Strength-enhanced Sn–In low-temperature alloy with surface-modified ZrO₂ nanoparticle addition

Low-temperature packaging is essential for the widespread use of flexible electronic devices, and Sn–In eutectic alloys have attracted considerable attention because of their low melting temperatures. However, these alloys have a lower strength compared with other types of solder alloys. This study aimed to investigate the effect of adding nanoparticles on the mechanical strength of Sn–In eutectic alloys while keeping their melting temperature unchanged. ZrO₂ nanoparticles coated with NiO (NiO/ZrO₂ nanoparticles) were utilized to strengthen Sn–In eutectic alloys with a high dispersity. Sn–In composite alloys reinforced with NiO/ZrO₂ nanoparticles were fabricated, and tensile strength evaluation and microstructure observations were conducted. The experimental results showed that the addition of nanoparticles to the Sn–In eutectic alloys did not change their melting behavior. The tensile strength of the Sn–In composite alloys reinforced with NiO/ZrO₂ nanoparticles increased by up to 35.6%, which was attributed to grain refinement and dispersion strengthening. Even after thermal aging at 60 ºC, the Sn–In composite alloys reinforced with NiO/ZrO₂ nanoparticles showed a 1.11 times higher ultimate tensile strength than that of the non-aged, non-reinforced eutectic alloy, despite grain coarsening. This was attributed to the contribution of dispersion strengthening. These results indicate that the addition of NiO/ZrO₂ nanoparticles is an effective method to improve the strength of low-melting-temperature alloys.The version of record of this article, first published in Journal of Materials Science: Materials in Electronics, is available online at Publisher’s website: https://doi.org/10.1007/s10854-023-11344-

Development of automated brightfield double In Situ hybridization (BDISH) application for HER2 gene and chromosome 17 centromere (CEN 17) for breast carcinomas and an assay performance comparison to manual dual color HER2 fluorescence In Situ hybridization (FISH)

BACKGROUND: Human epidermal growth factor receptor 2 (HER2) fluorescence in situ hybridization (FISH) is a quantitative assay for selecting breast cancer patients for trastuzumab therapy. However, current HER2 FISH procedures are labor intensive, manual methods that require skilled technologists and specialized fluorescence microscopy. Furthermore, FISH slides cannot be archived for long term storage and review. Our objective was to develop an automated brightfield double in situ hybridization (BDISH) application for HER2 gene and chromosome 17 centromere (CEN 17) and test the assay performance with dual color HER2 FISH evaluated breast carcinomas. METHODS: The BDISH assay was developed with the nick translated dinitrophenyl (DNP)-labeled HER2 DNA probe and DNP-labeled CEN 17 oligoprobe on the Ventana BenchMark(® )XT slide processing system. Detection of HER2 and CEN 17 signals was accomplished with the silver acetate, hydroquinone, and H(2)O(2 )reaction with horseradish peroxidase (HRP) and the fast red and naphthol phosphate reaction with alkaline phosphatise (AP), respectively. The BDISH specificity was optimized with formalin-fixed, paraffin-embedded xenograft tumors, MCF7 (non-amplified HER2 gene) and BT-474 (amplified HER2 gene). Then, the BDISH performance was evaluated with 94 routinely processed breast cancer tissues. Interpretation of HER2 and CEN 17 BDISH slides was conducted by 4 observers using a conventional brightfield microscope without oil immersion objectives. RESULTS: Sequential hybridization and signal detection for HER2 and CEN 17 ISH demonstrated both DNA targets in the same cells. HER2 signals were visualized as discrete black metallic silver dots while CEN 17 signals were detected as slightly larger red dots. Our study demonstrated a high consensus concordance between HER2 FISH and BDISH results of clinical breast carcinoma cases based on the historical scoring method (98.9%, Simple Kappa = 0.9736, 95% CI = 0.9222 – 1.0000) and the ASCO/CAP scoring method with the FISH equivocal cases (95.7%, Simple Kappa = 0.8993%, 95% CI = 0.8068 – 0.9919) and without the FISH equivocal cases (100%, Simple Kappa = 1.0000%, 95% CI = 1.0000 – 1.0000). CONCLUSION: Automated BDISH applications for HER2 and CEN 17 targets were successfully developed and it might be able to replace manual two-color HER2 FISH methods. The application also has the potential to be used for other gene targets. The use of BDISH technology allows the simultaneous analyses of two DNA targets within the context of tissue morphological observation

New Methods for ALK Status Diagnosis in Non–Small-Cell Lung Cancer: An Improved ALK Immunohistochemical Assay and a New, Brightfield, Dual ALK IHC–In Situ Hybridization Assay

Introduction:The demonstration of anaplastic lymphoma kinase (ALK) positivity in non–small-cell lung cancer (NSCLC) has been hindered by the technical complexity and interpretative challenges of fluorescence in situ hybridization methods for detection of ALK gene rearrangement and by the inadequate sensitivity of existing immunohistochemistry (IHC) methods for ALK protein detection. In this study, we sought to increase the sensitivity of ALK IHC detection and to develop a brightfield assay for concurrent detection of ALK protein expression and ALK gene rearrangement.Methods:We developed a horseradish peroxidase–based IHC detection system using the novel, nonendogenous hapten 3-hydroxy-2-quinoxaline (HQ) and tyramide. We also developed a dual gene protein ALK assay combining a brightfield break-apart in situ hybridization ALK assay with another sensitive IHC method using the novel, nonendogenous hapten 5-nitro-3-pyrazole. We examined the sensitivity and accuracy of these methods using surgically resected NSCLC cases examined with ALK fluorescence in situ hybridization.Results:The new HQ-tyramide IHC detection system offered readily interpretable staining with substantially greater sensitivity than conventional ALK IHC, and produced heterogeneous and homogeneous patterns of ALK protein staining among ALK-positive NSCLC surgical cases. The new 5-nitro-3-pyrazole–based IHC detection system was similar in ALK detection sensitivity to the HQ-tyramide IHC system and was compatible with the brightfield in situ hybridization assay.Conclusion:The new HQ-tyramide IHC reagent system allows more sensitive assessment of ALK protein status in NSCLC cases. The new ALK gene-protein assay allows the concurrent visualization of ALK gene and ALK protein status in single cells, allowing more accurate ALK status determination even in heterogeneous specimens

The Fifth Data Release of the Sloan Digital Sky Survey

This paper describes the Fifth Data Release (DR5) of the Sloan Digital Sky Survey (SDSS). DR5 includes all survey quality data taken through June 2005 and represents the completion of the SDSS-I project (whose successor, SDSS-II will continue through mid-2008). It includes five-band photometric data for 217 million objects selected over 8000 square degrees, and 1,048,960 spectra of galaxies, quasars, and stars selected from 5713 square degrees of that imaging data. These numbers represent a roughly 20% increment over those of the Fourth Data Release; all the data from previous data releases are included in the present release. In addition to "standard" SDSS observations, DR5 includes repeat scans of the southern equatorial stripe, imaging scans across M31 and the core of the Perseus cluster of galaxies, and the first spectroscopic data from SEGUE, a survey to explore the kinematics and chemical evolution of the Galaxy. The catalog database incorporates several new features, including photometric redshifts of galaxies, tables of matched objects in overlap regions of the imaging survey, and tools that allow precise computations of survey geometry for statistical investigations.Comment: ApJ Supp, in press, October 2007. This paper describes DR5. The SDSS Sixth Data Release (DR6) is now public, available from http://www.sdss.or

Steroidogenic cell populations in follicles of the chicken ovary

A two cell theory for steroidogenesis in preovulatory follicles of the chicken ovary states that the granulosa layer metabolizes cholesterol to progestins and progestins are, then, metabolized to androgens and estrogens by the theca layer. However, the precise site of steroidogenic cells in the theca layer of preovulatory follicles and in small follicles of the chicken ovary has not been identified. Therefore, objectives of my dissertation were: (1) to identify steroidogenic cells in the theca layer of preovulatory follicles by immunocytochemistry for P450 steroidogenic enzymes and to measure steroid production by isolated theca cells in a short term cell incubation (Experiment 1); (2) to localize cell populations containing P450 steroidogenic enzymes in small follicles by immunocytochemistry (Experiment 2); and (3) to identify the site of 3$\beta$-hydroxysteroid dehydrogenase (3$\beta$-HSD) in small, preovulatory, and postovulatory follicles (Experiment 3). Follicles were obtained from regularly laying chickens 2 hours after oviposition of the first egg of a clutch. P450 steroidogenic enzymes stained in Experiments 1 and 2 were cholesterol side-chain cleavage cytochrome P450, 17$\alpha$-hydroxylase cytochrome P450, and aromatase cytochrome P450 to identify pregnenolone-, androgen-, or estrogen-producing cells, respectively.Experiment 1. The theca layer of preovulatory follicles contains three steroidogenic cell populations: (1) interstitial cells for progestin and androgen production from cholesterol; (2) fibroblasts as a possible conversion site from progestins to androgens; and (3) aromatase cells for estrogen production from androgens (a multiple cell theory for steroidogenesis in the theca layer of preovulatory follicles).Experiment 2. In small follicles, the theca layer, but not the granulosa layer, is the site of steroidogenesis. There are two populations of steroid synthesizing cells in the theca layer of small follicles: (1) interstitial cells for progestin and androgen production and (2) aromatase cells for estrogen production (a two cell theory for steroidogenesis in small follicles).Experiment 3. The localization of 3$\beta$-HSD shifts from the theca layer of small follicles to the granulosa and theca layers of preovulatory follicles and, then, to the granulosa layer of the postovulatory follicle.In conclusion, the localization and distribution of steroidogenic cells in follicles change during follicular maturation and the interaction between steroidogenic cells is required for complete steroid production in follicles of the chicken ovary.U of I OnlyETDs are only available to UIUC Users without author permissio