Abstract: A semiconductor device includes a gate structure that extends from a first surface into a semiconductor portion and that surrounds a transistor section of the semiconductor portion. A field plate structure includes a field electrode and extends from the first surface into the transistor section. A mesa section of the semiconductor portion separates the field plate structure and the gate structure. A contact structure includes a first portion directly adjoining the mesa section and a second portion directly adjoining the field electrode. The first and second portions include stripes and are directly connected to each other.

Abstract: A semiconductor device includes a gate structure that extends from a first surface into a semiconductor portion and that surrounds a transistor section of the semiconductor portion. A field plate structure includes a field electrode and extends from the first surface into the transistor section. A mesa section of the semiconductor portion separates the field plate structure and the gate structure. A contact structure includes a first portion directly adjoining the mesa section and a second portion directly adjoining the field electrode. The first and second portions include stripes and are directly connected to each other.

Abstract: The invention relates to a method for producing biologically active ?-NGF from the proform proNGF. After expressing the proform of the ?-NGF in a prokaryotic host cell, the recombinant protein is isolated in the form of insoluble inactive aggregates (inclusion bodies). After the solubilization thereof in a strong denaturing agent and the subsequent conversion thereof into the natural conformation, which is determined by the disulfide bridges present in the natural ?-NGF, biologically active ?-NGF is obtained by subsequently splitting-off the prosequence.

Abstract: The invention relates to a method for producing biologically active ?-NGF from the proform proNGF. After expressing the proform of the ?-NGF in a prokaryotic host cell, the recombinant protein is isolated in the form of insoluble inactive aggregates (inclusion bodies). After the solubilization thereof in a strong denaturing agent and the subsequent conversion thereof into the natural conformation, which is determined by the disulfide bridges present in the natural ?-NGF, biologically active ?-NGF is obtained by subsequently splitting-off the prosequence.

Abstract: The invention relates to a method for producing biologically active ?-NGF from the proform proNGF. After expressing the proform of the ?-NGF in a prokaryotic host cell, the recombinant protein is isolated in the form of insoluble inactive aggregates (inclusion bodies). After the solubilization thereof in a strong denaturing agent and the subsequent conversion thereof into the natural conformation, which is determined by the disulfide bridges present in the natural ?-NGF, biologically active ?-NGF is obtained by subsequently splitting-off the prosequence.

Abstract: In order to recombinantly prepare a biologically active protein of the TGF-? superfamily, a protein, whose amino terminus consists of the pro sequence of a protein of the TGF-? superfamily, or parts thereof, to which the mature domain of this protein or of another protein of TGF-? superfamily which exhibits at least 35% homology with mature BMP-2 is attached, is expressed in prokaryotes under conditions in which at least a part of the protein is obtained in the form of inclusion bodies, the inclusion bodies are isolated and solubilized under denaturing conditions, the denatured, monomeric and biologically inactive protein which has been solubilized from the inclusion bodies is renatured, with folding and dimerization to give the soluble, biologically active conformation and, where appropriate, after the renaturation, the mature protein is released proteolytically from its pro form.

Abstract: In order to recombinantly prepare a biologically active protein of the TGF-&bgr; superfamily, a protein, whose amino terminus consists of the pro sequence of a protein of the TGF-&bgr; superfamily, or parts thereof, to which the mature domain of this protein or of another protein of TGF-&bgr; superfamily which exhibits at least 35% homology with mature BMP-2 is attached, is expressed in prokaryotes under conditions in which at least a part of the protein is obtained in the form of inclusion bodies, the inclusion bodies are isolated and solubilized under denaturing conditions, the denatured, monomeric and biologically inactive protein which has been solubilized from the inclusion bodies is renatured, with folding and dimerization to give the soluble, biologically active conformation and, where appropriate, after the renaturation, the mature protein is released proteolytically from its pro form.

Abstract: A process for the production of a naturally folded eukaryotic polypeptide containing two or several cysteines linked by disulfide bridges by a) culturing prokaryotic cells in which the said prokaryotic cells contain an expression vector which codes for the said polypeptide which contains a prokaryotic signal sequence at the N-terminus, b) secreting the polypeptide into the periplasm or the medium, c) cleaving the signal sequence and isolating the polypeptide from the periplasm or the medium, which is characterized in that a nucleic acid coding for a molecular chaperone is additionally expressed in the said prokaryotic cell and the chaperone is secreted into the periplasm, is suitable for the recombinant production of polypeptides in prokaryotes in a high yield.

Abstract: A process produces a water-soluble, naturally folded eukaryotic polypeptide containing two or several cysteines linked by disulfide bridges. This process involves culturing prokaryotic cells, a) in which the prokaryotic cells contain an expression vector which encodes the polypeptide which contains a prokaryotic signal sequence at the N-terminus, b) under conditions under which the polypeptide is secreted into the periplasm or the medium, c) cleaving the signal sequence and isolating the polypeptide from the periplasm or the medium. In this process, the culturing is carried out in the presence of arginine or a compound of the formula I R2—CO—NR1 (I) in which R and R1 represent hydrogen or a saturated or unsaturated branched or unbranched C1-C4 alkyl chain and R2 represents hydrogen, NHR1 or a saturated or unsaturated branched or unbranched C1-C3 alkyl chain, is suitable for the recombinant production of polypeptides in prokaryotes in a high yield.