Cytokines & Chemokines

Interleukin-1beta (IL-1β) is a non-secreted proinflammatory cytokine produced mainly by activated macrophages, as well as neutrophils, epithelial cells, and endothelial cells. It possesses metabolic, physiological, haematopoietic activities, and plays one of the central roles in the regulation of the immune responses. Both IL-1αand IL-1β binds to the same receptor and have similar but not identical biological properties. The mature rat IL1β shares 90 % a.a. sequence identity with cotton rat and mouse and 65 % to 77 % with canine, human,and rhesus IL1β.

Interleukin-1beta (IL-1β) is a non-secreted proinflammatory cytokine produced mainly by activated macrophages, as well as neutrophils, epithelial cells, and endothelial cells. It possesses metabolic, physiological, haematopoietic activities, and plays one of the central roles in the regulation of the immune responses. Both IL-1αand IL-1β binds to the same receptor and have similar but not identical biological properties. The mature rat IL1β shares 90 % a.a. sequence identity with cotton rat and mouse and 65 % to 77 % with canine, human,and rhesus IL1β.

Ciliary neurotrophic factor (CNTF) is a polypeptide hormone whose actions appear to be restricted to the nervous system where it promotes neurotransmitter synthesis and neurite outgrowth in certain neuronal populations. CNTF was initially identified as a trophic factor for embryonic chick ciliary parasympathetic neurons in culture. Furthermore, the protein is also a potent survival factor for neurons and oligodendrocytes and may be relevant in reducing tissue destruction during inflammatory attacks. In addition, CNTF is useful for treatment of motor neuron disease and it could reduce food intake without causing hunger or stress. Recombinant murine CNTF containing 198 amino acids and it shares 82 % and 95 % a.a. sequence identity with human and rat CNTF.

Ciliary neurotrophic factor (CNTF) is a polypeptide hormone whose actions appear to be restricted to the nervous system where it promotes neurotransmitter synthesis and neurite outgrowth in certain neuronal populations. CNTF was initially identified as a trophic factor for embryonic chick ciliary parasympathetic neurons in culture. Furthermore, the protein is also a potent survival factor for neurons and oligodendrocytes and may be relevant in reducing tissue destruction during inflammatory attacks. In addition, CNTF is useful for treatment of motor neuron disease and it could reduce food intake without causing hunger or stress. Recombinant murine CNTF containing 198 amino acids and it shares 82 % and 95 % a.a. sequence identity with human and rat CNTF.

Ciliary neurotrophic factor (CNTF) is a polypeptide hormone whose actions appear to be restricted to the nervous system where it promotes neurotransmitter synthesis and neurite outgrowth in certain neuronal populations. CNTF was initially identified as a trophic factor for embryonic chick ciliary parasympathetic neurons in culture. Furthermore, the protein is also a potent survival factor for neurons and oligodendrocytes and may be relevant in reducing tissue destruction during inflammatory attacks. In addition, CNTF is useful for treatment of motor neuron disease and it could reduce food intake without causing hunger or stress. Recombinant murine CNTF containing 198 amino acids and it shares 82 % and 95 % a.a. sequence identity with human and rat CNTF.

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the virus that causes coronavirus disease 2019 (COVID-19), the respiratory illness responsible for the COVID-19 pandemic. SARS-CoV-2 also known as 2019-nCoV, is a positive-sense single-stranded RNA virus and is believed to have zoonotic origins and has close genetic similarity to bat coronaviruses. The receptor binding domain (RBD) of spike protein of the SARS-CoV-2 virus binds Angiotensin-Converting Enzyme 2 (ACE2) to invade the host cells. Based on structural biology studies, the RBD can be oriented either in the up/standing or down/lying state with the up/standing state associated with higher pathogenicity.

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the virus that causes coronavirus disease 2019 (COVID-19), the respiratory illness responsible for the COVID-19 pandemic. SARS-CoV-2 also known as 2019-nCoV, is a positive-sense single-stranded RNA virus and is believed to have zoonotic origins and has close genetic similarity to bat coronaviruses. The receptor binding domain (RBD) of spike protein of the SARS-CoV-2 virus binds Angiotensin-Converting Enzyme 2 (ACE2) to invade the host cells. Based on structural biology studies, the RBD can be oriented either in the up/standing or down/lying state with the up/standing state associated with higher pathogenicity.

The KRAS gene provides instructions for making a protein called K-Ras, part of the RAS/MAPK pathway. The protein relays signals from outside the cell to the cell's nucleus. These signals instruct the cell to grow and divide (proliferate) or to mature and take on specialized functions (differentiate). The K-Ras protein is a GTPase, which means it converts a molecule called GTP into another molecule called GDP. In this way the K-Ras protein acts like a switch that is turned on and off by the GTP and GDP molecules. KRAS is usually tethered to cell membranes because of the presence of an isoprene group on its C-terminus. There are two protein products of the KRAS gene in mammalian cells that result from the use of alternative exon 4 (exon 4A and 4B respectively): K-Ras4A and K-Ras4B, these proteins have different structure in their C-terminal region and use different mechanisms to localize to cellular membranes including the plasma membrane.

The KRAS gene provides instructions for making a protein called K-Ras, part of the RAS/MAPK pathway. The protein relays signals from outside the cell to the cell's nucleus. These signals instruct the cell to grow and divide (proliferate) or to mature and take on specialized functions (differentiate). The K-Ras protein is a GTPase, which means it converts a molecule called GTP into another molecule called GDP. In this way the K-Ras protein acts like a switch that is turned on and off by the GTP and GDP molecules. KRAS is usually tethered to cell membranes because of the presence of an isoprene group on its C-terminus. There are two protein products of the KRAS gene in mammalian cells that result from the use of alternative exon 4 (exon 4A and 4B respectively): K-Ras4A and K-Ras4B, these proteins have different structure in their C-terminal region and use different mechanisms to localize to cellular membranes including the plasma membrane.