Abstract: An optical fiber switching device includes a holding base, a threaded axle and two guide spindles installed in the holding base, a motor connected with the threaded axle to drive the threaded axle to rotate, and a positioning block meshed with the threaded axle and supported by the two guide spindles. When the motor is actuated, the positioning block is linearly moved along the threaded axle and kept in balance, thus a first collimating lens disposed on the positioning block is able to be precisely aligned with a second collimating lens which is disposed at a side of the holding base. Because the first collimating lens and the second collimating lens are precisely in alignment, any possible insertion loss of the optical fiber switching device is minimized.

Abstract: The present invention relates to KCNQ proteins defining potassium channels. In particular, the invention concerns the human KCNQ2, human KCNQ3, murine KCNQ2, and rat KCNQ2 proteins reported herein. KCNQ2 and KCNQ3 proteins are nervous system-selective and may be involved in neurotransmission and neuroprotection. The KCNQ2 and KCNQ3 of the present invention can be used to assay for modulators of the proteins, which would be useful in treatment of such disorders as ataxia, myokymia, seizures, Alzheimer's disease, Parkinson's disease, age-associated memory loss, learning deficiencies, motor neuron diseases, epilepsy, stroke, and the like.

Abstract: A new chimeric plasminogen activator with high fibrin affinity was designed to bind to a fibrin clot and initiate clot destruction in the presence of thrombin, but not plasmin. The chimeric molecule has an antibody variable region having a fibrin-specific antigen binding site and a single chain urokinase region having a thrombin activation site but not a plasmin activation site. The preferred embodiment, 59D8-ScuPA-T, has an N-terminal fragment of an anti-fibrin antibody (59DB) and a C-terminal thrombin-activatable low molecular weight single-chain urokinase plasminogen activator (scuPA-T). The scuPA-T portion was obtained by deletion of two amino acids (Phe157 and Lys 158) that make up the plasmin activation site from low molecular weight single chain urokinase-type plasminogen activator (scuPA).