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最近の記事

2025/11/17
Narrative Review of Patient Cancer Tissue-Derived Zebrafish Xenograft Models for Evaluating Drug Sensitivity as an Avatar Model for Clinical Application
2025/10/31
Zebrafish Xenograft Model for Predicting Cisplatin Efficacy in Muscle-Invasive Bladder Cancer
2025/10/16
AI-Driven Image Analysis for Precision Screening Transposon-Mediated Transgenesis of NFκB eGFP Reporter System in Zebrafish
2025/08/06
Variation and classification of chemically-induced zebrafish malformations for the ICH S5 (R3) guideline: an atlas for zebrafish teratogenesis
2024/08/06
Validation of a new protocol for a zebrafish MEFL (malformation or embryo-fetal lethality) test method that conforms to the ICH S5 (R3) guideline
2024/05/21
In vivo assessment of individual and total proteinuria in zebrafish larvae using the solvatochromic compound ZMB741
2021/10/31
Generation of a Transgenic Zebrafish Line for In Vivo Assessment of Hepatic Apoptosis
2021/08/19
Patient-Derived Cancer Xenograft Zebrafish Model (PDXZ) for Drug Discovery Screening and Personalized Medicine
2021/07/09
Establishment of a Quality Control Protocol for Zebrafish Developmental Toxicity Studies
2020/10/13
Gap junction protein beta 4 plays an important role in cardiac function in humans, rodents, and zebrafish

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1999/01/01
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Human S100A11 Exhibits Differential Steady-State RNA Levels in Various Tissues and Distinct Subcellular Localization.

Hiroyasu Inada, Michiko Naka, Toshio Tanaka, Gabriela E. Davey and Claus W. Heizmann
Biochem. Biophys. Res. Commun. 263 135-138 1999
Abstract

In order to analyze the steady-state RNA levels of S100A11 in different tissues, a cDNA fragment of human S100A11 was isolated from a cDNA library. The obtained fragment was labeled and hybridized to RNA isolated from various tissues. The Northern blot analysis revealed that S100A11 RNA levels varied from high in placenta, through intermediate in heart, lung, kidney, and most muscle samples, to barely detectable in brain. An efficient purification method for recombinant S100A11 yielding high quantities was developed. Furthermore, to examine the subcellular localization of this protein, the human polypeptide S100A11 antibodies were raised in rabbit. S100A11 was found to have a localization distinct from other S100 proteins examined, and is mostly localized in the nucleus, with slight variations among different glioblastoma cell types.



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