interleukin related

IL-22 Protein, Human, Recombinant (hIgG2 hFc) is expressed in HEK293 mammalian cells with C-hIgG2 Fc tag. The predicted molecular weight is 50-62 KDa and the accession number is Q9GZX6.

IL-22 Protein, Mouse, Recombinant (mFc) is expressed in HEK293 mammalian cells with C-mFc tag. The predicted molecular weight is 50-65 KDa and the accession number is Q9JJY9.

IL-22 Protein, Human, Recombinant (hIgG4 hFc) is expressed in HEK293 mammalian cells with C-hIgG4 Fc tag. The predicted molecular weight is 50-75 KDa and the accession number is Q9GZX6.

Interleukin-36 gamma (IL-36γ) is a member of the interleukin 1 cytokine family that includes three closely related genes, IL-36α, β, and γ, formerly known as IL-1F6, F8, and F9 respectively. IL-36α has been detected in both neuronal and synovial tissue, whereas IL-36β and IL-36γ are expressed in both cutaneous and mucosal epithelial cells, including the respiratory tract. IL-36β and IL-36γ stimulate proliferation, maturation and or cytokine expression by innate immune cells (such as keratinocytes and dendritic cells), and adaptive immune cells (neutrophils and T-cells) in both humans and mice. The activity of IL-36α is mediated by interleukin 1 receptor-like 2 (IL1RL2 IL1R-rp2), and is specifically inhibited by interleukin 1 family, member 5 (IL1F5 IL-1 delta). IL-36γ plays an important role in communicating the cell death to surrounding cells.

IL-22 Protein, Mouse, Recombinant (E. coli) is expressed in E. coli expression system. The predicted molecular weight is 15 KDa and the accession number is Q9JJY9.

Interleukin 25 (IL-25) belongs to the Interleukin 17 (IL-17) family of proteins, which is comprised of six members (IL-17, IL-17B through IL-17F). These proteins are secreted and are structurally related by sharing a conserved cysteine-knot fold near the C-terminus, but have considerable sequence divergence at the N-terminus. With the exception of IL-17B, which exists as a non-covalently linked dimer, all IL-17 family members are disulfide-linked dimers. IL-17 family proteins are pro-inflammatory cytokines that induce local cytokine production and are involved in the regulation of immune functions. Human interleukin-17E (IL17E), also referred to as Interleukin-25 (IL25), is a distinct member of the IL17 cytokine family comprised of at least six members sharing a conserved cysteine-knot structure but divergent at the N-terminus. IL25 is a glycoprotein secreted as dimers by innate effector eosinophils and basophils, and present at very low levels in various peripheral tissues. IL25, together with IL17B, are ligands for the cytokine receptor IL17BR, and the cross-linking induces NF-κB activation and production of the proinflammatory chemokine IL-8, as well as ERK, JNK, and p38 activation. Overexpression of IL25 gene in transgenic mice suggested that this cytokine can regulate hematopoietic and immune functions, and additionally is identified as a proinflammatory cytokine favoring Th2-type immune responses possibly by enhancing the maintenance and functions of adaptive Th2 memory cells.

Tumor necrosis factor receptor superfamily member 3, also known as Lymphotoxin-beta receptor,Tumor necrosis factor C receptor,Tumor necrosis factor receptor 2-related protein,Tumor necrosis factor receptor type III,LTBR,TNFCR, TNFR3 and TNFRSF3, is a member of the tumor necrosis factor (TNF) family of receptors. LTBR is a single-pass type I membrane protein and contains four TNFR-Cys repeats. It is expressed on the surface of most cell types, but not on T and B lymphocytes. LTBR and its ligand play a role in the development and organization of lymphoid tissue and transformed cells. Activation of LTBR can trigger apoptosis. In addition, LTBR can lead to the release of the cytokine interleukin 8.

Interleukin-31 receptor A (IL-31RA) is a newly identified type I cytokine receptor, that is related to gp130, the common receptor of the interleukin (IL) -6 family cytokines. IL-31RA forms a functional receptor complex for IL-31 together with the beta subunit of oncostatin M receptor (OSMRbeta). OSMRbeta is expressed in a subset of small-sized nociceptive neurons of adult dorsal root ganglia (DRGs).IL-31 and OSM may thus have redundant functions in the development of OSMRbeta-expressing neurons. IL-31RA Protein, Human, Recombinant (aa 20-519, His) is expressed in HEK293 mammalian cells with C-His tag. The predicted molecular weight is 58.2 kDa and the accession number is Q8NI17-1.

IL15RA is a high-affinity receptor for interleukin-15. Il15ra associates as a heterotrimer with the IL-2 receptor beta and gamma subunits to initiate signal transduction. It can signal both in cis and trans where IL15R from one subset of cells presents IL15 to neighboring IL2RG-expressing cells. Il15ra is expressed in special cells including a wide variety of Tand B cells and non-lymphoid cells.IL-15 is a cytokine that regulates T cell and natural killer cell activation and proliferation. IL-15 binds to the alpha subunit of the IL-15RA with high affinity. IL-15 also binds to the beta and gamma chains of the IL-2 receptor, but not the alpha subunit of the IL2 receptor. IL-15 is structurally and functionally related to IL-2. Both cytokines share some subunits of receptors, allowing them to compete for and negatively regulate each other's activity. The number of CD8+ memory T cells is controlled by a balance between IL-15 and IL-2. Despite their many overlapping functional properties, IL-2 and IL-15 are, in fact, quite distinct players in the immune system. IL-15 is constitutively expressed by a wide variety of cell types and tissues, including monocytes, macrophages and DCs. The enhanced activity of the IL-15N72D:IL-15RαSu Fc complex is likely the result of the increased binding activity of IL-15N72D to IL-15Rβγ c , optimized cytokine trans-presentation by the IL-15RαSu domain, the dimeric nature of the cytokine domain and its increased in vivo half-life compared to IL-15. These findings indicate that this IL-15 superagonist complex could serve as a superior immunostimulatory therapeutic agent.

Interleukin-20 receptor subunit beta（IL20RB） is a single-pass type I membrane protein and belongs to the type II cytokine receptor family. It contains 2 fibronectin type-III domains. There are two kinds of type II cytokine receptors : cytokine receptors that bind type I and type II interferons; cytokine receptors that bind members of the interleukin-10 family (interleukin-10, interleukin-20 and interleukin-22). Type II cytokine receptors are similar to type I cytokine receptors except they do not possess the signature sequence WSXWS that is characteristic of type I receptors. They are expressed on the surface of certain cells, which bind and respond to a select group of cytokines. These receptors are related predominantly by sequence similarities in their extracellular portions that are composed of tandem Ig-like domains. The intracellular domain of type II cytokine receptors is typically associated with a tyrosine kinase belonging to the Janus kinase (JAK) family.

The Interleukin-17 family proteins, comprising six members (IL-17, IL-17B through IL-17F),are secreted, structurally related proteins that share a conserved cysteine-knot fold near the C-terminus, but have considerable sequence divergence at the N-terminus. IL-17 family proteins are proinflammatory cytokines that induce local cytokine production and are involved in the regulation of immune functions. Among IL-17 family members, IL-17D is most closely related to IL-17B, sharing 27% aa sequence homology. IL-17D is expressed preferentially in skeletal muscle, heart, adipose tissue, lung, pancreas, and nervous system. Like other IL-17 family members, IL-17D modulates immune responses indirectly by stimulating the production of myeloid growth factors and chemokines including IL-6, IL-8, and GM-CSF. IL-17D has also been shown to suppress the proliferation of myeloid progenitors in colony formation assays.

Mouse Interleukin 33 (IL-33) is a 30 kDa proinflammatory cytokine which may also regulates gene transcription in producer cells. IL-33 is constitutively expressed in smooth muscle and airway epithelia. IL-33 was identified based on sequence and structural homology with IL-1 family cytokines. It is up‑regulated in arterial smooth muscle, dermal fibroblasts, and keratinocytes following IL-1 alpha or IL‑1 beta stimulation. IL-33 is structurally related to IL-1, which induces helper T cells to produce type 2 cytokines and acts through the receptor IL1RL-1. BindingIL-33 to this receptor activates NF-kappa-B and MAP kinases and induces in vitro Th2 cells to produce cytokines. In vivo, IL-33 induces the expression of IL-4, IL-5, IL-13 and also leads to severe pathological changes in mucosal organs.

Interleukin-31 receptor A (IL-31RA) is a newly identified type I cytokine receptor, that is related to gp130, the common receptor of the interleukin (IL) -6 family cytokines. IL-31RA forms a functional receptor complex for IL-31 together with the beta subunit of oncostatin M receptor (OSMRbeta). OSMRbeta is expressed in a subset of small-sized nociceptive neurons of adult dorsal root ganglia (DRGs).IL-31 and OSM may thus have redundant functions in the development of OSMRbeta-expressing neurons. IL-31RA Protein, Human, Recombinant (aa 20-519, hFc) is expressed in HEK293 mammalian cells with C-hFc tag. The predicted molecular weight is 83.8 kDa and the accession number is Q8NI17-1.

XCL2 is a small cytokine belonging to the XC chemokine family. Chemokines are a group of cytokines. Members of this group of so-called C-Chemokines belong to the SCY family of cytokines and are designated XCL (L for ligand) followed by a number. XCL2 is the new designation of SCM-1-beta. XCL2 is highly related to another chemokine called XCL1. XCL2 gene is located on chromosome 1 in humans. XCL2 is predominantly expressed in activated T cells, but can also be found at low levels in unstimulated cells. XCL2 induces chemotaxis of cells expressing the chemokine receptor XCR1. XCL2 gene has been proposed to participate in pathways (Chemokine signaling pathway, Cytokine-cytokine receptor interaction) and processes (blood circulation, signal transduction, chemotaxis, immune response). XCL2 are expected to have molecular function (chemokine activity) and to localize in various compartments (extracellular space, extracellular region). A putative protein interactor has been described (XCR1). The spliced mRNA putatively encodes a good protein, containing small cytokines (intecrine chemokine), interleukin-8 like domain; the complete protein appears to be secreted.

Interleukin-31 receptor A (IL-31RA) is a newly identified type I cytokine receptor, that is related to gp130, the common receptor of the interleukin (IL) -6 family cytokines. IL-31RA forms a functional receptor complex for IL-31 together with the beta subunit of oncostatin M receptor (OSMRbeta). OSMRbeta is expressed in a subset of small-sized nociceptive neurons of adult dorsal root ganglia (DRGs).IL-31 and OSM may thus have redundant functions in the development of OSMRbeta-expressing neurons. IL-31RA Protein, Mouse, Recombinant (His) is expressed in HEK293 mammalian cells with C-His tag. The predicted molecular weight is 56.3 kDa and the accession number is Q8K5B1-1.

Monocyte Chemoattractant Proteins 4 (MCP-4 CCL13) is a member of a distinct, structurally-related subclass of CC chemokines mainly involved in recruitment of eosinphils to inflammatory sites. CCL13 MCP-4, is a CC family chemokine that is chemoattractant for eosinophils, basophils, monocytes, macrophages, immature dendritic cells, and T cells, and its capable of inducing crucial immuno-modulatory responses through its effects on epithelial, muscular and endothelial cells. Similar to other CC chemokines, CCL13 binds to several chemokine receptors (CCR1, CCR2 and CCR3), allowing it to elicit different effects on its target cells. A number of studies have shown that CCL13 is involved in many chronic inflammatory diseases, in which it functions as a pivotal molecule involved in the selective recruitment of cell lineages to the inflamed tissues and their subsequent activation. MCP-4 CCL13 is secreted from chondrocytes and activates the proliferation of rheumatoid synovial cells, thereby leading to joint destruction in RA. The interferon-gamma in combination with interleukin-1beta tumor necrosis factor-alpha activates the production of MCP-4 CCL13 from chondrocytes in RA joints, and that secreted MCP-4 CCL13 enhances fibroblast-like synoviocyte proliferation by activating the extracellular signal-regulated kinase mitogen-activated protein kinase cascade. CCL13 may have some role in the pathogenesis of systemic sclerosis (SSc).

Interleukin-17 is a potent pro-inflammatory cytokine produced by activated memory T cells. There are at least six members of the IL-17 family in humans and in mice. Today, IL-17 represents a family of structurally related cytokines that share a highly conserved C-terminal region but differ from one another in their N-terminal regions and in their distinct biological roles. The six known members of this family, IL-17A through IL-17F, are secreted as homodimers. IL-17F also regulates cartilage matrix turnover and inhibits angiogenesis.

Human Interleukin 31 (IL-31) is a cytokine containing a four-helix bundle structure. It shares several structural and functional characteristics with IL-6, Oncostatin M, LIF, and Cardiotrophin-1. Human IL-31 cDNA encodes a 164 amino acid precursor that contains a 23 amino acid signal peptide and a 141 amino acid mature protein. Human and mouse IL-31 share 24% sequence identity in the mature region. IL-31 is mainly associated with activated T cells and is preferentially expressed by type 2 helper T cells (Th2). IL-31 signals via a heterodimeric receptor complex composed of a gp130 related molecule termed IL-31RA (also GPL and GLMR) and an Oncostatin M receptor (OSM Rβ). The IL-31 receptor is constitutively expressed by keratinocytes and upregulated by IFNγ on monocytes. GPL OSMR signaling is a strong activator of STAT3 and STAT5, and can also activate STAT1, Jak1, and Jak2 signaling pathways. IL-31 regulated immune responses have been implicated in skin physiology and inflammatory skin diseases. Studies have shown that IL31 induces severe pruritis (itching) and dermatitis in transgenic mice.

Interleukin-1 receptor antagonist protein (Il1rn), also known as IL-1ra, IRAP or IL1 inhibitor, is a member of the interleukin 1 cytokine family. This protein inhibits the activities of interleukin 1 alpha (IL1A) and interleukin 1 beta (IL1B), and modulates a variety of interleukin 1 related immune and inflammatory responses. The mouse Il1rn gene encodes a 178 amino acids (aa) protein with a 26 aa signal peptide. Mouse Il1rn protein shares 26% and 19% identity with its homologues IL-1 beta and IL-1 alpha, respectively. Il1rn can Inhibits the activity of interleukin-1 by binding to receptor IL1R1 and preventing its association with the coreceptor IL1RAP for signaling, but has no interleukin-1 like activity. Recently, an recombinant human Il1rn protein is used in the treatment of rheumatoid arthritis, an autoimmune disease in which IL-1 plays a key role.

Interleukin (IL)‑12B, which encodes the p40 subunit common to IL‑12 and IL‑23, as one of the genes for which expression in fibroblast‑like synoviocytes from patients with rheumatoid arthritis (RA‑FLS) is induced by DcR3.Decoy receptor 3 (DcR3) competitively binds to three ligands, Fas ligand, lymphotoxin‑related inducible ligand that competes for glycoprotein D binding to herpesvirus entry mediator on T cells and tumor necrosis factor‑like ligand 1A (TL1A), to prevent their effects. Recent studies have suggested that DcR3 directly affects cells as a ligand.

IL15RA is a high-affinity receptor for interleukin-15. Il15ra associates as a heterotrimer with the IL-2 receptor beta and gamma subunits to initiate signal transduction. It can signal both in cis and trans where IL15R from one subset of cells presents IL15 to neighboring IL2RG-expressing cells. Il15ra is expressed in special cells including a wide variety of Tand B cells and non-lymphoid cells.IL-15 is a cytokine that regulates T cell and natural killer cell activation and proliferation. IL-15 binds to the alpha subunit of the IL-15RA with high affinity. IL-15 also binds to the beta and gamma chains of the IL-2 receptor, but not the alpha subunit of the IL2 receptor. IL-15 is structurally and functionally related to IL-2. Both cytokines share some subunits of receptors, allowing them to compete for and negatively regulate each other's activity. The number of CD8+ memory T cells is controlled by a balance between IL-15 and IL-2. Despite their many overlapping functional properties, IL-2 and IL-15 are, in fact, quite distinct players in the immune system. IL-15 is constitutively expressed by a wide variety of cell types and tissues, including monocytes, macrophages and DCs.