Cytokines & Chemokines

SARS-CoV-2 (Severe Acute Respiratory Syndrome Coronavirus 2) also known as 2019-nCoV (2019 Novel Coronavirus) is a virus that causes illnesses ranging from the common cold to severe diseases. The spike protein mutation D614G became dominant during the globally pandemic. The D614G mutation enhances its replication ability in upper respiratory tract, transmission ability and viral loads in the patients’ lung epithelial cells. It may also affect vaccine efficacy and antibody therapy.

SARS-CoV-2 (Severe Acute Respiratory Syndrome Coronavirus 2) also known as 2019-nCoV (2019 Novel Coronavirus) is a virus that causes illnesses ranging from the common cold to severe diseases. SARS-CoV-2 Spike Protein is composed of S1 domain and S2 domain. S1 contains a receptor-binding domain (RBD) that can specifically bind to angiotensin-converting enzyme 2 (ACE2), the receptor on target cells. It is believed that SARS-CoV-2 Spike Protein (RBD) has potential value for the diagnosis of the virus.

SARS-CoV-2 (Severe Acute Respiratory Syndrome Coronavirus 2) also known as 2019-nCoV (2019 Novel Coronavirus) is a virus that causes illnesses ranging from the common cold to severe diseases. SARS-CoV-2 Spike Protein is composed of S1 domain and S2 domain. S1 contains a receptor-binding domain (RBD) that can specifically bind to angiotensin-converting enzyme 2 (ACE2), the receptor on target cells. It is believed that SARS-CoV-2 Spike Protein (RBD) has potential value for the diagnosis of the virus.

SARS-CoV-2 (Severe Acute Respiratory Syndrome Coronavirus 2) also known as 2019-nCoV (2019 Novel Coronavirus) is a virus that causes illnesses ranging from the common cold to severe diseases. SARS-CoV-2 Spike Protein is composed of S1 domain and S2 domain. S1 contains a receptor-binding domain (RBD) that can specifically bind to angiotensin-converting enzyme 2 (ACE2), the receptor on target cells. S protein plays an important role in the induction of neutralizing antibodies and T-cell responses, as well as protective immunity.

SARS-CoV-2 (Severe Acute Respiratory Syndrome Coronavirus 2) also known as 2019-nCoV (2019 Novel Coronavirus) is a virus that causes illnesses ranging from the common cold to severe diseases. SARS-CoV-2 Spike Protein is composed of S1 domain and S2 domain. S1 contains a receptor-binding domain (RBD) that can specifically bind to angiotensin-converting enzyme 2 (ACE2), the receptor on target cells. S protein plays an important role in the induction of neutralizing antibodies and T-cell responses, as well as protective immunity.

Angiotensin-Converting Enzyme 2 (ACE-2) is an integral membrane protein and a zinc metalloprotease of the ACE family. The ACE family includes somatic and germinal ACE. ACE-2 cleaves angiotensins I and II as a carboxypeptidase. ACE-2 converts angiotensin I to angiotensin 1-9, and angiotensin II to angiotensin 1-7. ACE 2 is also able to hydrolyze apelin-13 and dynorphin-13 with high efficiency. It has high binding affinity to S-RBD.

Angiotensin-Converting Enzyme 2 (ACE-2) is an integral membrane protein and a zinc metalloprotease of the ACE family. The ACE family includes somatic and germinal ACE. ACE-2 cleaves angiotensins I and II as a carboxypeptidase. ACE-2 converts angiotensin I to angiotensin 1-9, and angiotensin II to angiotensin 1-7. ACE 2 is also able to hydrolyze apelin-13 and dynorphin-13 with high efficiency. It has high binding affinity to S-RBD.

SARS-CoV-2 (Severe Acute Respiratory Syndrome Coronavirus 2) also known as 2019-nCoV (2019 Novel Coronavirus) is a virus that causes illnesses ranging from the common cold to severe diseases. The spike protein mutation N501Y is one of six key contact residues within the receptor-binding domain (RBD) and has been identified as increasing binding affinity to human and murine ACE2.

SARS-CoV-2 (Severe Acute Respiratory Syndrome Coronavirus 2) also known as 2019-nCoV (2019 Novel Coronavirus) is a virus that causes illnesses ranging from the common cold to severe diseases. The spike protein mutation N501Y is one of six key contact residues within the receptor-binding domain (RBD) and has been identified as increasing binding affinity to human and murine ACE2.