R_Products

FGF10/KGF2 is a member of the Fibroblast Growth Factor family of proteins. KGF2 cDNA encodes a 208 amino acid residue protein with a hydrophobic amino-terminal signal peptide. Human KGF2 shares 92% and 95% amino acid sequence identity with mouse and rat KGF2, respectively. In the FGF family, KGF2 is most closely related to FGF7 (KGF1), FGF3 and FGF22 (see additional information). The expression of KGF2 transcript has been shown to be most abundant in the embryo and adult lung. Recombinant KGF2 has been shown to be mitogenic for epithelial and epidermal cells but not fibroblasts. KGF2 may play unique roles in brain and lung development, wound healing and limb bud formation.

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

Recombinant Rat Fibroblast Growth Factor 18
FGF18

FGF18 is a member of the Fibroblast Growth Factor family of mitogenic proteins. FGF18 has been shown in vitro to induce neurite outgrowth in PC12 cells. Studies of the similar proteins in mouse and chick suggest that this protein is a pleiotropic growth factor that stimulates proliferation in tissues such as the liver and small intestine. FGF18 acts as a trophic factor for elastic chondrocytes in vivo and articular chondrocytes cultured in vitro and plays an autocrine role in normal articular cartilage repair. It is most closely related to FGF8 and FGF17 (see additional information).

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Source: Escherichia coli

FGF21 is a member of the Fibroblast Growth Factor family of proteins. It is in the same endocrine signaling subfamily as FGF19 and FGF23. FGF21 is a heparin-binding ligand for FGFR1c and FGFR4 that requires the presence of beta-klotho. Expression of FGF21 mRNA has been observed in the liver, the thymus, and several types of adipose tissue. It has been shown to stimulate glucose incorporation in differentiated adipocytes, independent of insulin activity. It has been suggested that FGF21 also acts as key regulator in the adaptation to stress.

FGF9 is a member of the Fibroblast Growth Factor family of proteins. Proteins of this family play a central role during prenatal development and postnatal growth and regeneration of a variety of tissues, by promoting cellular proliferation and differentiation. FGF9 targets glial cells, astrocytes and other cells that express FGFR 1c, 2c, 3b, 3c and 4. FGF9 is a potent mitogen for both prostatic epithelial and stromal cells in culture and is an abundant, secreted growth factor that can act as both a paracrine mitogen for epithelial cells and as an autocrine mitogen for stromal cells. There is a 99% amino acid sequence homology between human, mouse and rat FGF9 proteins. In the FGF family, FGF9 is most closely associated with FGF16 and FGF20 (see additional information).

Glial cell-derived neurotrophic factor (GDNF) is a small protein that promotes the survival of various neuronal subpopulations in both the central as well as the peripheral nervous systems at different stages of their development. GDNF is a founding member of the GDNF family of ligands (GFL) and has been shown to interact with GDNF family receptor alpha 1 (GDNFA1) and GDNFA2. Rat GDNF exists as a homodimer and contains seven conserved cysteine residues, one of which (Cys 101) is used for inter-chain disulfide bridging while the others are involved in intramolecular ring formation known as the cystine knot configuration.

Glia maturation factor beta is an actin-binding protein that shows sequence similarity to the ADF/ cofilin family. It is expressed in the cytosol and on the cell surface of astrocytes and interacts with target receptors in a juxtacrine manner. GMFB is involved in the differentiation of glial cells and neurons. It stimulates axon regeneration and proliferation of astroblasts, and inhibits proliferation of tumors. It also reversibly inhibits proliferation of neuronal and non-neuronal neoplastic cells by arresting the cell cycle in the G0/G1 phase. It is suggested that GMFB acts an intracellular regulator of signal pathways. Analysis of crystallography and NMR reveals structural differences between murine and human ADF-H domains.

Heparin-binding epidermal growth factor-like growth factor (HBEGF) is synthesized as a transmembrane precursor that is cleaved by a protease to release HBEGF as the ectodomain. Its expression stimulates neurogenesis and is increased after the brain experiences cerebral hypoxia. HBEGF is known to participate in a variety of normal physiological processes such as blastocyst implantation and wound healing, as well as in pathological processes such as tumor growth, SMC hyperplasia and atherosclerosis. HBEGF is a glycoprotein exhibiting mitogenic and chemotactic activity in smooth muscle cells and fibroblasts.

Interferon gamma is the only type II interferon and binds to the heterodimeric IFNGR that consists of two chains, IFNGR1 and IFNGR2. This interaction activates the JAK-STAT pathway. IFNG is produced primarily by T-lymphocytes and natural killer (NK) cells. It is critical for innate and adaptive immunity against viral and intracellular bacterial infections. This is due partly to its ability to inhibit viral replication directly, but also due to its immunostimulatory and immunomodulatory effects. IFNG induces the production of cytokines and upregulates the expression of class I and II MHC antigens, Fc receptors, and leukocyte adhesion molecules. It modulates macrophage effector functions, influences isotype switching, and potentiates the secretion of immunoglobulins by B cells. Additionally, IFNG augments TH1 cell expansion and may be required for TH1 cell differentiation.

The Insulin-like growth factors (IGFs) are mitogenic polypeptide growth factors that stimulate the proliferation and survival of various cell types including muscle, bone, and cartilage tissue in vitro. They are predominantly produced in the liver. 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 (IGF IR). Mature IGFs are generated through proteolytic processing of inactive precursor proteins. Recombinant human IGF1 is a globular protein containing 70 amino acids, and 3 intra-molecular disulfide bonds.

Interleukin 13 (IL13) is an immunoregulatory cytokine produced primarily by activated Th2-cells, mast cells and natural killer (NK) cells. Targeted deletion of IL13 in mice resulted in impaired Th2 cell development, and indicated an important role for IL13 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 induce isotype switching, which results in an increased production of IgE. Blocking IL13 activity inhibits the pathophysiology of asthma.

Interleukin-13 (IL13) is expressed by the IL13 gene and secreted by many cell types, especially helper T-cells type 2 (Th2). The high solution form of IL13 is reported to be a monomer with two internal disulfide bonds that contribute to a bundled four α-helix configuration. Targeted deletion of IL13 in mice resulted in impaired Th2-cell development, and indicated an important role for IL13 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 that results in an increased production of IgE. Mature rat IL13 shares 60%, 76%, and 60% amino acid sequence identity with human, mouse, and rhesus IL13, respectively.

Interleukin-13 (IL13) is expressed by the IL13 gene and secreted by many cell types, especially type 2 helper T-cells (Th2). The high solution form of IL13 has been reported to be a monomer with two internal disulfide bonds that contribute to its bundled four F-helix configuration. Targeted deletion of IL13 in mice resulted in impaired Th2 cell development and suggested an important role for IL13 in the expulsion of gastrointestinal parasites. IL13 exerts anti-inflammatory effects on monocytes and macrophages, and it 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 induce isotype switching, which results in an increased production of IgE. Mature rhesus IL13 shares 95%, 59% and 60% amino acid sequence identity with human, mouse, and rat IL13, respectively.

Interleukin-16 (IL16), also called lymphocyte chemoattractant factor (LCF), is predominately secreted by lymphocytes, epithelial cells, eosinophils, and CD8+ T-cells. It has many functions, including the induction of IL-2Rα 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 signals through the CD4 receptor. Furthermore, recombinant rhesus macaque IL16 contains 121 amino acid residues and shares 95% and 85% amino acid sequence identity with human and murine IL16, respectively.

Rat Interleukin 17A (IL17A) belongs to the IL17 family that contains IL17A, IL17B, IL17C, IL17D, IL17E and IL17F. All of the members of the IL17 family are proinflammatory cytokines that share four conserved cysteine residues, but diverge at the N-terminus. Both recombinant and natural IL17 have been shown to exist as disulfide linked homodimers, and mature IL17 contains one potential N-linked glycosylation site. IL17 is a T-cell expressed pleiotropic cytokine that regulates the activities of NF-kappaB and mitogen-activated protein kinases, and can stimulate the expression of IL-6 and cyclooxygenase-2 (PTGS2/COX-2), as well as enhance the production of nitric oxide (NO).

Interleukin-1 alpha (IL1A) is a nonsecreted pro-inflammatory cytokine produced mainly by activated macrophages, as well as neutrophils, epithelial cells and endothelial cells. It possesses metabolic, physiological and hematopoietic activities, and plays one of the central roles in the regulation of immune responses. Both IL1A and IL1B bind to the same receptor and have similar but not identical biological properties. Recombinant rat IL1A contains 150 amino acids, which is a single nonglycosylated polypeptide.

Interleukin 1 alpha (IL1α) 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 IL1α and IL1β binds to the same receptor and has similar if not identical biological properties. Recombinant rhesus macaque IL1 alpha contains 150 amino acids which is a single nonglycosylated polypeptide. Among various species, the amino acid sequence of mature IL1α is conserved 60% to 70% and human IL1 has been found to be biologically active on murine cell lines.

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 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 IL1A is predominantly a cell associated cytokine, IL1B is a secreted cytokine.

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, 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 IL1A is predominantly a cell associated cytokine, IL1B is a secreted cytokine. The 17.3 kDa mature rhesus IL1B shares 98% amino acid sequence identity with human IL-1B.

Rat recombinant interleukin-1 receptor antagonist protein (IL1RN) was initially called the IL1 inhibitor which is encoded by the IL1RN gene. IL1RN is a member of the interleukin-1 (IL1) cytokine family, and is secreted by various types of cells including immune cells, epithelial cells and adipocytes. IL1RN can inhibit the activity of IL1 by binding to the IL1R1 receptor and preventing its association with the co-receptor IL1RAP. IL1RN is also used in the treatment of rheumatoid arthritis, an autoimmune disease in which IL1 plays a key role. The rat IL1RN is a single nonglycosylated polypeptide chain, containing 152 amino acids that has been shown to block the inflammatory responses induced by IL1 both in vitro and in vivo.

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IL2 is a powerful immunoregulatory lymphokine produced by T-cells in response to antigenic or mitogenic stimulation. It is expressed by CD4+ and CD8+ T-cells, γδ T-cells, B-cells, dendritic cells, and eosinophils. 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 interact independently 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.