Abstract: An assay device (1) comprises a base (2) and glass plate lid (3). The base (2) has an array of shallow microwells (4), each having a flat rim (9), all rims being co-planar. When the lid (3) is placed on the base (2) a thin capillary gap (10) is formed on each rim, acting as a liquid seal for a microwell chamber. The liquid is excess sample liquid and further excess is accommodated in overspill cavities (6) between the microwells (4). Because of the liquid seal and shallow configuration the benefits of microfluidic devices are achieved together with the handling convenience and use of conventional detection equipment of conventional microplate devices.

Abstract: A protein encoded by a gene comprises nucleic acid sequence SEQ ID No. 1, 2, 3, 4, 5, 6 or a derivative or mutant or fragment or variant or peptide thereof. The protein promotes the attachment and modulates the motility and invasion capability of cells.

Abstract: An assay device (1) comprises a base (2) and glass plate lid (3). The base (2) has an array of shallow microwells (4), each having a flat rim (9), all rims being co-planar. When the lid (3) is placed on the base (2) a thin capillary gap (10) is formed on each rim, acting as a liquid seal for a microwell chamber. The liquid is excess sample liquid and further excess is accommodated in overspill cavities (6) between the microwells (4). Because of the liquid seal and shallow configuration the benefits of microfluidic devices are achieved together with the handling convenience and use of conventional detection equipment of conventional microplate devices.

Abstract: Active Survival Domains in the Insulin-like Growth Factor-I Receptor (IGF-IR) required for transmitting the survival signal in vertebrate cells have been identified. In FL5.12 cells transfected with wild type IGF-I receptors, IGF-I provided protection from IL-3 withdrawal analogous to the protection afforded by expression of Bcl-2. Under the same conditions, IGF-I did not have a significant mitogenic effect on FL5.12 cells expressing IGF-I receptors. An IGF-I receptor with a mutation at the ATP-binding site did not provide protection from apoptosis. However, mutations at tyrosine residue 950 or in the tyrosine cluster (1131, 1135, and 1136) in the kinase domain resulted in receptors that retained survival function. In the C-terminus of the IGF-IR, mutation at tyrosine 1251 and at histidine 1293 and lysine 1294 abolished apoptotic function, whereas mutation of the four scrines at 1280-1283 did not affect survival. Surprisingly, receptors truncated at the C-terminus had enhanced anti-apoptotic function.

Abstract: Active Survival Domains in the Insulin-like Growth Factor-I Receptor (IGF-IR) required for transmitting the survival signal in vertebrate cells have been identified. In FL5.12 cells transfected with wild type IGF-I receptors, IGF-I provided protection from IL-3 withdrawal analogous to the protection afforded by expression of Bcl-2. Under the same conditions, IGF-I did not have a significant mitogenic effect on FL5.12 cells expressing IGF-I receptors. An IGF-I receptor with a mutation at the ATP-binding site did not provide protection from apoptosis. However, mutations at tyrosine residue 950 or in the tyrosine cluster (1131, 1135, and 1136) in the kinase domain resulted in receptors that retained survival function. In the C-terminus of the IGF-IR, mutation at tyrosine 1251 and at histidine 1293 and lysine 1294 abolished apoptotic function, whereas mutation of the four serines at 1280-1283 did not affect survival. Surprisingly, receptors truncated at the C-terminus had enhanced anti-apoptotic function.