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Interleukin-36A (IL36A) is a pro-inflammatory cytokine that plays an important role in the pathophysiology of several diseases. IL36A, IL36B and IL36G (formerly IL1F6, IL1F8, and IL1F9) are IL1 family members that signal through the IL1 receptor family members IL1Rrp2 (IL1RL2) and IL1RAcP. Studies have shown that IL36A is mainly found in the skin and lymphoid tissues, as well as fetal brain, trachea, stomach and intestine. Notably, IL36A is the only novel IL1 family member expressed on T-cells. IL36A contains 153 amino acid residues, which make up a single nonglycosylated polypeptide that shares 57-68% amino acid sequence identity with mouse, rabbit, equine and bovine IL36A, and 27-57% amino acid sequence identity with other novel IL1 family members.

Interleukin-36A (IL36A) is a pro-inflammatory cytokine that plays an important role in the pathophysiology of several diseases. IL36A, IL36B and IL36G (formerly IL1F6, IL1F8, and IL1F9) are IL1 family members that signal through the IL1 receptor family members IL1Rrp2 (IL1RL2) and IL1RAcP. Studies have shown that IL36A is mainly found in the skin and lymphoid tissues, as well as fetal brain, trachea, stomach and intestine. Notably, IL36A is the only novel IL1 family member expressed on T-cells. IL36A contains 158 amino acid residues which make up a single nonglycosylated polypeptide that is 30% homologous in amino acid sequence to IL1ra, and 27%, 31%, 36%, 46%, 57% and 28% homologous to IL1G, IL36Ra/IL1F5, IL37/IL1F7, IL36G/IL1F8, IL36H/IL1F9 and IL1F10 respectively.

Interleukin-36B (IL36B) is a pro-inflammatory cytokine that plays an important role in the pathophysiology of several diseases. IL36A, IL36B and IL36G (formerly IL1F6, IL1F8, and IL1F9) are IL1 family members that signal through the IL1 receptor family members IL1Rrp2 (IL1RL2) and IL1RAcP. IL36B has been reported to be expressed at higher levels in psoriatic plaques rather than symptomless psoriatic skin or healthy control skin. Furthermore, IL36B can stimulate production of IL6 and IL8 in synovial fibroblasts, articular chondrocytes and mature adipocytes.

Interleukin-36B (IL36B) is a pro-inflammatory cytokine that plays an important role in the pathophysiology of several diseases. IL36A, IL36B and IL36G (formerly IL1F6, IL1F8, and IL1F9) are IL1 family members that signal through the IL1 receptor family members IL1Rrp2 (IL1RL2) and IL1RAcP. IL36B has been reported to be expressed at higher levels in psoriatic plaques rather than symptomless psoriatic skin or healthy control skin. Furthermore, IL36B can stimulate production of IL6 and IL8 in synovial fibroblasts, articular chondrocytes and mature adipocytes. Human IL36B shares low sequence identity with IL1B, IL36RN, IL36A and IL36G.

Interleukin-36G (IL36G) is a pro-inflammatory cytokine that plays an important role in the pathophysiology of several diseases. IL36A, IL36B and IL36G (formerly IL1F6, IL1F8, and IL1F9) are IL1 family members that signal through the IL1 receptor family members IL1Rrp2 (IL1RL2) and IL1RAcP. IL36G is secreted when transfected into 293-T cells and could constitute part of an independent signaling system analogous to that of IL1A and IL1B receptor agonist and interleukin-1 receptor type I (IL1R1). Furthermore, IL36G also can function as an agonist of NFκB activation through the orphan IL1-receptor-related protein 2. Human IL36G (152 a.a.) shares 58%, 59%, 68% and 69% amino acid sequence identity with mouse, rat, bovine and equine IL36G, respectively, and 23-57% amino acid sequence identity with other family members.

Interleukin-36G (IL36G) is a pro-inflammatory cytokine that plays an important role in the pathophysiology of several diseases. IL36A, IL36B and IL36G; (formerly IL1F6, IL1F8, and IL1F9) are IL1 family members that signal through the IL1 receptor family members IL1Rrp2 (IL1RL2) and IL1RAcP. IL36B is secreted when transfected into 293-T cells and could constitute part of an independent signaling system analogous to that of IL1A and IL1B receptor agonist and interleukin-1 receptor type I (IL1R1). Furthermore, IL36G also can function as an agonist of NFκB activation through the orphan IL1-receptor-related protein 2. Recombinant human IL36G is synthesized as a protein that contains no signal sequence, no prosegment and no potential N-linked glycosylation site.There is a 53% amino acid homology between human and mouse IL36G. IL36G also has a 25-55% amino acid homology with IL36G and IL1RN, IL1B, IL36RN, IL36A, IL37, IL36B and IL1F10.

Interleukin-36 receptor antagonist (IL36RN) is a secreted protein which belongs to the interleukin 1 cytokine family (IL1 family) and is predominantly expressed in keratinocytes but not in fibroblasts, endothelial cells or melanocytes. IL36RN has been reported to antagonize the biological activity of IL36A (IL1F6), IL36B (IL1F8), and IL36G (IL1F9). Furthermore, it could constitute part of an independent signaling system analogous to IL1A, IL1B receptor agonist and interleukin-1 receptor type I (IL1R1). However, the receptor for IL36RN has not been positively identified. Indirect evidence suggests that IL1Rrp2 is its receptor. Recombinant human IL36RN contains 154 amino acid residues and shares 91% amino acid sequence identity with murine IL36RN.

Interleukin 4 is a pleiotropic cytokine that regulates diverse T-cell and B-cell responses, including cell proliferation, survival and gene expression. Produced by mast cells, T-cells and bone marrow stromal cells, IL4 regulates the differentiation of naive CD4+ T-cells into helper Th2 cells, characterized by their cytokine-secretion profile that includes secretion of IL4, IL5, IL6, IL10, and IL13, which favor a humoral immune response. Another dominant function of IL4 is the regulation of immunoglobulin class switching to the IgG1 and IgE isotypes. Excessive IL4 production by Th2 cells has been associated with elevated IgE production and allergy.

The IL5 gene is located on chromosome 5 in humans, in close proximity to the genes encoding IL3, IL4, and granulocyte-macrophage colony-stimulating factor (CSF2), which are often co-expressed in TH2 cells. Through binding to the IL5 receptor, IL5 stimulates B cell growth and increases immunoglobulin secretion and is also a key mediator in eosinophil activation. Interleukin 5 has long been associated with the cause of several allergic diseases including allergic rhinitis and asthma. Human IL5 is 115 amino acids long (murine IL5 has 133 amino acids) and is a TH2 cytokine that is part of the hematopoietic family. Unlike other members of this cytokine family (namely IL3 and CSF2), this glycoprotein is a homodimer in its active form.

Interleukin-6 (IL6) is encoded by theIL6 gene in humans and acts as both a pro-inflammatory and anti-inflammatory cytokine. It is secreted by T-cells and macrophages to stimulate an immune response. Furthermore, it plays an essential role in the final differentiation of B-cells into Ig-secreting cells, which are involved in lymphocyte and monocyte differentiation. IL6 also induces myeloma and plasmacytoma growth. The human IL6 is a single nonglycosylated polypeptide chain containing 183 amino acids and it signals through a cell-surface type I cytokine receptor complex consisting of the ligand-binding IL6RG chain (CD126), and the signal- transducing component gp130 (also called CD130). The human IL6 is equally active on mouse and rat cells.

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Interleukin-7 (IL7) is encoded by the IL7 gene and secreted by stromal cells in the red marrow and thymus. It binds to the IL7 receptor, a heterodimer consisting of IL7 receptor alpha and IL2 receptor gamma chains. IL7 stimulates the differentiation of hematopoietic stem cells into lymphoid progenitor cells. IL7 can also stimulate the proliferation of B-cells, T cells and NK cells (natural killer cells). Murine IL7 has approximately 61% amino acid sequence identity with human IL7, and both proteins exhibit cross-species activity. IL7 has been examined as an immunotherapy agent in many human clinical trials for various malignancies, along with its role in HIV-positive individuals.

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Interleukin-8 (IL8) is encoded by the IL8 gene and produced by macrophages and other cell types such as epithelial cells. IL8 is synthesized by endothelial cells, which stock IL8 in their storage vesicles. There are many receptors capable of binding to IL8; however, the molecules with the highest affinity to IL8 are receptors CXCR1 and CXCR2. As a member of the CXC chemokine family, one of the functions of IL8 is the induction of chemotaxis in its target cells, like neutrophil granulocytes, basophils, and T-cells. IL8 (72a.a.) has a 5-10-fold higher activity on neutrophil activation compared to IL8 (77 a.a.). IL8 is often associated with inflammation, and has been cited as a pro-inflammatory mediator in gingivitis and psoriasis.

Interleukin-8 (IL8) is encoded by the IL8 gene and produced by macrophages and other cell types such as epithelial cells. There are many receptors capable of binding to IL8; however, the molecules with the highest affinity to IL8 are receptors CXCR1 and CXCR2. As a member of the CXC chemokine family, one of the functions of IL8 is the induction of chemotaxis in its target cells, like neutrophil granulocytes, basophils and T-cells. IL8 (72a.a.) has a 5-10-fold higher activity on neutrophil activation, compared to IL8 (77 a.a.). IL8 is often associated with inflammation, and has been cited as a pro-inflammatory mediator in gingivitis and psoriasis.

Interleukin-9 (IL9) is encoded by the IL9 gene and is produced by T-cells and specifically by CD4+ helper cells. IL9 was originally identified as a cytokine found in the conditioned medium of a human T-cell leukemia virus type I (HTLVI) transformed T-cell line. IL9 functions through the IL-9 receptor, which activates different signal transducer and activator (STAT) proteins and thus connects this cytokine to various biological processes. IL9 can support the growth of IL-2 independent and IL4 independent helper T-cells. Human IL9 has approximately 56% amino acid sequence identity with murine IL9. The gene encoding this cytokine has been identified as a candidate gene for asthma. Genetic studies on a mouse model of asthma demonstrated that this cytokine is a determining factor in the pathogenesis of bronchial hyperresponsiveness.

C-kit ligand, the recently identified ligand for the kit tyrosine kinase receptor, is mapped to the mouse S1 locus. This pleiotropic cytokine, alternately known as stem cell factor (SCF), mast cell growth factor (MGF) and steel-factor (SLF), plays essential roles in gametogenesis, melanogenesis and early stages of hematopoiesis. In vitro and in vivo KITLG can stimulate the proliferation of mature, as well as the proliferation and maturation of immature mast cells. KITLG acts in a synergistic manner on purified primitive human and mouse hematopoietic precursors, with various growth factors (such as IL1, IL3, IL6, IL7 and Epo,) to induce myeloid, erythroid and lymphoid lineage colony formation. The finding that KITLG is also expressed in the nervous system suggests a possible role for KITLG in the development of the nervous system.

L-Histidinol dihydrochloride is a histamine precursor. It has been shown to reversibly inhibit protein synthesis.

Homocysteine is a cysteine homolog,and only differs by having an additional methylene bridge. It is often used in vitro as a reference to measure L-homocysteine in plasma in order to diagnose homocystinuria. This genetic disorder causes the body to be unable to process certain amino acids.

Higher levels of homocysteine found in the body is due to having vitamin B6 or B12 deficiencies. Finding higher levels may indicate possible cardiovascular disease; however, reducing the levels of homocysteine in the body does not appear to remedy the situation.

Leukemia Inhibitory Factor (LIF) is a lymphoid factor which promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. LIF binds to the specific LIFR-α, which forms a heterodimer containing a GP130 signal transducing subunit.LIF is normally expressed in the trophectoderm of the developing embryo and has a number of other activities including cholinergic neuron differentiation, control of stem cell pluripotency, bone and fat metabolism, mitogenesis of certain factor dependent cell lines and promotion of megakaryocyte production in vivo. LIF is not required for human embryonic stem cell cultures.

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MANF is a secreted neurotrophic factor that is expressed in brain, neuronal and certain non-neuronal tissues. It has been shown to promote survival, growth and function of dopamine specific neurons. MANF and its structural homolog CDNF each contain an N-terminal saposin-like lipid binding domain and a carboxyl-terminal domain, which is not homologous to previously characterized protein structures. MANF has been identified as a soluble ER stress protein induced by the unfolded protein response. MANF and CDNF can prevent 6-OHDA induced degeneration of dopaminergic neurons by triggering survival pathways, as shown in a rat experimental model of Parkinson disease.