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bs-0675P is one synthetic peptide derived from human FGFR2. Fibroblast growth factors (FGFs) are members of a large family of structurally related polypeptides that are potent physiological regulators of growth and differentiation for a wide variety of cells of mesodermal, ectodermal and endodermal origin. Four genes encoding for high affinity cell surface FGF receptors (FGFRs) have been identified: FGFR1, FGFR2, FGFR3 and FGFR4. FGFRs are members of the tyrosine kinase family of growth fac

KGF is a member of 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. This protein is a potent epithelial cell specific growth factor, whose mitogenic activity is predominantly exhibited in keratinocytes but not in fibroblasts and endothelial cells. Studies of mouse and

This gene encodes a serum protein found in association with the major histocompatibility complex (MHC) class I heavy chain on the surface of nearly all nucleated cells. The protein has a predominantly beta-pleated sheet structure that can form amyloid fibrils in some pathological conditions. A mutation in this gene has been shown to result in hypercatabolic hypoproteinemia.[provided by RefSeq, Sep 2009].

D-DIMER is A fibrin degradation fragment or product that is produced by the action of plasmin on fibrin in the clot dissolution process.$nHuman Gene ID : D-DIMER

The nuclear pore complex is a massive structure that extends across the nuclear envelope, forming a gateway that regulates the flow of macromolecules between the nucleus and the cytoplasm. Nucleoporins are the main components of the nuclear pore complex in eukaryotic cells. The protein encoded by this gene is a member of the FG-repeat containing nucleoporins and is localized to the nuclear pore central plug. This protein associates with the importin alpha/beta complex which is involved in the

Neuroligin 1 is a synaptic cell-adhesion molecule that is enriched in postsynaptic densities where it may recruit receptors, channels, and signal-transduction molecules to synaptic sites of cell adhesion. In addition, the neuroligin/beta-neurexin junction may be involved in the excitatory/inhibitory specification of CNS neuron synapses. A role for Neuroligin 1 is also suggested in autism.