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. 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.

IL-17D is a secreted cytokine with homology to the IL-17 family of proteins. It is preferentially expressed in skeletal muscle, brain, adipose tissue, heart, lung, and pancreas. It has been reported that IL-17D has the ability to stimulate the production of other cytokines from target tissues such as endothelial cells, treatment of endothelial cells with purified rIL-17D protein stimulated the production of IL-6, IL-8, and GM-CSF. In addition, rIL-17D also demonstrated an inhibitory effect on hemopoiesis of myeloid progenitor cells in colony formation assays.

Fibroblast growth factor receptor 2 (FGFR2) also known as CD332 is a receptor for fibroblast growth factor and it has important roles in embryonic development and tissue repair, especially bone and blood vessels. FGFR2 has two naturally occurring isoforms, FGFR2IIIb and FGFR2IIIc, created by splicing of the third immunoglobulin-like domain. FGFR2IIIb is predominantly found in ectoderm derived tissues and endothelial organ lining. Like the other members of the fibroblast growth factor receptor family, these receptors signal by binding to their ligand and dimerisation (pairing of receptors), which causes the tyrosine kinase domains to initiate a cascade of intracellular signals. On a molecular level these signals mediate cell division, growth and differentiation.

Fibroblast growth factor receptor 2 (FGFR2) also known as CD332 is a receptor for fibroblast growth factor and it has important roles in embryonic development and tissue repair, especially bone and blood vessels. FGFR2 has two naturally occurring isoforms, FGFR2IIIb and FGFR2IIIc, created by splicing of the third immunoglobulin-like domain. FGFR2IIIb is predominantly found in ectoderm derived tissues and endothelial organ lining. Like the other members of the fibroblast growth factor receptor family, these receptors signal by binding to their ligand and dimerisation (pairing of receptors), which causes the tyrosine kinase domains to initiate a cascade of intracellular signals. On a molecular level these signals mediate cell division, growth and differentiation.

Fibroblast growth factor receptor 2 (FGFR2) also known as CD332 is a receptor for fibroblast growth factor and it has important roles in embryonic development and tissue repair, especially bone and blood vessels. FGFR2 has two naturally occurring isoforms, FGFR2IIIb and FGFR2IIIc, created by splicing of the third immunoglobulin-like domain. FGFR2IIIb is predominantly found in ectoderm derived tissues and endothelial organ lining. Like the other members of the fibroblast growth factor receptor family, these receptors signal by binding to their ligand and dimerisation (pairing of receptors), which causes the tyrosine kinase domains to initiate a cascade of intracellular signals. On a molecular level these signals mediate cell division, growth and differentiation.

Kallikrein-related peptidase 7 (KLK7) is a serine protease and was initially purified from the epidermis and characterised as stratum corneum chymotryptic enzyme (SCCE). It was later identified as the seventh member of the human kallikrein family. KLK7 is secreted as an inactive zymogen in the stratum granulosum layer of the epidermis and may be activated by KLK5 or matriptase. Once active, KLK7 is able to cleave desmocollin and corneodesmosin, indicating a role for KLK7 in maintaining skin homeostasis.

Kallikrein-related peptidase 7 (KLK7) is a serine protease and was initially purified from the epidermis and characterised as stratum corneum chymotryptic enzyme (SCCE). It was later identified as the seventh member of the human kallikrein family. KLK7 is secreted as an inactive zymogen in the stratum granulosum layer of the epidermis and may be activated by KLK5 or matriptase. Once active, KLK7 is able to cleave desmocollin and corneodesmosin, indicating a role for KLK7 in maintaining skin homeostasis.

VEGF-R2 belongs to a family of proteins called receptor tyrosine kinases. The receptor has three main parts: one part extends out of the cell and binds to VEGF, another spans the cell’s membrane, while the third part is found inside the cell. The current model of VEGF-R2 activation is that VEGF binds to individual VEGF-R2 receptor proteins on the membrane, and brings two of them close enough to form a complex called a dimer. The receptor dimer is activated and initiates signaling within the cell. VEGF-R2 is a receptor tyrosine kinase (RTK) which transduces biochemical signals via lateral dimerization in the plasma membrane. Like most RTKs, VEGF-R2 is composed of an extracellular (EC) domain, a transmembrane (TM) domain, and an intracellular (IC) domain consisting of a kinase domain and sequences required for downstream signaling. The EC domain consists of seven immunoglobulin homology (Ig) domains, termed D1 (at the N-terminus) to D7 (closest to the membrane). VEGF-R2 binds to, and is