50g

Chloroform-d, 99.8 Atom Percent D, Contains 0.05 Percent (v/v) Tetramethylsilane

Chlorothiazide

Ciliary Neurotrophic Factor (CNTF) is a cytokine belonging to the Interleukin 6 (IL-6) family, which also includes IL-6, Oncostatin M, Leukemia Inhibitory Factor (LIF), and Cardiotrophin-1. Structurally, CNTF resembles a four-helix bundle composition, similar to the other members of the IL-6 family. The receptor for CNTF is composed of three parts: a gp130-like subunit common in the IL-6 receptor family, a LIF Receptor β subunit, and a CNTF specific α receptor subunit. Upon binding to the CNTF, the β subunit of the CNTF receptor will undergo tyrosine phosphorylation, and activate the intracellular JAK/STAT pathway. The main function of CNTF in vivo is to promote the differentiation and survival of a variety of neurons and glial cells, including sympathetic precursor cells and spinal motor neurons.

Ciliary neurotrophic factor (CNTF) is a polypeptide hormone whose actions appear to be restricted to the nervous system where it promotes neurotransmitter synthesis and neurite outgrowth in certain neuronal populations. CNTF was initially identified as a trophic factor for embryonic chick ciliary parasympathetic neurons in culture. Furthermore, the protein is also a potent survival factor for neurons and oligodendrocytes and may be relevant in reducing tissue destruction during inflammatory attacks. In addition, CNTF is useful for treatment of motor neuron disease and it could reduce food intake without causing hunger or stress. Recombinant murine CNTF containing 198 amino acids and it shares 82 % and 95 % a.a. sequence identity with human and rat CNTF.

Ciliary Neurotrophic Factor (CNTF) is a polypeptide hormone which acts within the nervous system where it promotes neurotransmitter synthesis and neurite outgrowth in certain neuronal populations. CNTF is a potent survival factor for neurons and oligodendrocytes and may play a role in reducing tissue damage during increased inflammation. A mutation in this gene, which results in aberrant splicing, leads to ciliary neurotrophic factor deficiency, however this phenotype is not causally related to neurologic disease.

Cytotoxic T lymphocyte-associated molecule-4 (CTLA-4) is a cell surface molecule that is closely related to CD28, and a powerful negative regulator of T cell activation. Structurally, CTLA-4 is a member of the Ig superfamily, having a single extracellular V-like domain , homology with CD28; The overall sequence homology between CD28 and CTLA-4 is about 20%, but they share a 27% (murine) to 31% (human) identity at the amino acid level. Inhibitory receptor acting as a major negative regulator of T-cell responses. The affinity of CTLA-4 for its natural B7 family ligands, CD80 and CD86, is considerably stronger than the affinity of their cognate stimulatory coreceptor CD28.

CTLA-4 (Cytotoxic T-Lymphocyte Antigen 4) is also known as CD152, is an Inhibitory receptor acting as a major negative regulator of T-cell responses. CTLA-4 is a member of the immunoglobulin superfamily, which is expressed on the surface of T cells and transmits an inhibitory signal to T cells. CTLA-4 and CD28 are homologous receptors expressed by both CD4+ and CD8+ T cells, which mediate opposing functions in T-cell activation. Both receptors share a pair of ligands expressed on the surface of antigen-presenting cells (APCs). The affinity of CTLA-4 for its natural B7 family ligands, CD80 and CD86, is considerably stronger than the affinity of their cognate stimulatory co-receptor CD28.

D-Xylose

Dimethyl Sulfoxide-d6, 99.9 Atom Percent D

Dimethyl Sulfoxide-d6, 99.9 Atom Percent D, Contains 0.05 Percent TMS

Dickkopf related protein 1 (DKK-1) is a chemokine that belongs to the DKK protein family, which also includes DKK-2, DKK-3 and DKK-4. DKK-1 was originally identified as a Xenopus head forming molecule that behaves as an antagonist for Wnt signaling. It is one of the most up-regulated genes during androgen-potentiated balding, with DKK-1 messenger RNA up-regulated a few hours after DHT treatment of hair follicles at the dermal papilla in vitro. Neutralizing bodies against DKK-1 reverses DHT effects on outer root sheath keratinocytes. DKK-1 expression is attenuated by L-threonate, a metabolite of ascorbate in vitro. DKK-1 promotes LRP6 internalization and degradation as it forms a ternary complex with the cell surface receptor Kremen. DKK-1 not only functions as a head inducer during development, but also regulates joint remodeling and bone formation, which indicate sits role in the pathogenesis of rheumatoid arthritis and multiple myeloma.

Dickkopf related protein 1 (DKK-1) is a chemokine that belongs to the DKK protein family, which also includes DKK-2, DKK-3 and DKK-4. DKK-1 was originally identified as a Xenopus head forming molecule that behaves as an antagonist for Wnt signaling. It is one of the most up-regulated genes during androgen-potentiated balding, with DKK-1 messenger RNA up-regulated a few hours after DHT treatment of hair follicles at the dermal papilla in vitro. Neutralizing bodies against DKK-1 reverses DHT effects on outer root sheath keratinocytes. DKK-1 expression is attenuated by L-threonate, a metabolite of ascorbate in vitro. DKK-1 promotes LRP6 internalization and degradation as it forms a ternary complex with the cell surface receptor Kremen. DKK-1 not only functions in head formation during development, but also regulates joint remodeling and bone formation indicating its potential role in the pathogenesis of rheumatoid arthritis and multiple myeloma.

DNAM-1 (DNAX accessory molecule-1), also known as CD226, platelet and T cell activation antigen 1 (PTA1) and TLiSA1, is a member of the Ig superfamily containing two Ig-like domains of the V set and is encoded by a gene on human chromosome 18q22.3. DNAM-1 is an activating receptor expressed on natural killer (NK) cells, CD8+ T cells, and other immune cells. Upon recognition of its ligands, CD155 and CD112, DNAM-1 promotes NK cell–mediated elimination of transformed and virus-infected cells. It also has a key role in expansion and maintenance of virus-specific memory NK cells. DNAM-1 is the cell surface receptor of NECTIN2. Upon ligand binding, it stimulates T cell proliferation and cytokine production, including that of IL2, IL5, IL10, IL13 and IFNG.

CD226 (Cluster of Differentiation 226), also known as PTA1 (outdated term, ‘platelet and T cell activation antigen 1’)[5] or DNAM-1 (DNAX Accessory Molecule-1), is a ~65 kDa glycoprotein expressed on the surface of natural killer cells, platelets, monocytes and a subset of T cells. It is a member of the immunoglobulin superfamily. This protein is involved in intercellular adhesion, lymphocyte signaling, cytotoxicity and lymphokine secretion mediated by cytotoxic T-lymphocyte (CTL) and NK cell. It is the cell surface receptor for NECTIN2 and its main ligands are CD112 and CD155. It stimulates T-cell proliferation and cytokine production, including that of IL-2, IL-5, IL-10, IL-13, and IFNγ upon ligand binding.

Epidermal Growth Factor (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 the EGF receptor (EGFR) also known as erbB1, is a class I tyrosine kinase receptor. This receptor also binds with TGF-α and VGF (vaccinia virus growth factor). EGF-receptor binding results in cellular proliferation, differentiation, and survival. EGF is a low-molecular-weight polypeptide first purified from the mouse submandibular gland, but since then found in many human tissues including submandibular gland, parotid gland. Salivary EGF, which seems also regulated by dietary inorganic iodine, also plays an important physiological role in the maintenance of oro-esophageal and gastric tissue integrity. The biological effects of salivary EGF include healing of oral and gastroesophageal ulcers, inhibition of gastric acid secretion, stimulation of DNA synthesis as well as mucosal protection from intraluminal injurious factors such as gastric acid, bile acids, pepsin, and trypsin and to physical, chemical and bacterial agents.

EGF Receptor, also known as ERBB, ERBB1 and HER1, is a type I transmembrane protein belonging to the tyrosine protein kinase family. It belongs to a family of tyrosine kinase receptors including Human EGF Receptors (HER) 2, 3, and 4 which all play important roles in cell growth and differentiation. Their primary ligands are EGF, Heparin-Binding EGF and Transforming Growth Factor α. Upon ligand binding, EGFR undergoes asymmetric dimerization, composed of an “activator” and a “receiver”. EGFR and its family members are disregulated in numerous cancers. In particular, EGFR is overexpressed in many epithelial solid tumors. Evidence suggests EGFR is an excellent target for pharmacologic intervention in Non Small Cell Lung Cancer (NSCLC) due to its high level of expression and prominent role in tumor growth and metastasis.

Epidermal Growth Factor (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 the EGF receptor (EGFR) also known as erbB1, is a class I tyrosine kinase receptor. This receptor also binds with TGF-α and VGF (vaccinia virus growth factor). EGF-receptor binding results in cellular proliferation, differentiation, and survival. EGF is a low-molecular-weight polypeptide first purified from the mouse submandibular gland, but since then found in many human tissues including submandibular gland, parotid gland. Salivary EGF, which seems also regulated by dietary inorganic iodine, also plays an important physiological role in the maintenance of oro-esophageal and gastric tissue integrity. The biological effects of salivary EGF include healing of oral and gastroesophageal ulcers, inhibition of gastric acid secretion, stimulation of DNA synthesis as well as mucosal protection from intraluminal injurious factors such as gastric acid, bile acids, pepsin, and trypsin and to physical, chemical and bacterial agents.

Epidermal Growth Factor (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 the EGF receptor (EGFR) also known as erbB1, is a class I tyrosine kinase receptor. This receptor also binds with TGF-α and VGF (vaccinia virus growth factor). EGF-receptor binding results in cellular proliferation, differentiation, and survival. EGF is a low-molecular-weight polypeptide first purified from the mouse submandibular gland, but since then found in many human tissues including submandibular gland, parotid gland. Salivary EGF, which seems also regulated by dietary inorganic iodine, also plays an important physiological role in the maintenance of oro-esophageal and gastric tissue integrity. The biological effects of salivary EGF include healing of oral and gastroesophageal ulcers, inhibition of gastric acid secretion, stimulation of DNA synthesis as well as mucosal protection from intraluminal injurious factors such as gastric acid, bile acids, pepsin, and trypsin and to physical, chemical and bacterial agents.

Epidermal Growth Factor (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 the EGF receptor (EGFR) also known as erbB1, is a class I tyrosine kinase receptor. This receptor also binds with TGF-α and VGF (vaccinia virus growth factor). EGF-receptor binding results in cellular proliferation, differentiation, and survival. EGF is a low-molecular-weight polypeptide first purified from the mouse submandibular gland, but since then found in many human tissues including submandibular gland, parotid gland. Salivary EGF, which seems also regulated by dietary inorganic iodine, also plays an important physiological role in the maintenance of oro-esophageal and gastric tissue integrity. The biological effects of salivary EGF include healing of oral and gastroesophageal ulcers, inhibition of gastric acid secretion, stimulation of DNA synthesis as well as mucosal protection from intraluminal injurious factors such as gastric acid, bile acids, pepsin, and trypsin and to physical, chemical and bacterial agents.

Epidermal Growth Factor (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 the EGF receptor (EGFR) also known as erbB1, is a class I tyrosine kinase receptor. This receptor also binds with TGF-α and VGF (vaccinia virus growth factor). EGF-receptor binding results in cellular proliferation, differentiation, and survival. EGF is a low-molecular-weight polypeptide first purified from the mouse submandibular gland, but since then found in many human tissues including submandibular gland, parotid gland. Salivary EGF, which seems also regulated by dietary inorganic iodine, also plays an important physiological role in the maintenance of oro-esophageal and gastric tissue integrity. The biological effects of salivary EGF include healing of oral and gastroesophageal ulcers, inhibition of gastric acid secretion, stimulation of DNA synthesis as well as mucosal protection from intraluminal injurious factors such as gastric acid, bile acids, pepsin, and trypsin and to physical, chemical and bacterial agents.

Enterokinase (EK) is an enzyme produced by cells of the duodenum and involved in human digestion. It plays a role of turning trypsinogen to its active form trypsin, and indirectly activates the pancreatic digestive enzymes. Enterokinase is a specific protease that cleaves after a lysine preceded by four aspartic acids: Asp-Asp-Asp-Asp-Lys(DDDDK↑). Enterokinase will not work if the recognition site is followed by a proline. rbEKhas the highest activity than EK of other species and is used wildly in biochemical applications. rbEK with 6 × His-tag binds with Ni2+ affinity chromatography and was designed for removing from digestion system.

Recombinant Bovine Enterokinase (His-tagged) (rbEK) as the light chain is a single glycosylated polypeptide chain containing 200 amino acids, 6 × His at C-terminus. A fully biologically active molecule, rbEK has a molecular mass of 40 kDa and is obtained by proprietary chromatographic techniques at GenScript.

Erythropoietin (EPO), a glycoprotein produced primarily by the kidney, is the principal factor that regulates erythropoiesis by stimulating the proliferation and differentiation of erythroid progenitor cells. The production of EPO by kidney cells is increased in response to hypoxia or anemia. Recombinant EPO has been approved for the treatment of anemia associated with chronic renal failure as well as for anemia of AZT treated AIDS patients.The cDNAs for EPO have been cloned from human, mouse, canine, etc. The mature proteins from the various species are highly conserved, exhibiting greater than 80% sequence identity at the amino acid level. Human EPO cDNA encodes a 193 amino acid residue precursor protein that is processed to yield a 165 amino acid residue mature protein. EPO contains one O-linked and three N-linked glycosylation sites. Glycosylation of EPO is required for EPO biological activities in vivo. EPO exhibits structural as well as amino sequence identity to the amino terminal 153 amino acid region of thrombopoietin.

Fibroblast Growth Factor-10 (FGF-10) is a mitogen mainly produced by mesenchymal stem cells in the lung. FGF-10 belongs to the heparin binding FGF family, and is also known as Keratinocyte Growth Factor-2 (KGF-2). It shares homology with KGF and receptor binding to FGFR2-IIIb. However, while KGF induces proliferation and differentiation of various epithelial cells, FGF-10 promotes budding and branching morphogenesis during the multi-organ development via mesenchymal-epithelial cell interactions. FGF-10 is critical for lung and limb development, and is regulated by Shh during early development.

Fibroblast Growth Factor-10 (FGF-10) is a mitogen mainly produced by mesenchymal stem cells in lung. FGF-10 belongs to the heparin binding FGF family, and is also known as Keratinocyte Growth Factor-2 (KGF-2). It shares homology with KGF, and both KGF and FGF-10 activate the receptor FGFR2-IIIb. However, unlike KGF, which induces the proliferation and differentiation of various epithelial cells, FGF-10 is an essential factor for the budding and branching morphogenesis during multi-organ development via mesenchymal-epithelial interactions. FGF-10 is crucial for lung and limb development and is regulated by Shh during early development.

Fibroblast Growth Factor-16 (FGF-16) is a heparin binding growth factor, a member of the FGF family. All FGF family members are heparin­binding growth factors with a core 120 amino acid (aa) FGF domain that allows for a common tertiary structure. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. The rat homolog is predominantly expressed in embryonic brown adipose tissue and has significant mitogenic activity, which suggests a role in proliferation of embryonic brown adipose tissue. FGF-16 is most similar to FGF-9 (73 % amino acid identity). The protein sequence of human FGF-16 displays 98.6% identity with rat FGF-16. Chimpanzee FGF-16 (207 amino acids), chicken FGF-16 (207 amino acids), and zebrafish FGF-16 (203 amino acids) show 100 %, 89.9 %, and 79.2 % total amino acid identity with human FGF-16.

Fibroblast Growth Factor-18 (FGF-18) is a heparin-binding growth factor that is a member of the FGF family. FGF-18 signals through FGFR 1c, 2c, 3c, and 4. FGF-18 plays an important role in the regulation of cell proliferation, cell differentiation and cell migration. FGF-18 is required for normal ossification and bone development. It can also stimulate hepatic and intestinal proliferation.

Fibroblast Growth Factor 18 (FGF-18) is a pleiotropic cytokine belonging to the heparin-binding FGF family, which has 23 different members. Structurally, FGF-18 is closely related to FGF-8 and FGF-17. Like other FGFs, FGF-18 can bind to different FGF receptors in vivo. FGF-18 is expressed in various tissues and has multiple functions: during long bone growth, FGF-18 is expressed in perichondrium and developing joints, and regulates bone formation by inhibiting chondrocyte proliferation and differentiation; FGF-18 knock-out mice survive embryonic development, but exhibit skeletal abnormalities and die in the early neonatal period. FGF-18 also induces ectopic cartilage formation in the lung, and alters the morphology of the pulmonary mesenchyma.

FGF-21, also known as fibroblast growth factor-21 and FGFL, is a secreted growth factor belonging to theheparin-binding growth factor family. It is produced by hepatocytes in response to fatty acid stimulation. FGF-21 couples with its co-factor beta-Klotho to signal through FGFR1c and FGFR4. Signal transduction results in insulin-independent uptake of glucose by adipocytes. Clinical administration of FGF-21 induces energy expenditure, fat utilization and lipid excretion.

Fibroblast Growth Factor-21 (FGF-21) is a metabolic cytokine belonging to the heparin-binding FGF family. Along with FGF-19/15 and FGF-23, FGF-21 is categorized as a member of the atypical FGF subfamily, as it must be complexed to the Klotho co-receptor in order to bind to the FGF receptors and activate the downstream signaling pathway. In vivo FGF-21 is expressed in liver, pancreas, adipose tissue, and skeletal muscle, and it plays a central role in the energy metabolism. The expression of FGF-21 is stimulated by free fatty acids and insulin resistant states and is correlated with whole-body insulin resistance. FGF-21 activates glucose uptake in adipocytes and increases insulin sensitivity, implicating it as a novel target with potential anti-diabetic properties.

Fibroblast growth factor-21 (FGF21) belongs to the large FGF family which has at least 23 members. Along with FGF-19/15 and FGF-23, FGF-21 is categorized as a member of the atypical FGF subfamily, as it must be complexed to the Klotho co-receptor in order to bind to the FGF receptors and activate the downstream signaling pathway. FGF family members possess broad mitogenic and cell survival activities and are involved in a variety of biological processes including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion.

Fibroblast Growth Factor-6 (FGF-6) is a cytokine belonging to the heparin-binding FGF family, and is structurally related to other members of FGF family, particularly FGF-4. In vivo, FGF-6 exhibits an expression profile predominantly restricted tothe myogenic lineage, and it preferentially binds to two of the FGF receptors: FGFR1 and FGFR4. FGF-6 functions in muscle regeneration, myoblast proliferation and migration, and muscle differentiation in a dose-dependent manner. In vivo high concentration of recombinant FGF-6 up-regulates and down-regulates FGFR1 and FGFR4, respectively, as FGFR1 promotes the proliferation while FGFR4 promotes the differentiation in the muscle. Besides its dual function in muscle regeneration, FGF-6 may act as a regulator of bone metabolism as well.

Fibroblast Growth Factor-8 (FGF-8) is a heparin-binding growth factor of the FGF family. There are 4 known forms of FGF8 produced by alternative splicing: FGF8a, FGF-8b, FGF-8e and FGF-8f. The human and mouse FGF8b are identical of aa sequences. FGF-8 plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation and cell migration. FGF-8 is required for normal brain, eye, ear and limb development during embryogenesis. It is also required for normal development of the gonadotropin- releasing hormone (GnRH) neuronal system.

Fibroblast Growth Factor 8a (FGF-8a) is a cytokine belonging to the heparin-binding FGF family, which has at least 23 members. FGF-8 has 8 different isoforms, named FGF-8a through FGF-8h. Different FGF-8 isoforms have different affinities to the receptors, and thus participate in different signaling cascade pathways. FGF-8 has very widespread expression during embryonic development, and is an organizer and inducer for gastrulation, somitogenesis, morphogenesis, and limb induction. However, FGF-8 is also a potential oncogene: in normal adult cells, FGF-8 has very low expression, but FGF-8 is highly expressed in cancer cells of breast, prostate, and ovarian tumors. FGF-8 promotes tumor angiogenesis by increasing neovascularization, and induces osteoblastic differentiation.

Fibroblast Growth Factor 8e (FGF-8e) is a cytokine belonging to the heparin-binding FGF family, which has at least 23 members. FGF-8 has 8 different isoforms, named FGF-8a through FGF-8h. Different FGF-8 isoforms have different receptor affinities, and thus participate in different signaling cascade pathways. FGF-8 has widespread expression during embryonic development, promoting gastrulation, somitogenesis, morphogenesis, and limb formation. FGF-8 also has oncogenic potential. While in normal cells FGF-8 is expressed at very low levels, in breast, prostate and ovarian cancer FGF-8 is highly expressed.FGF-8 promotes tumor angiogenesis by increasing neovascularization, and inducing osteoblastic differentiation.

Fibroblast Growth Factor-9 (FGF-9) is a heparin binding growth factor that belongs to the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF-9 was isolated as a secreted factor that exhibits a growth-stimulating effect on cultured glial cells. In nervous system, this protein is produced mainly by neurons and may be important for glial cell development.

Fibroblast Growth Factor- acidic (FGF-acidic), also known as FGF-1 and endothelial cell growth factor, is a member of the FGF family which currently contain 23 members. FGF acidic and basic, unlike the other members of the family, lack signal peptides and are apparently secreted by mechanisms other than the classical protein secretion pathway. FGF acidic has been detected in large amounts in the brain. Other cells known to express FGF acidic include hepatocytes, vascular smooth muscle cells, CNS neurons, skeletal muscle cells, fibroblasts, keratinocytes, endothelial cells, intestinal columnar epithelium cells and pituitary basophils and acidophils. As with other FGF’s, FGF acidic exhibits considerable species cross reactivity. FGF acidic and FGF basic stimulate the proliferation of all cells of mesodermal origin, and many cells of neuroectodermal, ectodermal and endodermal origin.

Fibroblast Growth Factor- acidic (FGF-acidic) is a mitogen targeting at the endothelial cells, and belongs to the heparin binding FGF family, which contains 22 members. FGF-acidic binds to the receptor family FGFR1-4 in vivo with the assistance of heparin. However, along with FGF -basic, FGF-acidic lacks the signal peptide segment, and thus is not secreted via endoplasmic reticulum (ER) and Golgi bodies. Studies have shown that FGF-acidic is highly regulated, and it is a direct angiogenesis factor. If unregulated, angiogenesis could contribute to several diseases including arthritis, diabetes, ocular neovascularization, and especially tumors. Therefore, FGF-acidic is treated as a potential oncogene, and its overexpression is correlated tightly with several cancers.

Fibroblast Growth Factor-basic (FGF-basic), also known as FGF-2, is a pleiotropic cytokine and one of the prototypic members of the heparin-binding FGF family. Like other FGF family members, FGF-basic has the β trefoil structure. In vivo, FGF-basic is produced by a variety of cells, including cardiomycotes, fibroblasts, and vascular cells. FGF-basic regulates a variety of processes including cell proliferation, differentiation, survival, adhesion, motility, apoptosis, limb formation and wound healing. FGF-basic can be tumorigenic due to its role in angiogenesis and blood vessel remodeling. The angiogenic effects of FGF-basic can produce beneficial cardioprotection during acute heart injury.

Fibroblast Growth Factor-basic (FGF-basic), also known as FGF-2, is a pleiotropic cytokine and one of the prototypic members of the heparin-binding FGF family. Like other FGF family members, FGF-basic has the β trefoil structure. In vivo, FGF-basic is produced by a variety of cells, including cardiomycotes, fibroblasts, and vascular cells. FGF-basic regulates a variety of processes including cell proliferation, differentiation, survival, adhesion, motility, apoptosis, limb formation and wound healing. FGF-basic can be tumorigenic due to its role in angiogenesis and blood vessel remodeling. The angiogenic effects of FGF-basic can produce beneficial cardioprotection during acute heart injury.

Fibroblast Growth Factor-basic (FGF-basic), also known as FGF-2, is a pleiotropic cytokine and one of the prototypic members of the heparin-binding FGF family. Like other FGF family members, bFGF has the β trefoil structure. In vivo, bFGF is produced by a variety of cells, including cardiomycotes, fibroblasts, and vascular cells. bFGF regulates a variety of processes including cell proliferation, differentiation, survival, adhesion, motility, apoptosis, limb formation and wound healing. bFGF can be tumorigenic due to its role in angiogenesis and blood vessel remodeling. The angiogenic effects of bFGF can produce beneficial cardioprotection during acute heart injury.

Fibroblast Growth Factor-basic (FGF-basic), also known as FGF-2, is a pleiotropic cytokine and one of the prototypic members of the heparin-binding FGF family. Like other FGF family members, FGF-basic has the β trefoil structure. In vivo, FGF-basic is produced by a variety of cells, including cardiomycotes, fibroblasts, and vascular cells. FGF-basic regulates a variety of processes including cell proliferation, differentiation, survival, adhesion, motility, apoptosis, limb formation and wound healing. FGF-basic can be tumorigenic due to its role in angiogenesis and blood vessel remodeling. The angiogenic effects of FGF-basic can produce beneficial cardioprotection during acute heart injury.

Fibroblast Growth Factor-basic (FGF-basic), also known as HBGF-2, is a non-glycosylated heparin-binding growth factor that belongs to the FGF family. FGF-basic is present in basement membranes and in the subendothelial extracellular matrix of blood vessels. FGF-basic signals through FGFR1, 2, 3 and 4 that plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration.

Fibroblast Growth Factor-basic (FGF-basic), also known as FGF-2, is a pleiotropic cytokine and one of the prototypic members of the heparin-binding FGF family. Like other FGF family members, FGF-basic has the β trefoil structure. In vivo, FGF-basic is produced by a variety of cells, including cardiomycotes, fibroblasts, and vascular cells. FGF-basic regulates a variety of processes including cell proliferation, differentiation, survival, adhesion, motility, apoptosis, limb formation and wound healing. FGF-basic can be tumorigenic due to its role in angiogenesis and blood vessel remodeling. The angiogenic effects of FGF-basic can produce beneficial cardioprotection during acute heart injury.

Fibroblast growth factor receptor 2 (FGFR2) also known as CD332 is a receptor for fibroblast growth factor and it has important roles in embryonic development and tissue repair, especially bone and blood vessels. FGFR2 has two naturally occurring isoforms, FGFR2IIIb and FGFR2IIIc, created by splicing of the third immunoglobulin-like domain. FGFR2IIIb is predominantly found in ectoderm derived tissues and endothelial organ lining. Like the other members of the fibroblast growth factor receptor family, these receptors signal by binding to their ligand and dimerisation (pairing of receptors), which causes the tyrosine kinase domains to initiate a cascade of intracellular signals. On a molecular level these signals mediate cell division, growth and differentiation.

Fibroblast growth factor receptor 3(FGFR3) also known as CD333 (cluster of differentiation 333) is a member of the fibroblast growth factor receptor family, where amino acid sequence is highly conserved between members and throughout evolution. The FGFR3 gene produces various forms of the FGFR3 protein and the location varies depending on the isoform of the FGFR3 protein. Since the different forms are found within different tissues, the protein is responsible for multiple growth factor interactions. Gain of function mutations in FGFR3 inhibits chondrocyte proliferation and underlies achondroplasia and hypochondroplasia.

FGL1 (Fibrinogen-like protein 1), also known as hepatocyte-derived fibrinogen-related protein 1 (HFREP-1), HP-041, hepassocin (HPS), and liver fibrinogen-related protein 1 (LFIRE-1), is a liver-specific secreted protein belonging to the fibrinogen superfamily whose members share a fibrinogen domain at their C-termini. FGL1 is an immune suppressive molecule that inhibits the activation of antigen-specific T cells by acting as a major ligand of LAG3, and binds LAG3 independently of MHC class II.

Flt3L, also known as Fms-related tyrosine kinase 3 ligand and SL cytokine, is a single-pass type I membrane protein. It is expressed by stromal cells and T cells. Flt3L signals through tyrosine kinase receptor Flt3/Flk2 to stimulate the proliferation of early hematopoietic progenitor cells. It synergizes with other growth factors, such as GM-CSF, IL-3 and CSF, to promote the differentiation of both myeloid and lymphoid cells. Alternative splicing and proteolytic cleavage of membrane-bound Flt3L generates a soluble extracellular domain (ECD) isoform with full biological activity.

Fms-related tyrosine kinase 3 ligand (Flt3L) is growth fator stimulates the proliferation and differentiation of hematopoietic multipotent progenitors and promotes proliferation of NK cells and dendritic cell subgroups by combination with other growth factors. Flt3L is produced by T cells and stromal fibroblasts, and targeted various cells including hematopoietic stem cells, B cells, T cells, dendritic cells, and NK cells. Flt3L binds to it cognate tyrosine kinase receptor Flt3 and activates JAK/STAT signaling pathway.Flt3L is a hematopoietic four helical bundle cytokine with structurally homologous to stem cell factor (SCF) and colony stimulating facor 1 (CSF-1) demonstrated four conserved cysteines and two glycosylation sites. Flt3L naturally as a non-disulfide-linked homodimer with multiple isoforms. The extracellular portion is approximately 160 amino acid residues in length and the cytoplasmic segment is approximately 20-30 amino acid residues in length.

Granulocyte Colony-Stimulating Factor (G-CSF) contains internal disulfide bonds. Among the family of colony-stimulating factors, Granulocyte Colony Stimulating Factor (G-CSF) is the most potent inducer of terminal differentiation to granulocytes and macrophages of leukemic myeloid cell lines. The synthesis of Granulocyte Colony Stimulating Factor (G-CSF) can be induced by bacterial endotoxins, TNF, Interleukin-1 and GM-CSF. Prostaglandin E2 inhibits the synthesis of Granulocyte Colony Stimulating Factor (G-CSF). In epithelial, endothelial, and fibroblastic cells secretion of Granulocyte Colony Stimulating Factor (G-CSF) is induced by Interleukin-17.

Human Granulocyte Colony Stimulating Factor (G-CSF) contains internal disulfide bonds. Among the family of colony-stimulating factors, Granulocyte Colony Stimulating Factor (G-CSF) is the most potent inducer of terminal differentiation to granulocytes and macrophages of leukemic myeloid cell lines. The synthesis of Granulocyte Colony Stimulating Factor (G-CSF) can be induced by bacterial endotoxins, TNF, Interleukin-1 and GM-CSF. Prostaglandin E2 inhibits the synthesis of Granulocyte Colony Stimulating Factor (G-CSF). In epithelial, endothelial, and fibroblastic cells, the secretion of Granulocyte Colony Stimulating Factor (G-CSF) is induced by Interleukin-17.