We report on the photoresponse of mid-wavelength infrared radiation (MWIR) type-II superlattices (T2SLs) InAs/InAsSb high operating temperature (HOT) photoresistor grown on GaAs substrate. The device consists of a 200 periods of active layer grown on GaSb buffer layer. The photoresistor reached a 50% cut-off wavelength of 5 µm and 6 µm at 200 K and 300 K respectively. The time constant of 30 ns is observed at 200 K under 1 V bias. This is the first observation of the photoresponse in MWIR T2SLs InAs/InAsSb above 200 K.
Heterogeneous nuclear ribonucleoprotein K (hnRNP K), is a multifunctional protein that participates in a variety of regulatory processes of signal transduction and gene expression. To further characterize the significance of hnRNP K in different male germ cells, we investigated the expression profiles of hnRNP K at different developmental stages in pig and rat testes, and conducted a comparative analysis of expression patterns between these two species. In porcine testis development, both the mRNA and protein level of hnRNP K were down-regulated from 3 months to 8 months. However, the expression level of hnRNP K was abundant across the embryonic period in rats, and decreased gradually from 0 day post partum (dpp) to 14 dpp, then increased with the highest level presenting at 90 dpp. Immunolocalization analysis further confirmed the differential expression and localization of hnRNP K protein during testis development in pigs and rats. The results showed that hnRNP K was widely distributed in gonocytes, spermatogonia, sertoli cells and Leydig cells. The dynamic expression profile of hnRNP K may imply its crucial and potential roles in the development of the testis, which will provide a theoretical basis for the future study of molecular mechanism regulation of spermatogenesis.
Sapelovirus A (SV-A) is a positive-sense single-stranded RNA virus which is associated with acute diarrhea, pneumonia and reproductive disorders. The virus capsid is composed of four proteins, and the functions of the structural proteins are unclear. In this study, we expressed SV-A structural protein VP1 and studied its antigenicity and immunogenicity. SDS-PAGE analysis revealed that the target gene was expressed at high levels at 0.6 mM concentration of IPTG for 24 h. The mouse polyclonal antibody against SV-A VP1 protein was produced and reached a high antiserum titer (1: 2,048,000). Immunized mice sera with the recombinant SV-A VP1 protein showed specific recognition of purified VP1 protein by western blot assay and could recognize native SV-A VP1 protein in PK-15 cells infected with SV-A by indirect immunofluorescence assay. The successfully purified recombinant protein was able to preserve its antigenic determinants and the generated mouse anti-SV-A VP1 antibodies could recognize native SV-A, which may have the potential to be used to detect SV-A infection in pigs.