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- Vukusic, J., et al.
(författare)
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MOVPE-grown GaInNAsVCSELs at 1.3 mu m with conventional mirror design approach
- 2003
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Ingår i: Electronics Letters. - : Institution of Engineering and Technology (IET). - 0013-5194 .- 1350-911X. ; 39:8, s. 662-664
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Tidskriftsartikel (refereegranskat)abstract
- 1.3 mum oxide confined GaInNAs VCSELs designed using the same design philosophy used for standard 850 nm VCSELs is presented. The VCSELs have doped mirrors, with graded and highly doped interfaces, and are fabricated using production-friendly procedures. Multimode VCSELs (I I mum oxide aperture) with an emission wavelength of 1287 nm have a threshold current of 3 mA and produce I mW of output power at 20degreesC. The maximum operating temperature is 95degreesC. Emission at 1303 nm with I mW of output power and a threshold current of 7 mA has been observed from VCSELs with a larger detuning between the gain peak and the cavity resonance.
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| 5. |
- Sandilands, Aileen, et al.
(författare)
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Bfsp2 mutation found in mouse 129 strains causes the loss of CP49' and induces vimentin-dependent changes in the lens fibre cell cytoskeleton.
- 2004
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Ingår i: Experimental eye research. - : Elsevier BV. - 0014-4835. ; 78:4, s. 875-89
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Tidskriftsartikel (refereegranskat)abstract
- Here we report the first natural mutation in the mouse Bfsp2 gene. Characterisation of mouse Bfsp2 in the 129X1/SvJ revealed a mutation that deleted the acceptor site of exon 2. This results in exon 1 being erroneously spliced to exon 3 causing a frameshift in the reading frame and the introduction of a stop codon at position 2 of exon 3 in the Bfsp2 transcript. RT-PCR studies of lens RNA isolated from 129S1/SvImJ, 129S2/SvPas and 129S4/SvJae strains confirmed the presence of this mutation in these diverse 129 strains and similar mutations were found in both CBA and 101 strains, but not in C3H or C57BL/6J mouse strains. This mutation is predicted to result in a severely truncated protein product called CP49, comprising essentially only exon 1, but polyclonal antibodies to CP49 failed to detect either full length or fragments of CP49 in extracts made from either 129S1/SvImJ or 129S4/SvJae suggesting that these 129 strains lack CP49 protein. Like the knockout of Bfsp2 reported recently, filensin protein levels and its proteolytic processing were altered also in the 129S1/SvImJ and 129S4/SvJae strains compared to C57BL/6J. Electron microscopy of the lens cytoskeleton from 129S2/SvPas revealed similar morphological changes in the cytoskeleton as compared to the CP49 knockout, with beaded and intermediate filaments being apparently replaced by poorly defined filament-like material. Vimentin was a key component of this residual material as shown by immunoelectron microscopy and by the generation of a CP49/vimentin double knockout mouse. This report of a natural mutation in Bfsp2 in the 129 and other mouse strains also has important implications for lens studies that have used the 129X1/SvJ strain in knockout strategies.
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