optic

Optineurin Protein, Human, Recombinant (E. coli, His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 69.9 kDa and the accession number is Q96CV9.

Optineurin Protein, Human, Recombinant (His) is expressed in Baculovirus insect cells with C-9xHis tag. The predicted molecular weight is 68.0 kDa and the accession number is Q96CV9.

Ezrin is expressed in cerebral cortex, basal ganglia, hippocampus, hypophysis, and optic nerve. The N-terminus of ezrin contains a FERM domain which is further subdivided into three subdomains. The C-terminus contain a ERM domain. As a member of the ERM protein family, Ezrin serves as an intermediate between the plasma membrane and the actin cytoskeleton. It plays a key role in cell surface structure adhesion, migration, and organization. Ezrin probably involved in connections of major cytoskeletal structures to the plasma membrane. The N-terminal FERM domain strongly binds sodium-hydrogen exchanger regulatory factor (NHERF) proteins (involving long-range allostery). The C-terminal binds to actin, phosphatidylinositol bis-phosphate (PIP2) and membrane proteins like CD44 and ICAM-2. In epithelial cells, Ezrin is required for the formation of microvilli and membrane ruffles on the apical pole. Along with PLEKHG6, Ezrin is required for normal macropinocytosis.

Calcium/calmodulin-dependent myosin light chain kinase implicated in smooth muscle contraction via phosphorylation of myosin light chains (MLC). Also regulates actin-myosin interaction through a non-kinase activity. Phosphorylates PTK2B/PYK2 and myosin light-chains. Involved in the inflammatory response (e.g. apoptosis, vascular permeability, leukocyte diapedesis), cell motility and morphology, airway hyperreactivity and other activities relevant to asthma. Required for tonic airway smooth muscle contraction that is necessary for physiological and asthmatic airway resistance. Necessary for gastrointestinal motility. Implicated in the regulation of endothelial as well as vascular permeability, probably via the regulation of cytoskeletal rearrangements. In the nervous system it has been shown to control the growth initiation of astrocytic processes in culture and to participate in transmitter release at synapses formed between cultured sympathetic ganglion cells. Critical participant in signaling sequences that result in fibroblast apoptosis. Plays a role in the regulation of epithelial cell survival. Required for epithelial wound healing, especially during actomyosin ring contraction during purse-string wound closure. Mediates RhoA-dependent membrane blebbing. Triggers TRPC5 channel activity in a calcium-dependent signaling, by inducing its subcellular localization at the plasma membrane. Promotes cell migration (including tumor cells) and tumor metastasis. PTK2B/PYK2 activation by phosphorylation mediates ITGB2 activation and is thus essential to trigger neutrophil transmigration during acute lung injury (ALI). May regulate optic nerve head astrocyte migration. Probably involved in mitotic cytoskeletal regulation. Regulates tight junction probably by modulating ZO-1 exchange in the perijunctional actomyosin ring. Mediates burn-induced microvascular barrier injury; triggers endothelial contraction in the development of microvascular hyperpermeability by phosphorylating MLC. Essential for intestinal barrier dysfunction. Mediates Giardia spp.-mediated reduced epithelial barrier function during giardiasis intestinal infection via reorganization of cytoskeletal F-actin and tight junctional ZO-1. Necessary for hypotonicity-induced Ca(2+) entry and subsequent activation of volume-sensitive organic osmolyte/anion channels (VSOAC) in cervical cancer cells. Responsible for high proliferative ability of breast cancer cells through anti-apoptosis.

VIL2, also known as villin-2, belongs to the ERM protein family. It is expressed in cerebral cortex, basal ganglia, hippocampus, hypophysis, and optic nerve. VIL2 contains 1 FERM domain and may be involved in connections of major cytoskel

Oncomodulin-1 (OM) is a small, calcium-binding protein and a macrophage-derived growth factor, which can promote axon regeneration in retinal ganglion cells. Oncomodulin-1 is constitutively secreted by activated macrophages in the vitreous and retina in response to inflammatory conditions that promote optic nerve regeneration. Oncomodulin-1 binds RGCs with high affinity in vitro, but only when cAMP is pharmacologically elevated or if the membrane is permeabilized allowing Oncomodulin-1 access to the cytosolic compartment. Oncomodulin-1 is a member of the superfamily of calmodulin proteins and is a high-affinity calcium ion-binding protein and contains 2 EF-hand domains. OM is found in early embryonic cells in the placenta and also in tumors. It has some calmodulin-like activity with respect to enzyme activation and growth regulation.