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Interferon lambda 2, also known as interleukin 28A, belongs to the newly classified type III interferon family. Expression of IFNL2 is seen in a variety of cell types in response to viral infection or treatment with double-stranded RNA. IFNL2 exerts antiviral activity by activating mx proteins, 2',5'-oligoadenylate synthetase, and interferon regulatory factor 9. It signals through a heterodimeric receptor complex composed of IL10RB and IFNLR1 which activates the JAK-STAT pathway, phosphorylating STAT1, STAT2, and STAT3.

Interferon lambda 3, also known as interleukin 28B, belongs to the newly classified type III interferon family. Expression of IFNL3 is seen in a variety of cell types in response to viral infection or treatment with double-stranded RNA. IFNL3 exerts antiviral activity and up regulation of MHC class I antigen expression. It also plays a role in Toll-like receptor (TLR)-induced antiviral defense. IFNL3 signals through a heterodimeric receptor complex composed of IL10RB and IFNLR1 which activates the JAK-STAT pathway, phosphorylating STAT1, STAT2, and STAT3. In individuals with chronic hepatitis C, the presence of specific polymorphisms near this gene has been associated with an increased response in treatment for the condition with interferon and ribavirin.

The Insulin-like growth factors (IGFs) are mitogenic polypeptide growth factors, predominantly produced in the liver, that stimulate the proliferation and survival of various cell types, including muscle, bone and cartilage tissue in vitro. IGFs belong to the Insulin gene family and are similar by structure and function to insulin, but have a much higher growth-promoting activity. IGF1 expression is regulated by growth hormone, while IGF2 expression is influenced by placenta lactogen. Both IGF1 and IGF2 signal through the tyrosine kinase type I receptor (IGFIR). Mature IGFs are generated through proteolytic processing of inactive precursor proteins. Recombinant murine IGF1 is a globular protein containing 70 amino acids, and 3 intra-molecular disulfide bonds.

Interleukin-10 (IL10) is an immunosuppressive cytokine produced by a variety of mammalian cell types including macrophages, monocytes, T-cells, B-cells and keratinocytes. IL10 inhibits the expression of pro-inflammatory cytokines such as IL1 and TNFα. Like IL4, IL10 enhances humoral immune responses and attenuates cell-mediated immune reactions. Human IL10 is active on murine cells, but murine IL10 is inactive on human cells.

Interleukin-11 (IL11) is a pleiotropic cytokine that was originally detected in the conditioned medium of an IL1α-stimulated primate bone marrow stromal cell line (PU-34) as a mitogen for the IL6-responsive murine plasmacytoma cell line T11. IL11 contains no cysteine residues or potential glycosylation sites. IL11 has multiple effects on both hematopoietic and nonhematopoietic cells. Many of the biological effects described for IL11 overlap with those of IL6. In vitro, IL11 can synergize with IL3, IL4 and SCF to shorten the G0 period of early hematopoietic progenitors. IL11 also enhances the IL3-dependent megakaryocyte colony formation. IL11 has been found to stimulate the T-cell dependent development of specific immunoglobulin-secreting B-cells.

Interleukin-13 (IL13) is an immunoregulatory cytokine produced primarily by activated Th2 cells, along with mast cells and NK cells. Targeted deletion of IL13 in mice resulted in impaired Th2 cell development and indicated that IL13 plays an important role in the expulsion of gastrointestinal parasites. IL13 exerts anti-inflammatory effects on monocytes and macrophages and inhibits the expression of inflammatory cytokines such as IL1β, TNF-α, IL6 and IL8. IL13 has also been shown to enhance B-cell proliferation and to induce isotype switching which results in an increased production of IgE. It has been suggested that the blocking of IL13 and its downstream effectors could play a role in the mechanism of asthma. Human and murine IL13 are cross-species reactive.

Interleukin-16 (IL16) is also called lymphocyte chemoattractant factor (LCF) and is mostly secreted by lymphocytes, epithelial cells, eosinophils and CD8+ T-cells. It has many functions, including the induction of IL2Rα on T-cells, the suppression of human immunodeficiency virus (HIV) replication, and the inhibition of T-cell antigen receptor/CD3 mediated T-cell stimulation in mixed lymphocyte reactions. IL16 produces its signal through the CD4 receptor. Furthermore, recombinant murine interleukin-16 contains 118 amino acid residues and shares about 85% amino acid sequence identity with different isoforms of human IL16.

Interleukin-1 alpha (IL1A) is a nonsecreted pro-inflammatory cytokine produced in a variety of cells including monocytes, tissue macrophages, keratinocytes and other epithelial cells. Both IL1A and IL1B bind to the same receptor and have similar biological properties. These cytokines have a broad range of activities including stimulation of thymocyte proliferation by inducing IL2 release, B-cell maturation and proliferation, mitogenic FGF-like activity and the ability to stimulate the release of prostaglandin and collagenase from synovial cells. However, whereas IL1B is a secreted cytokine, IL1A is predominantly a cell associated cytokine.

Interleukin-1 beta (IL1B) is a pro-inflammatory cytokine produced in a variety of cells including monocytes, tissue macrophages, keratinocytes and other epithelial cells. Both IL1A and IL1B bind to the same receptor and have similar, if not identical, biological properties. These cytokines have a broad range of activities, including the stimulation of thymocyte proliferation, B-cell maturation and proliferation, mitogenic FGF-like activity and the ability to stimulate the release of prostaglandin and collagenase from synovial cells. However, whereas IL1A is predominantly a cell associated cytokine, IL1B is a secreted cytokine.

Sterile Filtered White Lyophilized Powder.

Interleukin-1 receptor antagonist (IL1RN) was initially called the interleukin-1 (IL1) inhibitor, which is encoded by the IL1RN gene and is a member of the IL1 cytokine family. IL1RN is secreted by various types of cells, including immune cells, epithelial cells and adipocytes. In addition, IL1RN inhibits the activity of IL1 by binding to the receptor IL1R1 and preventing its association with the co-receptor IL1RAP for signaling. IL1RN is also used in the treatment of rheumatoid arthritis, an autoimmune disease in which IL1 plays a key role. The murine IL1RN is a single nonglycosylated polypeptide chain containing 152 amino acids and has been shown to block the inflammatory responses induced by IL1 both in vitro and in vivo. The protein shows 26% amino acid homology to IL1B and 19% homology to IL1A. It also shares 90% amino acid sequence identity with rat IL1RN.

GoldBio growth factors are manufactured for RESEARCH USE ONLY and cannot be sold for human consumption!

Mature mouse Interleukin 2 (IL2) shares 58% amino acid sequence identity with human IL2. It shows strain-specific heterogeneity in an N-terminal region that contains a polyglutamine stretch. Mouse and human IL2 exhibit cross-species activity. The receptor for IL2 consists of three subunits that are present on the cell surface in varying preformed complexes. The 55 kDa IL2 Rα is specific for IL2 and binds with low affinity. The 75 kDa IL2 Rβ, which is also a component of the IL15 receptor, binds IL2 with intermediate affinity. The 64 kDa common gamma chain γc/IL2 Rγ, which is shared with the receptors for IL4, IL7, IL9, IL15, and IL21, does not independently interact with IL2. Upon ligand binding, signal transduction is performed by both IL2 Rβ and γc. It drives resting T cells to proliferate and induces IL2 and IL2 Rα synthesis. It contributes to T cell homeostasis by promoting the Fas-induced death of naive CD4+ T cells but not activated CD4+ memory lymphocytes. IL2 plays a central role in the expansion and maintenance of regulatory T cells, although it inhibits the development of Th17 polarized cells.

Interleukin-21 (IL21) is a pleiotropic cytokine produced by CD4+ T-cells in response to antigenic stimulation. Its action generally enhances antigen-specific responses of immune cells. The biological effects of IL21 include induction of differentiation of T-cells-stimulated B-cells into plasma cells and memory B-cells, stimulation of IgG production with IL4, and induction of apoptotic effects in naive B-cells and stimulated B-cells in the absence of T-cell signaling. Additionally, IL21 promotes the anti-tumorigenic activity of CD8+ T-cells and natural killer (NK) cells. IL21 exerts its effect through binding to a specific type I cytokine receptor, IL21R, which also contains the gamma chain (γc) found in other cytokine receptors, including IL2, IL4, IL7, IL9 and IL15. The IL21/IL21R interaction triggers a cascade of events which includes activation of the tyrosine kinases JAK1 and JAK3, followed by activation of the transcription factors STAT1 and STAT3.

IL22 belongs to the IL10 family of regulatory cytokines, which includes IL10, IL19, IL20, IL22, IL24 and IL26. Members of this family share partial homology in their amino acid sequences, but they are dissimilar in their biological functions. Produced by T-lymphocytes and dendritic cells, IL10 contributes to the inflammatory response in vivo. IL22 signals through CRF2-4 and IL22. IL22 along with IL17 are rapidly produced by splenic lymphoid tissue inducer–like cells (LTi-like cells) and can be also produced by Th17 cells. It is also likely that IL22 plays a role in the coordinated response of both the adaptive and innate immune systems. Recombinant mouse interleukin-22 contains 147 amino acids and has approximately 81% and 92% amino acid sequence identity with human and rat IL22, respectively.

Interleukin 3 is a pleiotropic factor produced primarily by activated T cells that can stimulate the proliferation and differentiation of pluripotent hematopoietic stem cells as well as various lineage committed progenitors. In addition, IL3 also affects the functional activity of mature mast cells, basophils, eosinophils and macrophages. Because of its multiple functions and targets, it was originally studied under different names, including mast cell growth factor, P-cell stimulating factor, burst promoting activity, multicolony stimulating factor, thy-1 inducing factor and WEHI-3 growth factor.

In addition to activated T cells, other cell types can also produce IL3, such as human thymic epithelial cells, activated murine mast cells, murine keratinocytes and neurons/astrocytes. At the amino acid sequence level, mature human and murine IL3 share only 29% sequence identity. Consistent with this lack of homology, IL3 activity is highly species-specific and human IL3 does not show activity on murine cells.

Interleukin-33 (IL33) is a pro-inflammatory protein that shares structural and functional characteristics with the IL1 cytokine family. It binds and signals through the IL1RL1/ST2 receptor, activating NF-κB and MAP kinases. IL33 induces production of T-helper-2 (Th2) cell related cytokines, including IL4, IL5 and IL13, and exerts multiple inflammation-related bioactivities. It has also been reported that after addition of IL33, the levels of interferon gamma (IFNG) were reduced in polarized mouse Th1 cells.

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 all IL1 family members that signal through the IL1 receptor family members IL1Rrp2 (IL1RL2) and IL1RAcP. IL36A is mainly found in skin and lymphoid tissues, but can also be found in fetal brain, trachea, stomach and intestine. IL36A is expressed by monocytes, B-cells and T-cells. Notably, IL36A is the only novel IL1 family member expressed on T-cells. Recombinant murine IL36A contains 153 amino acid residues, which compose a single nonglycosylated polypeptide. Specifically, mouse IL36A shares 83% amino acid sequence identity with rat IL36A, 54-60% with human, rabbit, equine and bovine IL36A.

Interleukin-36A (IL36A) is a pro-inflammatory cytokine, which plays an important role in the pathophysiology of several diseases. IL36A, IL36B, and IL36G (formerly IL1F6, IL1F8, and IL1F9) are all IL1 family members that signal through the IL1 receptor family members IL1Rrp2 (IL1RL2) and IL1RAcP. IL36A is mainly found in skin and lymphoid tissues, but can also be found in the fetal brain, trachea, stomach and intestine. IL36A is expressed by monocytes, B-cells and T-cells. Notably, IL36A is the only novel IL1 family member expressed on T-cells. Recombinant murine IL36A contains 160 amino acid residues which compose a single nonglycosylated polypeptide. Specifically, mouse IL36A shares 83% amino acid sequence identity with rat IL36A, 54-60% with human, rabbit, equine and bovine IL36A.

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

Interleukin-36B (IL36B) is a pro-inflammatory cytokine which plays an important role in the pathophysiology of several diseases. IL36A, IL36B, and IL36G (formerly IL1F6, IL1F8, and IL1F9) are all IL1 family members that signal through the IL1 receptor family members IL1Rrp2 (IL1RL2) and IL1RAcP. IL36B is reported to be expressed at higher levels in psoriatic plaques than in symptomless psoriatic skin or healthy control skin. IL36B can also stimulate the production of IL6 and IL8 in synovial fibrobasts, articular chondrocytes and mature adipocytes.Within the IL1 family, IL36B/IL1F8 shares 30%, 32%, 37%, 46%, 34%, 45% and 28% amino acid sequence identity with IL1RN, IL1B, IL36RN/IL1F5, IL36A/IL1F6, IL37/IL1F7, IL36G/IL1F9 and IL1F10, respectively.

Interleukin-36 receptor antagonist (IL36RN) is a secreted protein that 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). In addition, the receptor for IL36RN has not been positively identified; however there is indirect evidence that suggests IL1Rrp2 is the receptor. Recombinant murine IL36 RN contains 154 amino acid residues and shares 91% amino acid sequence identity with human IL36RN.