Thermal conductivity of isotopically enriched silicon carbide

Since the semiconductor silicon carbide presents attractive opportunities for the fabrication of novel electronic devices, there is significant interest in improving its material quality. Shrinking component sizes and high demands for efficiency and reliability make the capability to release excess heat an important factor for further development. Experience from Si and Diamond tells us that isotopic enrichment is a possible way to increase the thermal conductivity. We have produced samples of 4H-SiC that contain 28Si and 12C to a purity of 99.5%. The thermal conductivity in the c-direction of these samples has been measured by a transient thermoreflectance method. An improvement due to enrichment of at least 18% was found. The result is valid for a temperature of 45K above room temperature. A preliminary study of the temperature dependence of the thermal conductivity demonstrates a strong temperature dependence in agreement with earlier reports for 4H. \ua9 2013 IEEE

Selective and Signal-dependent Recruitment of Membrane Proteins to Secretory Granules Formed by Heterologously Expressed von Willebrand Factor

von Willebrand factor (vWF) is a large, multimeric protein secreted by endothelial cells and involved in hemostasis. When expressed in AtT-20 cells, vWF leads to the de novo formation of cigar-shaped organelles similar in appearance to the Weibel-Palade bodies of endothelial cells in which vWF is normally stored before regulated secretion. The membranes of this vWF-induced organelle, termed the pseudogranule, are uncharacterized. We have examined the ability of these pseudogranules, which we show are secretagogue responsive, to recruit membrane proteins. Coexpression experiments show that the Weibel-Palade body proteins P-selectin and CD63, as well as the secretory organelle membrane proteins vesicle-associated membrane protein-2 and synaptotagmin I are diverted away from the endogenous adrenocorticotropic hormone-containing secretory granules to the vWF-containing pseudogranules. However, transferrin receptor, lysosomal-associated membrane protein 1, and sialyl transferase are not recruited. The recruitment of P-selectin is dependent on a tyrosine-based motif within its cytoplasmic domain. Our data show that vWF pseudogranules specifically recruit a subset of membrane proteins, and that in a process explicitly driven by the pseudogranule content (i.e., vWF), the active recruitment of at least one component of the pseudogranule membrane (i.e., P-selectin) is dependent on residues of P-selectin that are cytosolic and therefore unable to directly interact with vWF