Abstract: Heat-activated adhesive tape has a backing comprising 88-92% acrylic polymer containing: 35-45% of a first alkyl acrylate monomer with alkyl groups containing 4 to 12 carbon atoms, 30-40% of a second alkyl acrylate monomer with alkyl groups containing 4 to 12 carbon atoms, 6-10% a first monoethylenically unsaturated polar copolymerizable monomer, 1-2% a second monoethylenically unsaturated polar copolymerizable monomer, 0.3-0.5% photoinitiator, 1-2% filler, 0.05-0.07% crosslinker/chain extender, and 8-12% hollow glass microspheres; and heat-activated adhesive layer on at least one side. A pressure-sensitive adhesive may be on the other side.

Abstract: A universal secretory signal originally derived from a piscine vitellogenin (Vtg) gene is inserted into various expression vectors for driving the secretion of the recombinant protein into the culture medium. This enhances the detection, quantification and downstream scaled-up purification of a recombinant protein of interest. The secretory signal system is very versatile, being conveniently and widely applicable to an array of heterologous host cells such as bacteria, yeast, insect, piscine, and mammalian cell lines (e.g., COS, CHO, NIH/3T3). The said secretory system is also applicable as a reporter vector for secretion of reporter proteins/enzymes, thus, enabling the detection of the reporter proteins (e.g., CAT, GFP) in the culture medium.

Abstract: The horseshoe crab, Carcinoscorpius rotundicauda Factor C cDNA (CrFC21) has been cloned into a shuttle baculoviral vector and another vector suitable for expression in insect cells. The recombinant baculoviral DNA was then transfected into the insect cells for expression of recombinant Factor C. Recombinant Factor C was found to be immunoreactive and is capable of binding both free and bound/immobilized lipid A. It is enzymatically active when triggered by LPS. The rFC is probably of the two-chain form, being cleaved into the heavy and light chains after activation by Gram negative bacterial endotoxin. As low as 0.01 pg (0.001 ng/ml) of LPS was detectable by the rFC, thus, indicating its potentials as a novel generation of “limulus amoebocyte lysate.

Abstract: A hydrocolloid bandage for the wound care designed for improved pliability and decreased peripheral edge lift. In particular, the invention is concerned with a hydrocolloid bandage which is absorbent, non-damaging to the skin and comfortable to the user preferably having at least a hydrocolloid region covered by film and adhesive layers which contact the user's skin at the periphery of the bandage.

Abstract: Hydrocolloid compositions are provided having improved advantages over previous hydrocolloid compositions. The novel hydrocolloid compositions herein disclosed are particularly useful in the manufacturing of dressings for application to the skin of a user for wound care, displaying improved integrity, absorption and adhesion. Methods of manufacturing the hydrocolloid compositions are also provided.

Abstract: A calendered hydrocolloid dressing for the wound care and a one step method of manufacturing the hydrocolloidal dressing are described. In particular, the invention is concerned with a hydrocolloid dressing which is absorbent, non-damaging to the skin and comfortable to the user preferably having at least a thermoplastic elastomer backing and water absorbent polymeric adhesive layer.

Abstract: Heat-activated adhesive tape has a backing comprising 88-92% acrylic polymer containing: 35-45% of a first alkyl acrylate monomer with alkyl groups containing 4 to 12 carbon atoms, 30-40% of a second alkyl acrylate monomer with alkyl groups containing 4 to 12 carbon atoms, 6-10% a first monoethylenically unsaturated polar copolymerizable monomer, 1-2% a second monoethylenically unsaturated polar copolymerizable monomer, 0.3-0.5% photoinitiator, 1-2% filler, 0.05-0.07% crosslinker/chain extender, and 8-12% hollow glass microspheres; and heat-activated adhesive layer on at least one side. A pressure-sensitive adhesive may be on the other side.

Abstract: CrFC21 cDNA was cloned into two mammalian vectors: pCIneo and pCDNAI, both of which carry the strong CMV promoter for expression in mammalian cell lines. Various CrFC cDNA constructs transformed into P. pastoris and S. cerevisiae were expressed to yield full-length recombinant Factor C (rCrFC) protein of .about.130 kDa which is immunoreactive. The rCrFC is expressed in an intracellular, insoluble form. Intracellular localization of the nascent protein provides protection from premature digestion by proteases secreted by the host cell. Subsequent to its synthesis, rCrFC is solubilized and purified under pyrogen-free conditions. Using established protocols, the protein can be denatured and renatured to recover its biological functionality. By manipulation of the 5' end of CrFC26, truncated constructs containing this cDNA are expressed by S. cerevisiae to give immunoreactive rCrFC. The rCrFC produced from both CrFC21 and CrFC26 constructs, solubilized by Triton X-100 or SDS, is found to be immunoreactive.

Abstract: CrFC21 cDNA was cloned into two mammalian vectors: pCIneo and pCDNAI, both of which carry the strong CMV promoter for expression in mammalian cell lines. Various CrFC cDNA constructs transformed into P. pastoris and S. cerevisiae were expressed to yield full-length recombinant Factor C (rCrFC) protein of .about.130 kDa which is immunoreactive. The rCrFC is expressed in an intracellular, insoluble form. Intracellular localization of the nascent protein provides protection from premature digestion by proteases secreted by the host cell. Subsequent to its synthesis, rCrFC is solubilized and purified under pyrogen-free conditions. Using established protocols, the protein can be denatured and renatured to recover its biological functionality. By manipulation of the 5' end of CrFC26, truncated constructs containing this cDNA are expressed by S. cerevisiae to give immunoreactive rCrFC. The rCrFC produced from both CrFC21 and CrFC26 constructs, solubilized by Triton X-100 or SDS, is found to be immunoreactive.

Abstract: Full-length and deletion subclones of cDNAs for Factor C of Carcinoscorpius rotundicauda are provided. These cDNAs have been cloned into .lambda.gt 22 and pGEM 11Zf(+). Further manipulations of the 5' and 3' ends of these cDNAs have been carried out, and these cDNAs have been further subcloned into other expression vectors such as pGEMEX-1, pET 3b, and the yeast shuttle vectors YEpsec 1 and pEMBLyex 4, and pPIC 9 and pHIL D2. Also provided are host cells transformed with expression vectors containing DNA molecules encoding proteins having Factor C-like enzymatic activity, methods of producing such proteins, methods for purifying Factor C zymogens, and methods for protecting Factor C zymogens from autoactivation by Gram negative bacterial endotoxin while the proenzyme is being purified and/or processed from amoebocyte lysates or from recombinant clones, or during storage or subsequent handling. This protection is afforded by the addition of 5-30% Me.sub.2 SO, which reversibly inhibits the Factor C zymogen.

Abstract: Full-length and deletion subclones of cDNAs for Factor C of Carcinoscorpius rotundicauda are provided. These cDNAs have been cloned into .lambda.gt 22 and pGEM 11Zf(+). Further manipulations of the 5' and 3' ends of these cDNAs have been carried out, and these cDNAs have been further subcloned into other expression vectors such as pGEMEX-1, pET 3b, and the yeast shuttle vectors YEpsec 1 and pEMBLyex 4, and pPIC 9 and pHIL D2. Also provided are host cells transformed with expression vectors containing DNA molecules encoding proteins having Factor C-like enzymatic activity, methods of producing such proteins, methods for purifying Factor C zymogens, and methods for protecting Factor C zymogens from autoactivation by Gram negative bacterial endotoxin while the proenzyme is being purified and/or processed from amoebocyte lysates or from recombinant clones, or during storage or subsequent handling. This protection is afforded by the addition of 5-30% Me.sub.2 SO, which reversibly inhibits the Factor C zymogen.