    Techniques: Membrane, Isolation, Derivative Assay, Infection, Neutralization, Binding Assay

    Molecular basis for viral interaction and cytokine neutralization. (A) Protein composition. Coomassie blue‐stained SDS‐PAGE gel of proteins extracted from [A&T]MLN and [A&T]M; LN serves as a negative control. (B) Presence of key functional proteins. Western blot analysis confirming the transfer of ACE2, IL‐6R, TNF‐R1, IL‐1R, CD116, and CD47 to [A&T]MLN and [A&T]M; LN serves as a negative control. (C) Protein secondary structure integrity. Far‐UV circular dichroism (CD) spectra of proteins extracted from [A&T]MLN, THP‐1 membrane, [A&T]M, AMLN, and TMLN. (D) Binding kinetics to SARS‐CoV‐2 spike protein. Biolayer interferometry (BLI) sensorgrams of serially diluted [A&T]MLN (62.5–1000 n m ) binding to immobilized spike S1+S2 ECD. Red lines represent the global fit to a 1:1 binding model ( R 2 = 0.99). (E, F) Virus‐induced changes in nanoparticle properties. Hydrodynamic diameter (E) and zeta potential (F) of [A&T]MLN after 2 h incubation with authentic wild‐type (WT) or Omicron BA.5 SARS‐CoV‐2. Data are presented as mean ± SD ( n = 3). Statistical significance was determined by one‐way ANOVA. ns, not significant; ** P < 0.01; *** P < 0.001; **** P < 0.0001. (G, H) Visualization of virus‐nanoparticle complexes. Representative TEM images of [A&T]MLN bound to authentic SARS‐CoV‐2 WT (G) or Omicron BA.5 (H). Scale bars, 100 nm. (I) In vitro cytokine neutralization. Residual levels of human recombinant IL‐6, IL‐1β, TNF‐α, and GM‐CSF after incubation with AMLN, TMLN, or [A&T]MLN (0–10 µg/mL), quantified by ELISA. Data are presented as mean ± SD ( n = 3). Statistical significance was determined by one‐way ANOVA. ns, not significant; * P < 0.05; ** P < 0.01; *** P < 0.001; **** P < 0.0001.

    Journal: Advanced Science

    Article Title: A Dual‐Membrane Biomimetic Nanoplatform Enables Triple‐Modal Therapy Against SARS‐CoV‐2 Through Viral Decoy, Inflammation Neutralizing, and Intracellular RNAi

    doi: 10.1002/advs.77581

    Figure Lengend Snippet: Molecular basis for viral interaction and cytokine neutralization. (A) Protein composition. Coomassie blue‐stained SDS‐PAGE gel of proteins extracted from [A&T]MLN and [A&T]M; LN serves as a negative control. (B) Presence of key functional proteins. Western blot analysis confirming the transfer of ACE2, IL‐6R, TNF‐R1, IL‐1R, CD116, and CD47 to [A&T]MLN and [A&T]M; LN serves as a negative control. (C) Protein secondary structure integrity. Far‐UV circular dichroism (CD) spectra of proteins extracted from [A&T]MLN, THP‐1 membrane, [A&T]M, AMLN, and TMLN. (D) Binding kinetics to SARS‐CoV‐2 spike protein. Biolayer interferometry (BLI) sensorgrams of serially diluted [A&T]MLN (62.5–1000 n m ) binding to immobilized spike S1+S2 ECD. Red lines represent the global fit to a 1:1 binding model ( R 2 = 0.99). (E, F) Virus‐induced changes in nanoparticle properties. Hydrodynamic diameter (E) and zeta potential (F) of [A&T]MLN after 2 h incubation with authentic wild‐type (WT) or Omicron BA.5 SARS‐CoV‐2. Data are presented as mean ± SD ( n = 3). Statistical significance was determined by one‐way ANOVA. ns, not significant; ** P < 0.01; *** P < 0.001; **** P < 0.0001. (G, H) Visualization of virus‐nanoparticle complexes. Representative TEM images of [A&T]MLN bound to authentic SARS‐CoV‐2 WT (G) or Omicron BA.5 (H). Scale bars, 100 nm. (I) In vitro cytokine neutralization. Residual levels of human recombinant IL‐6, IL‐1β, TNF‐α, and GM‐CSF after incubation with AMLN, TMLN, or [A&T]MLN (0–10 µg/mL), quantified by ELISA. Data are presented as mean ± SD ( n = 3). Statistical significance was determined by one‐way ANOVA. ns, not significant; * P < 0.05; ** P < 0.01; *** P < 0.001; **** P < 0.0001.

    Article Snippet: Male K18‐hACE2‐2A‐CreERT2 mice (6–8 weeks old; Saiye Model Biological Research Center Co., Ltd., China) were anesthetized and administered 50 μL of SARS‐CoV‐2 S1SP (RayBiotech, USA) via intratracheal instillation at a dose of 400 mg/kg, followed by an air bolus (150 μL) to promote distribution.

    Techniques: Neutralization, Staining, SDS Page, Negative Control, Functional Assay, Western Blot, Circular Dichroism, Membrane, Binding Assay, Virus, Zeta Potential Analyzer, Incubation, In Vitro, Recombinant, Enzyme-linked Immunosorbent Assay

    Broad‐spectrum antiviral activity of [A&T]MLN against SARS‐CoV‐2. (A) Dose‐response neutralization of pseudotyped SARS‐CoV‐2 variants. Neutralization activity of [A&T]MLN against a panel of pseudoviruses (WT, Alpha, Beta, Gamma, Delta, Omicron BA.4/5) was measured by a luciferase‐reporter assay. Data are presented as mean ± SD ( n = 3). (B) Contribution of the ACE2 membrane to neutralization potency. Neutralization of WT and Omicron BA.4/5 pseudoviruses by [A&T]MLN was compared to that of nanoparticles lacking the ACE2 membrane. Data are presented as mean ± SD ( n = 3). Statistical significance was determined by one‐way ANOVA. ns, not significant; * P < 0.05; **** P < 0.0001. (C) Schematic illustration of the authentic virus neutralization assay. (D) Neutralization of authentic SARS‐CoV‐2 variants. Vero E6 cells pretreated with [A&T]MLN (19.5–78 µg/mL) were infected with WT, Beta, or Omicron BA.5 viruses (MOI = 0.01). Viral titers were determined by TCID 50 . Data are presented as mean ± SD ( n = 3).

    Journal: Advanced Science

    Article Title: A Dual‐Membrane Biomimetic Nanoplatform Enables Triple‐Modal Therapy Against SARS‐CoV‐2 Through Viral Decoy, Inflammation Neutralizing, and Intracellular RNAi

    doi: 10.1002/advs.77581

    Figure Lengend Snippet: Broad‐spectrum antiviral activity of [A&T]MLN against SARS‐CoV‐2. (A) Dose‐response neutralization of pseudotyped SARS‐CoV‐2 variants. Neutralization activity of [A&T]MLN against a panel of pseudoviruses (WT, Alpha, Beta, Gamma, Delta, Omicron BA.4/5) was measured by a luciferase‐reporter assay. Data are presented as mean ± SD ( n = 3). (B) Contribution of the ACE2 membrane to neutralization potency. Neutralization of WT and Omicron BA.4/5 pseudoviruses by [A&T]MLN was compared to that of nanoparticles lacking the ACE2 membrane. Data are presented as mean ± SD ( n = 3). Statistical significance was determined by one‐way ANOVA. ns, not significant; * P < 0.05; **** P < 0.0001. (C) Schematic illustration of the authentic virus neutralization assay. (D) Neutralization of authentic SARS‐CoV‐2 variants. Vero E6 cells pretreated with [A&T]MLN (19.5–78 µg/mL) were infected with WT, Beta, or Omicron BA.5 viruses (MOI = 0.01). Viral titers were determined by TCID 50 . Data are presented as mean ± SD ( n = 3).

    Article Snippet: Male K18‐hACE2‐2A‐CreERT2 mice (6–8 weeks old; Saiye Model Biological Research Center Co., Ltd., China) were anesthetized and administered 50 μL of SARS‐CoV‐2 S1SP (RayBiotech, USA) via intratracheal instillation at a dose of 400 mg/kg, followed by an air bolus (150 μL) to promote distribution.

    Techniques: Activity Assay, Neutralization, Luciferase, Reporter Assay, Membrane, Virus, Infection