Cytokines & Chemokines

CXCL10 also known as IP-10 is belonging to the CXC chemokine family. It is encoded by the CXCL10 gene, and in murine it is also named the CRG-2 gene. The gene was originally identified as an immediate early gene induced in response to macrophage activation. This chemokine elicits its effects by binding to the cell surface chemokine receptor CXCR3. CXCL10 has been shown to be a chemoattractant for activated T-lymphocytes and monocytes/macrophages. It also has other roles, such as promotion of T cell adhesion to endothelial cells, and inhibition of bone marrow colony formation and angiogenesis. Murine CXCL10 shares approximately 67 % amino acid sequence identity with human CXCL10.

CXCL10 also known as IP-10 is belonging to the CXC chemokine family. It is encoded by the CXCL10 gene, and in murine it is also named the CRG-2 gene. The gene was originally identified as an immediate early gene induced in response to macrophage activation. This chemokine elicits its effects by binding to the cell surface chemokine receptor CXCR3. CXCL10 has been shown to be a chemoattractant for activated T-lymphocytes and monocytes/macrophages. It also has other roles, such as promotion of T cell adhesion to endothelial cells, and inhibition of bone marrow colony formation and angiogenesis. Murine CXCL10 shares approximately 67 % amino acid sequence identity with human CXCL10.

Murine FGF-18 is encoded by the FGF18 gene. By phylogenetic analysis and gene location analysis, FGF-18 is divided into FGF-8 subfamily which has three members FGF-8, FGF-17 and FGF-18. Using FGF knockout mice model, the numbers of this subfamily were testified that have crucial roles in embryo development. FGF-18–/– mice have decreased expression of osteogenic markers and delayed long-bone ossification. FGF-18 has been shown in vitro that this protein is able to induce neurite outgrowth in PC12 cells. In addition, it also has significant roles in lung development and has an anabolic effect on cartilage formation.

Murine FGF-18 is encoded by the FGF18 gene. By phylogenetic analysis and gene location analysis, FGF-18 is divided into FGF-8 subfamily which has three members FGF-8, FGF-17 and FGF-18. Using FGF knockout mice model, the numbers of this subfamily were testified that have crucial roles in embryo development. FGF-18–/– mice have decreased expression of osteogenic markers and delayed long-bone ossification. FGF-18 has been shown in vitro that this protein is able to induce neurite outgrowth in PC12 cells. In addition, it also has significant roles in lung development and has an anabolic effect on cartilage formation.

Interleukin-5 Receptor alpha (IL-5Rα, CD125) is a 60 kDa hematopoietin receptor that plays a dominant role in eosinophil biology. Mature human IL-5 Rα consists of a 322 aa extracellular domain (ECD) with a WSxWS motif and a four cysteine motif, a 20 aa transmembrane segment, and a 58 aa cytoplasmic domain. Within the ECD, human IL-5Rα shares 71% aa sequence identity with mouse and rat IL-5 Rα. Alternate splicing of human IL-5 Rα generates soluble secreted forms which function as IL-5 antagonists. The high affinity receptor for IL-5 is a complex that consists of the ligand binding IL-5 Rα and the transmembrane common β chain (βc/CD131) which is shared with the receptor complexes for IL-3 and GMCSF. IL-5 Rα binds IL-5 at low affinity and then associates with preformed βc oligomers to form the signaling competent receptor complex. IL-5 stimulation of CD34+ hematopoietic progenitor cells induces the up-regulation of transmembrane IL-5Rα followed by eosinophilic differentiation and activati

Interleukin-5 Receptor alpha (IL-5Rα, CD125) is a 60 kDa hematopoietin receptor that plays a dominant role in eosinophil biology. Mature human IL-5 Rα consists of a 322 aa extracellular domain (ECD) with a WSxWS motif and a four cysteine motif, a 20 aa transmembrane segment, and a 58 aa cytoplasmic domain. Within the ECD, human IL-5Rα shares 71% aa sequence identity with mouse and rat IL-5 Rα. Alternate splicing of human IL-5 Rα generates soluble secreted forms which function as IL-5 antagonists. The high affinity receptor for IL-5 is a complex that consists of the ligand binding IL-5 Rα and the transmembrane common β chain (βc/CD131) which is shared with the receptor complexes for IL-3 and GMCSF. IL-5 Rα binds IL-5 at low affinity and then associates with preformed βc oligomers to form the signaling competent receptor complex. IL-5 stimulation of CD34+ hematopoietic progenitor cells induces the up-regulation of transmembrane IL-5Rα followed by eosinophilic differentiation and activati

Interleukin-5 Receptor alpha (IL-5Rα, CD125) is a 60 kDa hematopoietin receptor that plays a dominant role in eosinophil biology. Mature human IL-5 Rα consists of a 322 aa extracellular domain (ECD) with a WSxWS motif and a four cysteine motif, a 20 aa transmembrane segment, and a 58 aa cytoplasmic domain. Within the ECD, human IL-5Rα shares 71% aa sequence identity with mouse and rat IL-5 Rα. Alternate splicing of human IL-5 Rα generates soluble secreted forms which function as IL-5 antagonists. The high affinity receptor for IL-5 is a complex that consists of the ligand binding IL-5 Rα and the transmembrane common β chain (βc/CD131) which is shared with the receptor complexes for IL-3 and GMCSF. IL-5 Rα binds IL-5 at low affinity and then associates with preformed βc oligomers to form the signaling competent receptor complex. IL-5 stimulation of CD34+ hematopoietic progenitor cells induces the up-regulation of transmembrane IL-5Rα followed by eosinophilic differentiation and activati

Cathepsin L is an enzyme. Cathepsin L, a lysosomal endopeptidase expressed in most eukaryotic cells, is a member of the papain-like family of cysteine proteinases. Cathepsin L plays a major role in antigen processing, tumor invasion and metastasis, bone resorption, and turnover of intracellular and secreted proteins involved in growth regulation. Unlike the precursor forms of other papain family members, the 43 kDa pro-cathepsin L itself is secreted from various cells. Pro-cathepsin L is the major excreted protein of malignantly transformed mouse fibroblasts and is also one of the major acidic cysteine proteases in mammalian cells.

Cathepsin L is an enzyme. Cathepsin L, a lysosomal endopeptidase expressed in most eukaryotic cells, is a member of the papain-like family of cysteine proteinases. Cathepsin L plays a major role in antigen processing, tumor invasion and metastasis, bone resorption, and turnover of intracellular and secreted proteins involved in growth regulation. Unlike the precursor forms of other papain family members, the 43 kDa pro-cathepsin L itself is secreted from various cells. Pro-cathepsin L is the major excreted protein of malignantly transformed mouse fibroblasts and is also one of the major acidic cysteine proteases in mammalian cells.