Description: A quantitative ELISA kit for measuring Human in samples from biological fluids.

Description: Human Severe acute respiratory Coronavirus 2 Spike Glycoprotein S1 (SARS-CoV-2 Spike S1), GenBank Accession No. QHD43416.1, a.a. 13-665, fused at the C-terminus of the Fc portion of human IgG1, with a C-terminal Avi-tag, expressed in a HEK293 expression system and enzymatically biotinylated using Avi-tag™ technology. Biotinylation is confirmed to be ≥90%. MW=102 kDa. This protein runs at a higher MW by SDS-PAGE due to glycosylation.

Description: Human Severe acute respiratory Coronavirus 2 Spike Glycoprotein S1 (SARS-CoV-2 Spike S1), GenBank Accession No. QHD43416.1, a.a. 13-665, fused at the C-terminus of the Fc portion of human IgG1, with a C-terminal Avi-tag, expressed in a HEK293 expression system and enzymatically biotinylated using Avi-tag™ technology. Biotinylation is confirmed to be ≥90%. MW=102 kDa. This protein runs at a higher MW by SDS-PAGE due to glycosylation.

Description: Severe acute respiratory Coronavirus 2 Spike Glycoprotein S1 (SARS-CoV-2 Spike S1), GenBank Accession No. QHD43416.1, a.a. 16-685, fused at the C-terminus of the Fc portion of human IgG1, with a C-terminal Avi-tag, expressed in a HEK293 expression system enzymatically biotinylated using Avi-tag™ technology. Biotinylation is confirmed to be ≥90%. MW=104 kDa. This protein runs at a higher molecular weight due to glycosylation.

Description: Severe acute respiratory Coronavirus 2 Spike Glycoprotein S1 (SARS-CoV-2 Spike S1), GenBank Accession No. QHD43416.1, a.a. 16-685, fused at the C-terminus of the Fc portion of human IgG1, with a C-terminal Avi-tag, expressed in a HEK293 expression system enzymatically biotinylated using Avi-tag™ technology. Biotinylation is confirmed to be ≥90%. MW=104 kDa. This protein runs at a higher molecular weight due to glycosylation.

Description: Recombinant SARS-CoV-2 Spike protein S1 subunit, encompassing amino acids 16-685. This protein corresponds to SARS-CoV-2 Variant B.1.618 originally identified in India, and contains deletions Y145 and H146 as well as mutations E484K and D614G. It was constructed with a C-terminal Avi-Tag™ followed by a His-tag (6xHis). The protein was affinity purified.

Description: Recombinant SARS-CoV-2 Spike protein S1 subunit, encompassing amino acids 16-685. This protein corresponds to SARS-CoV2 variant B.1.429, also known as variant Epsilon originally discovered in California (USA), and contains mutations W152C, L452R and D614G. The construct also contains a C-terminal Avi-Tag™ followed by a His-tag (6xHis). The protein was enzymatically biotinylated using the Avi-Tag™ and affinity purified. 

Description: Recombinant SARS-CoV-2 Spike protein S1 subunit, encompassing amino acids 16-685. This protein corresponds to SARS-CoV2 variant B.1.617.2, also known as variant Delta originally discovered in India, and contains mutations T19R, G142D, R158G, L452R, T478K, D614G and P681R as well as deletion E156-F157. The construct also contains a C-terminal Avi-Tag™ followed by a His-tag (6xHis). The protein was affinity purified. 

Description: Recombinant SARS-CoV-2 Spike protein S1 subunit, encompassing amino acids 16-685. This protein corresponds to SARS-CoV2 variant B.1.617.2, also known as variant Delta originally discovered in India, and contains mutations T19R, G142D, R158G, L452R, T478K, D614G and P681R as well as deletion E156-F157. The construct also contains a C-terminal Avi-Tag™ followed by a His-tag (6xHis). The protein was affinity purified. 

Description: Coronavirus disease 2019 (COVID-19), formerly known as 2019-nCoV acute respiratory disease, is an infectious disease caused by SARS-CoV-2, a virus closely related to the SARS virus (1). The disease is the cause of the 2019–20 coronavirus outbreak (2). The structure of 2019-nCoV consists of the following: a Spike protein (S), hemagglutinin-esterease dimer (HE), a membrane glycoprotein (M), an envelope protein (E) a nucleoclapid protein (N) and RNA. Coronavirus invades cells through Spike (S) glycoproteins, a class I fusion protein. It is the major viral surface protein that coronavirus uses to bind to the human cell surface receptor. It also mediates the fusion of host and viral cell membrane, allowing the virus to enter human cells and begin infection (3). The spike protein is the major target for neutralizing antibodies and vaccine development (4). The protein modeling suggests that there is strong interaction between Spike protein receptor-binding domain and its host receptor angiotensin-converting enzyme 2 (ACE2), which regulate both the cross-species and human-to-human transmissions of COVID-19 (5). The recent study has shown that the SARS-CoV-2 spike protein binds ACE2 with higher affinity than SARS-CoV spike protein (6).

Description: Coronavirus disease 2019 (COVID-19), formerly known as 2019-nCoV acute respiratory disease, is an infectious disease caused by SARS-CoV-2, a virus closely related to the SARS virus (1). The disease is the cause of the 2019–20 coronavirus outbreak (2). The structure of 2019-nCoV consists of the following: a Spike protein (S), hemagglutinin-esterease dimer (HE), a membrane glycoprotein (M), an envelope protein (E) a nucleoclapid protein (N) and RNA. Coronavirus invades cells through Spike (S) glycoproteins, a class I fusion protein. It is the major viral surface protein that coronavirus uses to bind to the human cell surface receptor. It also mediates the fusion of host and viral cell membrane, allowing the virus to enter human cells and begin infection (3). The spike protein is the major target for neutralizing antibodies and vaccine development (4). The protein modeling suggests that there is strong interaction between Spike protein receptor-binding domain and its host receptor angiotensin-converting enzyme 2 (ACE2), which regulate both the cross-species and human-to-human transmissions of COVID-19 (5). The recent study has shown that the SARS-CoV-2 spike protein binds ACE2 with higher affinity than SARS-CoV spike protein (6).

Description: The Spike S1 (B.1.617 Variant) (SARS-CoV-2): ACE2 TR-FRET Assay is designed to measure the inhibition of the binding between Spike S1 (B.1.617) (SARS-CoV-2) and human ACE2 in a homogeneous 384 reaction format. This TR-FRET-based assay requires no time-consuming washing steps, making it especially suitable for high throughput screening applications. The assay procedure is straightforward and simple; the test inhibitor compound is incubated with biotinylated Spike S1, Eu-labeled ACE2, and the dye-labeled acceptor for one hour. Then the TR-FRET signal is measured using a fluorescence reader capable of measuring Time Resolved-Fluorescence Resonance Energy Transfer (TR-FRET).

Description: The Spike S1 (B.1.618 Variant) (SARS-CoV-2): ACE2 TR-FRET Assay is designed to measure the inhibition of the binding between Spike S1 (B.1.618) (SARS-CoV-2) and human ACE2 in a homogeneous 384 reaction format. This TR-FRET-based assay requires no time-consuming washing steps, making it especially suitable for high throughput screening applications. The assay procedure is straightforward and simple; the test inhibitor compound is incubated with biotinylated Spike S1, Eu-labeled ACE2, and the dye-labeled acceptor for one hour. Then the TR-FRET signal is measured using a fluorescence reader capable of measuring Time Resolved-Fluorescence Resonance Energy Transfer (TR-FRET).

Description: SARS-CoV-2 delta variant, a variant of concern (VOC), known as B.1.617.2, was detected in India in October of 2020. However, it rapidly spread all over of the world and now it is the dominant variant in the world, which account for more than 99% of the cases. This variant carries at least 13 mutations in spike protein across the sub lineages, including L452R, D614G, P681R and K417N, which can increase the affinity to the human ACE2 receptor. Enhanced transmission of the Delta variant was observed globally, which is at least 2.5 times more contagious as the other variants. The Delta variant affects the effectiveness of COVID19 vaccine and is resistant to neutralization to some extent.