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FGF1/AFGF [B3]
Description Fibroblast growth factor-1 (FGF1), also designated acidic FGF, and fibroblast growth factor-2 (FGF2), also designated basic FGF, are members of a family of growth factors that stimulate proliferation of cells of mesenchymal, epithe-lial and neuroectodermal origin. Additional members of the FGF family include the oncogenes FGF3 (Int2) and FGF4 (hst/Kaposi), FGF5, FGF6, FGF7 (KGF), FGF8 (AIGF), FGF9 (GAF) and FGF10-FGF23. Members of the FGF family share 30-55% amino acid sequence identity and similar gene structure, and are capable of transforming cultured cells when overexpressed in transfected cells. Cellular receptors for FGFs are members of a second multigene family including four tyrosine kinases, designated Flg (FGFR-1), Bek (FGFR-L), TKF and FGFR-3. (Shipping Cost: €200.00) Host Mouse Application ELISA, Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human -
FGF2/BFGF [C2]
Description Fibroblast growth factor-1 (FGF1), also designated acidic FGF, and fibroblast growth factor-2 (FGF2), also designated basic FGF, are members of a family of growth factors that stimulate proliferation of cells of mesenchymal, epithe-lial and neuroectodermal origin. Additional members of the FGF family include the oncogenes FGF3 (Int2) and FGF4 (hst/Kaposi), FGF5, FGF6, FGF7 (KGF), FGF8 (AIGF), FGF9 (GAF) and FGF10-FGF23. Members of the FGF family share 30-55% amino acid sequence identity and similar gene structure, and are capable of transforming cultured cells when overexpressed in transfected cells. Cellular receptors for FGFs are members of a second multigene family including four tyrosine kinases, designated Flg (FGFR-1), Bek (FGFR-L), TKF and FGFR-3. (Shipping Cost: €200.00) Host Mouse Application ELISA, Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human, Mouse, Rat -
FGF2/BFGF [C2]
Description Fibroblast growth factor-1 (FGF1), also designated acidic FGF, and fibroblast growth factor-2 (FGF2), also designated basic FGF, are members of a family of growth factors that stimulate proliferation of cells of mesenchymal, epithe-lial and neuroectodermal origin. Additional members of the FGF family include the oncogenes FGF3 (Int2) and FGF4 (hst/Kaposi), FGF5, FGF6, FGF7 (KGF), FGF8 (AIGF), FGF9 (GAF) and FGF10-FGF23. Members of the FGF family share 30-55% amino acid sequence identity and similar gene structure, and are capable of transforming cultured cells when overexpressed in transfected cells. Cellular receptors for FGFs are members of a second multigene family including four tyrosine kinases, designated Flg (FGFR-1), Bek (FGFR-L), TKF and FGFR-3. (Shipping Cost: €200.00) Host Mouse Application ELISA, Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human, Mouse, Rat -
Fibrinogen [4F7]
Description Fibrinogen is the main protein of blood coagulation system. It is a large protein and it consists of two identical subunits that contain three polypeptide chains: alpha, beta and gamma. All chains are connected with each other by a number of disulfide bonds. Fibrinopeptides A (1 to 16 amino acids) and B (1 to 17 amino acids) are released by thrombin from the N terminal parts of alpha and beta chains, respectively. In this way fibrinogen is converted into fibrin, which by means of polymerization forms a fibrin clot. Fibrinogen clotting underlies pathogenesis of MI, thromboembolism and thromboses of arteries and veins, since fibrin is the main substrate for thrombus formation. Fibrinogen activation is also involved in pathogenesis of inflammation, tumor growth and many other diseases. The normal fibrinogen concentration in plasma is about 3 mg/ml. The elevated level of fibrinogen in patient's blood is regarded as an independent risk factor for cardiovascular diseases. An increase in bloo Host Mouse Application Immunofluorescence (IF), Immunohistochemistry (IHC) Reactivity Human -
Fibromodulin/FMOD [H11]
Description Small leucine-rich proteoglycans (SLRPs), such as Decorin, Biglycan, Fibromodulin and Lumican, mediate extracellular matrix organization and are binding partners of TGFβ. Fibromodulin is a collagen-binding Keratan sulphate proteoglycan that influences adhesion processes of connective tissue and plays a role in fibrillogenesis by regulating collagen fibril spacing and thickness. The core proteins of SLRPs consist of a central region of leucine-rich repeats flanked by disulfide-linkages of the terminal domains. Fibromodulin is a ubiquitous protein that is most prominent in articular cartilage, tendon and ligament. The human Fibromodulin gene maps to chromosome 1q32.1 and encodes a 376 amino acid protein. (Shipping Cost: €200.00) Host Mouse Application ELISA, Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human, Mouse, Rat -
Fibronectin [HFN7.1]
Description Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization. Participates in the regulation of type I collagen deposition by osteoblasts. Anastellin binds fibronectin and induces fibril formation. This fibronectin polymer, named superfibronectin, exhibits enhanced adhesive properties. Both anastellin and superfibronectin inhibit tumor growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and inhibits lysophospholipid signaling. (Shipping Cost: €200.00) Host Mouse Application Flow cytometry (FC), Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC) Reactivity Human -
Fibronectin [HFN7.1]
Description Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization. Participates in the regulation of type I collagen deposition by osteoblasts. Anastellin binds fibronectin and induces fibril formation. This fibronectin polymer, named superfibronectin, exhibits enhanced adhesive properties. Both anastellin and superfibronectin inhibit tumor growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and inhibits lysophospholipid signaling. (Shipping Cost: €200.00) Host Mouse Application Flow cytometry (FC), Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC) Reactivity Human -
Filamin A/Filamin 1 [E3]
Description Caldesmon, Filamin A (or Filamin 1), Nebulin and Villin are differentially expressed and regulated actin binding proteins. Both muscular (CDh) and non-muscular (CDl) forms of Caldesmon have been identified and each has been shown to bind to Actin as well as to calmodulin and Myosin. CDh is expressed predominantly on thin filaments in smooth muscle, whereas CDl is widely expressed in nonmuscle tissues and cells. Filamin A functions as a crosslinking protein forming a flexible link between two actin filaments. It is composed of two identical polypeptide chains each joined to the other at one end, with an actin binding site at the other. It is present in human platelets, lymphocytes, fibroblasts and smooth muscle actin. Nebulin is a large filamentous protein specific to muscle tissue that may function as a ruler for filament length. Several isoforms of Nebulin are produced by alternative exon usage. Villin is Ca2+-regulated and is the major structural component of the brush border of abso Host Mouse Application Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human, Mouse, Rat -
Filamin A/Filamin 1 [E3]
Description Caldesmon, Filamin A (or Filamin 1), Nebulin and Villin are differentially expressed and regulated actin binding proteins. Both muscular (CDh) and non-muscular (CDl) forms of Caldesmon have been identified and each has been shown to bind to Actin as well as to calmodulin and Myosin. CDh is expressed predominantly on thin filaments in smooth muscle, whereas CDl is widely expressed in nonmuscle tissues and cells. Filamin A functions as a crosslinking protein forming a flexible link between two actin filaments. It is composed of two identical polypeptide chains each joined to the other at one end, with an actin binding site at the other. It is present in human platelets, lymphocytes, fibroblasts and smooth muscle actin. Nebulin is a large filamentous protein specific to muscle tissue that may function as a ruler for filament length. Several isoforms of Nebulin are produced by alternative exon usage. Villin is Ca2+-regulated and is the major structural component of the brush border of abso Host Mouse Application Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human, Mouse, Rat -
FLI-1 [G146-22]
Description The FLI-1 gene and FLI-1 protein are best known for their critical role in the pathogenesis of ES/PNET. More than 85% of ES/PNET are characterized by the translocation t(11;22)(q24;q12) that results in the fusion of the ews gene on chromosome 22 to the FLI-1 gene on chromosome 11. FLI-1 is a member of the ETS (erythroblastosis virus-associated transforming sequences) family of DNA-binding transcription factors and is involved in cellular proliferation and tumorigen esis. FLI-1 is normally expressed in endothelial cells and in hematopoietic cells, including T lymphocytes. The immunohistochemical detection of FLI-1 protein has been shown in two recent studies to be valuable in the discrimination of ES/PNET from most of its potential mimics, with the notable exception of lymphoblastic lymphoma. The FLI-1 gene has also recently been shown to play an important role in the embryologic development of blood vessels. FLI-1 is a highly sensitive (92%) and specific (100%) marker of both benign an Host Mouse Application Immunohistochemistry (IHC) Reactivity Human