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Your Position: Casa > High quality proteins for SARS-CoV-2 related research and development

High quality proteins for SARS-CoV-2 related research and development

Recombinant proteins

High purity and authentic structure

SARS-CoV-2 S protein, His Tag, Super stable trimer (MALS & NS-EM verified) (Cat.No. SPN-C52H9)

The well-folded trimeric particles of SARS-CoV-2 S protein, His Tag, Super stable trimer (SPN-C52H9) was verified by negative stain electron micrography. The particles are similar in size and appearance to SARS-CoV-2 trimers reported in published literature.

High bioactivity verified

Bioactivity-ELISA

SARS-CoV-2 (COVID-19) S1 protein, Mouse IgG2a Fc Tag
Cat.No. S1N-C5257

Immobilized Human ACE2, Fc Tag (Cat. No. AC2-H5257) at 2 μg/mL (100 μL/well) can bind SARS-CoV-2 S1 protein, Mouse IgG2a Fc Tag (Cat. No. S1N-C5257) with a linear range of 0.4-6 ng/mL (QC tested).

Bioactivity-FACS

SARS-CoV-2 (COVID-19) S1 protein, Mouse IgG2a Fc Tag
Cat.No. S1N-C5257

FACS analysis shows that SARS-CoV-2 S1 protein, Mouse IgG2a Fc Tag (Cat. No. S1N-C5257) can bind to Vero E6 cells surface ACE2. The concentration of SARS-CoV-2 S1 protein is 3 μg/ml. (Routinely tested).

Binding assay between host receptors and virus proteins(ELISA&BLI)

Bioactivity- ELISA

Human ACE2 / ACEH Protein, Fc Tag (MALS verified)
Cat.No. AC2-H5257

Immobilized Human ACE2, Fc Tag (Cat. No. AC2-H5257) at 1 μg/mL (100 μL/well) can bind SARS-CoV-2 S protein, His Tag, Super stable trimer (Cat. No. SPN-C52H9) with a linear range of 0.4-6 ng/mL (QC tested).

Bioactivity- BLI

Biotinylated Human Neuropilin-1 / NRP1 / CD304 Protein, His,Avitag™
Cat.No. NR1-H82E3

Loaded Biotinylated Human Neuropilin-1, His,Avitag (Cat. No. NR1-H82E3) on SA Biosensor, can bind SARS-CoV-2 S1 protein, His Tag (Cat. No. S1N-C52H3) with an affinity constant of 0.663 μM as determined in BLI assay (ForteBio Octet Red96e)

Antibodies

Binding assay of antibodies

Anti-SARS-CoV-2 RBD Potent Neutralizing Antibody, Chimeric mAb, Human IgG1 (AM128)
Cat.No. SPD-M128

Bioactivity- ELISA

Immobilized SARS-CoV-2 S protein RBD, His Tag (Cat. No. SPD-C52H1) at 1 μg/mL (100 μL/well) can bind Anti-SARS-CoV-2 RBD Potent Neutralizing Antibody, Chimeric mAb, Human IgG1 (AM128) (Cat. No. SPD-M128) with a linear range of 0.2-1.5ng/mL (QC tested).

Anti-SARS-CoV-2 Spike RBD Neutralizing Antibody, Human IgG1 (AS35)
Cat.No. SAD-S35

Bioactivity- ELISA

FACS analysis shows that the binding of SARS-CoV-2 S protein RBD, Mouse IgG2a Fc Tag (Cat. No. SPD-C5259) to Vero E6 cells surface ACE2 was inhibited by increasing concentration of Anti-SARS-CoV-2 Neutralizing Antibody, Human IgG1 (Cat. No. SAD-S35). The concentration of SARS-CoV-2 S protein RBD used is 5μg/ml. The IC50 is 10.33 μg/ml (Routinely tested).

Bioactivity- ELISA

FACS analysis shows that SARS-CoV-2 S protein RBD, Mouse IgG2a Fc Tag (Cat. No. SPD-C5259) can bind to Vero E6 cells surface ACE2. The concentration of SARS-CoV-2 S protein RBD is 5 μg/ml.


Neutralizing activity was verified by Pseudovirus experiment verified

Anti-SARS-CoV-2 RBD Potent Neutralizing Antibody, Chimeric mAb, Human IgG1 (AM128) (Cat.No. SPD-M128)

Serial dilutions of Anti-SARS-CoV-2 Spike NTD Antibody, Chimeric mAb (Cat. No. SPD-M128) were incubated with luciferase/SARS-CoV-2 spike pseudoviruses. HEK293T cells stably expressing ACE2 were added after 90 min and neutralization titers (IC50) is 0.03255 nM, which is calculated as the serum dilution at which RLU were reduced by 50% compared with RLU in virus control wells after subtraction of background RLU in cell control wells.

High binding affinity between Neutralizing antibody and RBD mutants verified by BLI

Anti-SARS-CoV-2 RBD Potent Neutralizing Antibody, Chimeric mAb, Human IgG1 (AM128) (Cat.No. SPD-M128)

The differences BLI results between neutralizing antibody and RBD protein mutants(BLI)(KD: M)
More SARS-CoV-2 related products

>>> Proteins for COVID-19 Serological Test Development

>>> SARS-CoV-2 related kit products

>>> Pre-coupling protein magnetic beads

>>> Any custom requests, suggestions or feedback are welcome. click here.
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