Richard C. Meyer - La Habra CA Edward L. Carroll - Garden Grove CA
Assignee:
Beckman Instruments, Inc. - Fullerton CA
International Classification:
G01F 1300 B01L 302
US Classification:
7386414
Abstract:
Plunger operated pipet operable to execute different lengths of plunger movement during successive fluid pickup and fluid discharge operations or strokes. A stop member is movable between first and second locations in the pipet body to halt plunger movement at two different positions. A drive spring for driving the stop member from one location to the other is energized by a manually operable arming element and is retained in one location against action of the drive spring during a first plunger stroke. A release mechanism responsive to plunger movement during the first stroke disables the retaining means allowing the drive spring to move the stop member to the second location at which position the plunger is halted during the succeeding discharge stroke. The arming element is actuated by and in response to positioning of a replaceable tip on the pipet body. The arming element exerts a force on the tip sufficient to expel the tip from the body unless the tip is properly seated on the body thus ensuring that the pipet is armed if the tip is properly seated.
Compositions And Methods Comprising Cytostatic Protein Kinase
Jolinda A. Traugh - Riverside CA Regina D. Rooney - Del Mar CA Rolf Jakobi - Riverside CA Polygena T. Tuazon - Riverside CA William E. Meek - Colorado Springs CO Edward J. Carroll - Riverside CA Curtis A. Monnig - Riverside CA
Assignee:
The Regents of the University of California - Oakland CA
International Classification:
A61K 3851 C12N 912 C12P 2106 C07H 2104
US Classification:
424 945
Abstract:
The present invention presents a unique class of physiological suppressors of cell division and cleavage. In particular, the present invention presents p21-activated protein kinase PAK I, also known as protease activated protein kinase I (with the same abbreviation "PAK I") which has been purified to apparent homogeneity. PAK I is inactive, e. g. as a protein of about 60 kDa (denoted "p60", as determined by polyacrylamide gel electrophoresis) and is active when autophosphorylated, for example, following limited proteolysis, or binding of Cdc42, e. g. , as a protein of about 58 kDa (denoted "p58" as determined by polyacrylamide gel electrophoresis). The present invention also presents a fragment of PAK I, a peptide denoted p37, which contains the catalytic domain of PAK I. The purification, characterization, nucleotide and amino acid sequences of PAK I and p37 are also disclosed. Another aspect of the invention discloses the cytostatic activity of PAK I and its fragments.
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