Anti-GST monoclonal antibody, clone 33B7

Heterostructures (HS) have always been in attraction due to their inherited properties and different important applications. Integration of a phase-change material (PCM) with HS can tremendously extend the operating and application range using the "phase-tuning" of PCM for any optoelectronic devices. In the present study, we report a detailed study of electrical and optoelectronic characteristics of a p-p and p-n HS combining Ge2Sb2Te5 (GST) and Si. Reasonable 2 order of resistance switching is achieved by thermal annealing. The changes in optical properties are analysed using Ellipsometry, UV-Vis-NIR and Raman spectroscopy to speculate the optoelectronic behaviour of GST/Si samples. The optical and electrical characterization were analysed with aluminium (Al), platinum (Pt) and Ti/Au contacts. Appreciable rectifications varying from 500 to 1,000 at lower voltages are achieved with different contacts for both phases of GST. The change in rectification amount and current polarity are obtained with different kinds of contacts and at different incident wavelengths indicating different mechanisms of charge separation and collection. Responsivity of more than 9 A/W with<1,000 photo-current to dark-current ratio is demonstrated in wavelength range of 0.8-2 mu m under moderate range of biasing under mu W source power illumination. The characteristics obtained were justified with the prediction of band alignment with the help of work-function difference measurement by Kelvin-probe force microscopy and carrier density measurement by Hall experiment. Our results provide understanding to the opto-electrical behaviour of a heterojunction made of stacking PCM (GST) on Si highlighting their future use in photonic/optoelectronic-integrated circuits.

p53 is the most studied tumor suppressor and a key transcriptional factor, with discrete domains that regulate cellular pathways such as apoptosis, angiogenesis, cell-cycle arrest, DNA repair, and senescence. Previous studies have suggested that AIMP2, and ARS-interacting multifunctional protein 2, promote cell death via the protective interaction with p53 upon DNA damage. Also, oncogenic splicing variant of AIMP2 lacking exon2, AIMP2-DX2, compromises the pro-apoptotic activity and anti-proliferative activities of the AIMP2 by competing with AIMP2 for the binding with p53. However, the molecular mechanism for the interaction of p53 and AIMP2 remains elusive. Using NMR spectroscopy, we studied the structural details of the interaction of transactivation domain 1 (TAD1) of p53 with GST domain of AIMP2, which is also common in AIMP2-DX2. The chemical shift perturbation (CSP) experiments demonstrate that amino acid residues from EI7 to E28 of p53, known to bind to MDM2 are also involved in binding to AIMP2-DX2. Structure determination of this region based on the transferred-NOE (trNOE) data revealed that TAD1 of the p53 forms a turn structure with hydrophobic interactions by side chains of F19, L22, W23 and L26, distinct from the structure for MDM2 binding. Also, docking results based on NMR CSP data suggest the binding mode of p53 with AIMP2-DX2 GST domain. These data provide the first structural insight into the binding of the p53 TAD1 on AIMP2 and AIMP2-DX2. (C) 2020 Elsevier Inc. All rights reserved.