Description: Minimum order quantity: 1 unit of 1KIT

Description: Minimum order quantity: 1 unit of 1KIT

Description: Minimum order quantity: 1 unit of 1KIT

Description: LIF is a pleiotrophic factor produced by multiple cell types, including T cells, myelomonocytic lineages, fibroblasts, liver, heart and melanoma. LIF promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Other activities include the stimulation of acute phase protein synthesis by hepatocytes, stimulation of differentiation of cholinergic nerves, and suppression of adipogenesis by inhibiting the lipoprotein lipase in adipocytes. While human LIF is active on mouse cells and is widely used in the maintenance of murine ESC to prevent spontaneous differentiation, mouse LIF is not active on human cells due to its inability to bind to the human LIF receptor. Recombinant Murine LIF is a 19.9 kDa protein containing 180 amino acids residues, including three disulfide bonds.

Description: LIF is a pleiotrophic factor produced by multiple cell types, including T cells, myelomonocytic lineages, fibroblasts, liver, heart and melanoma. LIF promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Other activities include the stimulation of acute phase protein synthesis by hepatocytes, stimulation of differentiation of cholinergic nerves, and suppression of adipogenesis by inhibiting the lipoprotein lipase in adipocytes. While human LIF is active on mouse cells and is widely used in the maintenance of murine ESC to prevent spontaneous differentiation, mouse LIF is not active on human cells due to its inability to bind to the human LIF receptor. Recombinant Human LIF is a 19.7 kDa protein containing 180 amino acid residues, including three disulfide bonds.

Description: EGF is a potent growth factor that stimulates the proliferation of various epidermal and epithelial cells. Additionally, EGF has been shown to inhibit gastric secretion, and to be involved in wound healing. EGF signals through a receptor known as c-erbB, which is a class I tyrosine kinase receptor. This receptor also binds with TGF-α and VGF (vaccinia virus growth factor). Recombinant Murine EGF is a 6.0 kDa globular protein containing 53 amino acid residues, including 3 intramolecular disulfide bonds.

Description: TPO is a lineage-specific growth factor produced in the liver, kidney and skeletal muscle. It stimulates the proliferation and maturation of megakaryocytes, and promotes increased circulating levels of platelets in vivo. TPO signals through the c-mpl receptor, and acts as an important regulator of circulating platelets. Human and murine TPO exhibit cross-species reactivity. Recombinant Murine TPO is a fully biologically active 174 amino acid polypeptide (18.7 kDa), which contains the erythropoietin-like domain of the full length TPO protein.

Description: SCF is a hematopoietic growth factor that exerts its activity by signaling through the c-Kit receptor. SCF and c-Kit are essential for the survival, proliferation and differentiation of hematopoietic cells committed to the melanocyte and germ cell lineages. Human SCF manifests low activity on murine cells, while murine and rat SCF are fully active on human cells. The human SCF gene encodes for a 273 amino acid transmembrane protein, which contains a 25 amino acid N-terminal signal sequence, a 189 amino acid extracellular domain, a 23 amino acid transmembrane domain, and a 36 amino acid cytoplasmic domain. The secreted soluble form of SCF is generated by proteolytic processing of the membrane anchored precursor. Recombinant Rat SCF is an 18.4 kDa polypeptide containing 165 amino acid residues, which corresponds to the sequence of the secreted soluble form of SCF.

Description: EGF is a potent growth factor that stimulates the proliferation of various epidermal and epithelial cells. Additionally, EGF has been shown to inhibit gastric secretion, and to be involved in wound healing. EGF signals through a receptor known as c-erbB, which is a class I tyrosine kinase receptor. This receptor also binds with TGF-α and VGF (vaccinia virus growth factor). Recombinant Rat EGF is a 6.2 kDa globular protein containing 54 amino acid residues, including 3 intramolecular disulfide bonds.

Description: BAFF, a member of the TNF family of ligands, is expressed in T cells, macrophages, monocytes and dendritic cells. BAFF is involved in stimulation of B and T cell function, and is an important survival and maturation factor for peripheral B cells. BAFF signals through three different TNF receptors, TACI, BCMA and BAFF-R. The human BAFF gene codes for a 285 amino acid type II transmembrane protein containing a 46 amino acid cytoplasmic domain, a 21 amino acid transmembrane domain, and a 218 amino acid extracellular domain. Recombinant Human soluble BAFF is a 152 amino acid polypeptide (17.0 kDa), which contains the TNF-like portion of the extracellular domain of BAFF.

Description: GDNF is a disulfide-linked, homodimeric neurotrophic factor structurally related to Artemin, Neurturin and Persephin. These proteins belong to the cysteine-knot superfamily of growth factors that assume stable dimeric protein structures. GDNF signals through a multicomponent receptor system, composed of a RET and one of the four GFRα (α1-α4) receptors. GDNF specifically promotes dopamine uptake and survival, and morphological differentiation of midbrain neurons. Using a Parkinson’s disease mouse model, GDNF has been shown to improve conditions such as bradykinesia, rigidity, and postural instability. The functional human GDNF ligand is a disulfide-linked homodimer consisting of two 15 kDa polypeptide chains called monomers. Each monomer contains seven conserved cysteine residues, including Cys-101, which is used for inter-chain disulfide bridging, and others that are involved in the intramolecular ring formation known as the cysteine-knot configuration. The calculated molecular weight of Recombinant Human GDNF is 30.4 kDa.

Description: CNTF is a potent neural factor that was originally characterized as a vital factor for the survival of chick ciliary neurons in vitro. CNTF is also important for the survival of other neural cell types, including primary sensory neurons, motor neurons, basal forebrain neurons and type 2 astrocytes. CNTF is highly conserved across species and exhibits cross-species bioactivity. Recombinant Human CNTF is synthesized as a 199 amino acid polypeptide (22.8 kDa) lacking a hydrophobic N-terminal signal for secretion.

Description: VEGF is a potent growth and angiogenic cytokine. It stimulates proliferation and survival of endothelial cells, and promotes angiogenesis and vascular permeability. Expressed in vascularized tissues, VEGF plays a prominent role in normal and pathological angiogenesis. Substantial evidence implicates VEGF in the induction of tumor metastasis and intra-ocular neovascular syndromes. VEGF signals through three receptors; fms-like tyrosine kinase (flt-1), KDR gene product (the murine homolog of KDR is the flk-1 gene product) and the flt4 gene product. Recombinant Murine VEGF165 is a 39.0 kDa, disulfide-linked homodimeric protein consisting of two 165 amino acid polypeptide chains.

Description: GDNF is a disulfide-linked, homodimeric neurotrophic factor structurally related to Artemin, Neurturin and Persephin. These proteins belong to the cysteine-knot superfamily of growth factors that assume stable dimeric protein structures. GDNF signals through a multicomponent receptor system, composed of a RET and one of the four GFRα (α1-α4) receptors. GDNF specifically promotes dopamine uptake and survival, and morphological differentiation of midbrain neurons. Using a Parkinson’s disease mouse model, GDNF has been shown to improve conditions such as bradykinesia, rigidity, and postural instability. The functional murine GDNF ligand is a disulfide-linked homodimer consisting of two 15.1 kDa polypeptide chains called monomers. Each monomer contains seven conserved cysteine residues, including Cys-101, which is used for inter-chain disulfide bridging, and others that are involved in the intramolecular ring formation known as the cysteine-knot configuration. The calculated molecular weight of Recombinant Murine GDNF is 30.2 kDa.

Description: CNTF is a potent neural factor that was originally characterized as a vital factor for the survival of chick ciliary neurons in vitro. CNTF is also important for the survival of other neural cell types, including primary sensory neurons, motor neurons, basal forebrain neurons and type 2 astrocytes. CNTF is highly conserved across species and exhibits cross-species bioactivity. Recombinant Rat CNTF is synthesized as a 199 amino acid polypeptide (22.7 kDa) lacking a hydrophobic N-terminal signal for secretion.

Description: GDNF is a disulfide-linked, homodimeric neurotrophic factor structurally related to Artemin, Neurturin and Persephin. These proteins belong to the cysteine-knot superfamily of growth factors that assume stable dimeric protein structures. GDNF signals through a multicomponent receptor system, composed of a RET and one of the four GFRα (α1-α4) receptors. GDNF specifically promotes dopamine uptake and survival, and morphological differentiation of midbrain neurons. Using a Parkinson’s disease mouse model, GDNF has been shown to improve conditions such as bradykinesia, rigidity, and postural instability. The functional rat GDNF ligand is a disulfide-linked homodimer consisting of two 15 kDa polypeptide chains called monomers. Each monomer contains seven conserved cysteine residues, including Cys-101, which is used for inter-chain disulfide bridging, and others that are involved in the intramolecular ring formation known as the cysteine-knot configuration. The calculated molecular weight of Recombinant Rat GDNF is 30.0 kDa.

Description: Noggin belongs to a group of diffusible proteins that bind to ligands of the TGF-β family, and regulate their activity by inhibiting their access to signaling receptors. Noggin was originally identified as a BMP-4 antagonist whose action was critical for proper formation of the head and other dorsal structures. Consequently, noggin has been shown to modulate the activities of other BMPs including BMP-2,-7,-13, and -14. Targeted deletion of noggin in mice results in prenatal death, and a recessive phenotype displaying a severely malformed skeletal system. Conversely, transgenic mice over-expressing noggin in mature osteoblasts display impaired osteoblastic differentiation, reduced bone formation, and severe osteoporosis. Recombinant Murine Noggin is a 46.4 kDa disulfide-linked homodimer consisting of two 206 amino acid polypeptide chains.

Description: Encoded by the ob (obese) gene, Leptin is an adipose-derived cytokine that suppresses appetite and increases thermogenesis. Leptin exerts its anorectic effect via signaling through a hypothalamic receptor termed OB-R. Leptin has been shown to reduce body weight, food consumption, and plasma glucose levels in various in vivo models. Recombinant Human Leptin is a 16.0 kDa protein containing 147 amino acid residues.

Description: Encoded by the ob (obese) gene, Leptin is an adipose-derived cytokine that suppresses appetite and increases thermogenesis. Leptin exerts its anorectic effect via signaling through a hypothalamic receptor termed OB-R. Leptin has been shown to reduce body weight, food consumption, and plasma glucose levels in various in vivo models. Recombinant Murine Leptin is a 16.2 kDa protein containing 147 amino acid residues.

Description: IL-8 is a proinflammatory CXC chemokine that can signal through the CXCR1 and CXCR2 receptors. It is secreted by monocytes and endothelial cells. IL-8 chemoattracts and activates neutrophils. Recombinant Human IL-8 (monocyte-derived) is an 8.4 kDa protein containing 72 amino acid residues.

Description: IL-9 is an immunoregulatory cytokine produced by IL-2 activated Th2 lymphocytes. IL-9 enhances the proliferation of T lymphocytes, mast cells, erythroid precursor cells and megakaryoblastic leukemia cell lines. Over-expression of IL-9 has been implicated in the pathogenesis of anaplastic lymphoma and Hodgkin’s disease. Whereas murine IL-9 can function on human cells, human IL-9 is inactive on mouse cells. Recombinant Human IL-9 is a 14.0 kDa protein of 127 amino acid residues, including 10 cysteine residues that are fully conserved between the human and murine proteins.

Description: IL-2 is a powerful immunoregulatory lymphokine produced by T-cells in response to antigenic or mitogenic stimulation. IL-2/IL-2R signaling is required for T-cell proliferation and other fundamental functions that are essential for the immune response. IL-2 stimulates growth and differentiation of B-cells, NK cells, lymphokine-activated killer cells, monocytes, macrophages and oligodendrocytes. Recombinant Murine IL-2 is a 17.2 kDa protein containing 148 amino acid residues.

Description: IL-6 is a pleiotropic cytokine that plays an important role in host defense by regulating immune and inflammatory responses. Produced by T cells, monocytes, fibroblasts, endothelial cells and keratinocytes, IL-6 has diverse biological functions. It stimulates B cell differentiation and antibody production, synergizes with IL-3 in megakaryocyte development and platelet production, induces expression of hepatic acute-phase proteins, and regulates bone metabolism. IL-6 signals through the IL-6 receptor system that consists of two chains, IL-6Rα and gp130. Murine IL-6 is inactive on human cells, while both human and murine are equally active on murine cells. Recombinant Murine IL-6 is a 21.7 kDa protein containing 188 amino acid residues.

Description: Defensins (α and β) are cationic peptides with a broad spectrum of antimicrobial activity that comprise an important arm of the innate immune system. The α-defensins are distinguished from the β-defensins by the pairing of their three disulfide bonds. To date, six human β-defensins have been identified; BD-1, BD-2, BD-3, BD-4, BD-5 and BD-6. β-defensins are expressed on some leukocytes and at epithelial surfaces. In addition to their direct antimicrobial activities, they can act as chemoattractants towards immature dendritic cells and memory T cells. The β-defensin proteins are expressed as the C-terminal portion of precursors, and are released by proteolytic cleavage of a signal sequence and, in some cases, a propeptide sequence. β-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds. Recombinant Human BD-5 is a 5.8 kDa protein containing 51 amino acid residues.

Description: IL-2 is a powerful immunoregulatory lymphokine produced by T-cells in response to antigenic or mitogenic stimulation. IL-2/IL-2R signaling is required for T-cell proliferation and other fundamental functions that are essential for the immune response. IL-2 stimulates growth and differentiation of B-cells, NK cells, lymphokine-activated killer cells, monocytes, macrophages and oligodendrocytes. Recombinant Rat IL-2 is a 15.3 kDa protein containing 134 amino acid residues.

Description: FGF-9 is a heparin-binding growth factor that belongs to the FGF family. Proteins of this family play a central role during prenatal development, postnatal growth and regeneration of a variety of tissues, by promoting cellular proliferation and differentiation. FGF-9 targets glial cells, astrocytes cells and other cells that express FGFR 1c, 2c, 3b, 3c, and 4. Recombinant Human FGF-9 is a 23.2 kDa protein consisting of 206 amino acid residues.

Description: FGF-8 (FGF-8b) is a heparin-binding growth factor belonging to the FGF family. Proteins of this family play a central role during prenatal development, postnatal growth and regeneration of a variety of tissues, by promoting cellular proliferation and differentiation. There are 4 known alternate spliced forms of FGF8; FGF-8A, FGF-8B, FGF-8E and FGF-8F. The human and murine FGF-8A and B are identical, unlike human and mouse FGF-8E and F, which are 98% identical. FGF-8 targets mammary carcinoma cells and other cells expressing the FGF receptors. Recombinant Human/Murine FGF-8 (FGF-8b) is a 22.5 kDa protein consisting of 194 amino acid residues.

Description: FGF-4 is a heparin-binding growth factor that is a member of the FGF family. Proteins of this family play a central role during prenatal development, postnatal growth and regeneration of a variety of tissues, by promoting cellular proliferation and differentiation. FGF-4 signals through the FGFR 1c, 2c, 3c, and 4. Recombinant Human FGF-4 is a 19.7 kDa protein consisting of 182 amino acid residues.

Description: BMPs (Bone Morphogenetic Proteins) belong to the TGF-β superfamily of structurally related signaling proteins. BMP-2 is a potent osteoinductive cytokine, capable of inducing bone and cartilage formation in association with osteoconductive carriers such as collagen and synthetic hydroxyapatite. In addition to its osteogenic activity, BMP-2 plays an important role in cardiac morphogenesis, and is expressed in a variety of tissues, including lung, spleen, brain, liver, prostate, ovary, and small intestine. The functional form of BMP-2 is a 26 kDa protein composed of two identical 114 amino acid polypeptide chains linked by a single disulfide bond. Each BMP-2 monomer is expressed as the C-terminal part of a precursor polypeptide, which also contains a 23 amino acid signal sequence for secretion, and a 259 amino acid propeptide. After dimerization of this precursor, the covalent bonds between the propeptide (which is also a disulfide-linked homodimer) and the mature BMP-2 ligand are cleaved by a furin-type protease. Recombinant Human/Murine/Rat BMP-2 is a 26.0 kDa homodimeric protein consisting of two 115 amino acid polypeptide chains.

Description: IL-10 is an immunosuppressive cytokine produced by a variety of mammalian cell types including macrophages, monocytes, T cells, B cells and keratinocytes. IL-10 inhibits the expression of proinflammatory cytokines such as IL-1 and TNF-α. Like IL-4, IL-10 enhances humoral immune responses and attenuates cell-mediated immune reactions. Human IL-10 is active on murine cells, but murine IL-10 is inactive on human cells. Recombinant Human IL-10 is an 18.6 kDa protein of 161 amino acid residues.

Description: IL-11 is a multifunctional cytokine produced by stromal cells, such as fibroblasts, epithelial cells and osteoclasts. It is expressed in a wide variety of tissues, including thymus, lung, bone, connective tissue and central nervous system. IL-11 plays an important regulatory role in hematopoiesis by stimulating growth of myeloid, erythroid and megakaryocyte progenitor cells. It also regulates bone metabolism, inhibits production of proinflammatory cytokines, and protects against gastromucosal injury. Recombinant Human IL-11 is a 19.3 kDa protein consisting of 179 amino acid residues.

Description: IL-13 is an immunoregulatory cytokine produced primarily by activated Th2 cells, and also by mast cells and NK cells. Targeted deletion of IL-13 in mice resulted in impaired Th2 cell development and indicated an important role for IL-13 in the expulsion of gastrointestinal parasites. IL-13 exerts anti-inflammatory effects on monocytes and macrophages and it inhibits the expression of inflammatory cytokines such as IL-1β, TNF-α, IL-6 and IL-8. IL-13 has also been shown to enhance B cell proliferation and to induce isotype switching, resulting in increased production of IgE. Blocking of IL-13 activity inhibits the pathophysiology of asthma. Human and murine IL-13 are cross-species reactive. Recombinant Human IL-13 is a 12.6 kDa protein consisting of 115 amino acid residues.

Description: IL-21 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 IL-21 include: inducing the differentiation of T cell-stimulated B cells into plasma cells and memory B cells; the stimulation of IgG production in conjunction with IL-4; and the induction of apoptotic effects in naïve B cells and stimulated B cells in the absence of T cell signaling. Additionally, IL-21 promotes the anti-tumor activity of CD8+ T-cells and NK cells. IL-21 exerts its effect through binding to a specific type I cytokine receptor, IL-21R, which also contains the γ chain (γc) found in other cytokine receptors, including IL-2, IL-4, IL-7, IL-9 and IL-15. The IL-21/IL-21R 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. Recombinant Human IL-21 is a 15.4 kDa protein consisting of 132 amino acid residues.

Description: IL-22 is a member of the IL-10 family of regulatory cytokines, which includes IL-10, IL-19, IL-20, IL-22, IL-24 and IL-26. Members of this family share partial homology in their amino acid sequences, but they are dissimilar in their biological functions. Produced by T lymphocytes, IL-22 inhibits IL-4 production by Th2 cells, and induces acute phase reactants in the liver and pancreas. IL-22 signals through a receptor system consisting of IL-10Rβ/CRF2-4 and IL-22R, both of which are members of the class II cytokine-receptor family. Recombinant Human IL-22 is a 33.6 kDa, non-disulfide-linked, homodimeric protein consisting of two 147 amino acid polypeptide chains.

Description: Human IL-33 is a proinflammatory protein that shares structural and functional characteristics with the IL-1 cytokine family. It binds and signals through the IL-1RL1/ST2 receptor, to activate NF-κB and MAP kinases. IL-33 induces production of TH2 cell related cytokines, including IL-4, IL-5 and IL-13, and exerts multiple inflammation related bioactivities. Recombinant Human IL-33 is a 17.9 kDa protein containing 159 amino acid residues.

Description: The IL-1 family is comprised of 11 structurally related ligands, including recently re-named IL-37 (IL-1F7), which acts as a modulator of the immune response. Reduction of IL-37 synthesis in PBMCs leads to increased production of proinflammatory cytokines including IL-1 alpha, IL-1 beta, IL-6 and TNF- alpha. The role of IL-37 as an inhibitor of the innate inflammatory response is also corroborated by the observation that it is highly expressed in synovial tissue from patients with rheumatoid arthritis. Full length IL-37 resides primarily in the cytoplasm, but after activation through cleavage by CASP1, it can translocate to the nucleus where it exerts its activity by direct interaction with SMAD3. Recombinant Human IL-37 is a 19.4 kDa protein consisting of 174 amino acids, corresponding to the mature activated form of IL-37.

Description: IL-10 is an immunosuppressive cytokine produced by a variety of mammalian cell types including macrophages, monocytes, T cells, B cells and keratinocytes. IL-10 inhibits the expression of proinflammatory cytokines such as IL-1 and TNF-α. Like IL-4, IL-10 enhances humoral immune responses and attenuates cell-mediated immune reactions. Human IL-10 is active on murine cells, but murine IL-10 is inactive on human cells. Recombinant Murine IL-10 is an 18.7 kDa protein of 161 amino acid residues.

Description: IL-22 is a member of the IL-10 family of regulatory cytokines, which includes IL-10, IL-19, IL-20, IL-22, IL-24 and IL-26. Members of this family share partial homology in their amino acid sequences, but they are dissimilar in their biological functions. Produced by T lymphocytes, IL-22 inhibits IL-4 production by Th2 cells, and induces acute phase reactants in the liver and pancreas. IL-22 signals through a receptor system consisting of IL-10Rβ/CRF2-4 and IL-22R, both of which are members ofthe class II cytokine-receptor family. Recombinant Murine IL-22 is a 33.4 kDa, non-disulfide-linked, homodimeric protein consisting of two 147 amino acid polypeptide chains.

Description: G-CSF is a hematopoietic growth factor that stimulates the development of committed progenitor cells to neutrophils and enhances the functional activities of the mature end-cell. It is produced in response to specific stimulation by a variety of cells, including macrophages, fibroblasts, endothelial cells and bone marrow stroma. G-CSF is being used clinically to facilitate hematopoietic recovery after bone marrow transplantation. Human and murine G-CSF is cross-species reactive. Recombinant Murine G-CSF is a 19.0 kDa protein consisting of 179 amino acid residues.