Hepta-histidine
Hepta-histidine is an inhibitor of Ku70-Huntingtin protein interaction. Hepta-histidine can reverse the morphological abnormalities of primary neurons differentiatied from hiPSCs. Hepta-histidine prolongs the lifespan in severe Huntington’s disease R6/2 mouse model. Hepta-histidine ameliorates DNA damage in vitro. Hepta-histidine can be used to study anti-aggregation agent against Tau-associated neurodegenerative diseases such as Alzheimer’s disease and Huntington’s disease.
商品は「研究用試薬」です。人や動物の医療用・臨床診断用・食品用の製品ではありません。
研究用途以外に使用した場合、当社は一切の責任を負いかねます。
- CAS 番号: 64134-31-2
- 分子式: C42H51N21O8
- 分子量:978.01
-
保管条件:
Please store the product under the recommended conditions in the Certificate of Analysis.
生物活性
製品説明
化学情報
-
CAS 番号 64134-31-2
-
分子量 978.01
-
分子式 C42H51N21O8
-
配列
His-His-His-His-His-His-His
-
シーケンスの短縮
HHHHHHH
-
輸送条件
Room temperature in continental US; may vary elsewhere.
-
保管条件
Please store the product under the recommended conditions in the Certificate of Analysis.
プロトコル
-
Pull-down
The pull-down assay is an in vitro technique used to detect physical interactions between two or more proteins and an invaluable tool for confirming a predicted protein-protein interaction or identifying novel interacting partners. This method typically involves the use of affinity purification with various wash and elution steps.
-
Immunoprecipitation
Immunoprecipitation (IP) is an experimental method that uses the principle of antibody specific binding to purify and enrich target proteins.
-
Protocol for Bimolecular Fluorescence Complementation (BiFC) Assay
Bimolecular fluorescence complementation detects protein-protein proximity in living or fixed cells by fusing two candidate interaction partners to nonfluorescent N- and C-terminal fragments of a fluorescent protein; when the partners interact or remain close enough, the fluorescent fragments complement, mature, and generate a fluorescent signal at the site of the protein complex. The BiFC readout is fluorescence intensity and subcellular localization of the reconstituted fluorophore, which reflects formation or stabilization of a protein complex rather than direct biochemical binding kinetics; BiFC is therefore useful for mapping where interactions occur in cancer cells, neurons, macrophages, organoid-derived cells, or drug-screening systems, but results should be validated by independent assays such as co-IP or Western blot. BiFC signal formation is delayed by fluorophore maturation and can stabilize otherwise transient complexes, so it is not a real-time reversible interaction assay
-
Genotoxicity/Mutagenicity Study
The bacterial reverse mutation assay detects point mutations that restore amino-acid prototrophy in auxotrophic Salmonella typhimurium or Escherichia coli tester strains; after exposure to a test article, mutagenic activity is read out as an increased number of revertant colonies on minimal agar compared with the vehicle control. The assay uses tester strains with different mutation targets so that base-substitution and frameshift mutagens can be detected, and testing is performed with and without exogenous mammalian metabolic activation because some chemicals require biotransformation to become mutagenic.
-
Co-Immunoprecipitation
Co-immunoprecipitation technology can verify protein interaction based on the specific immune reaction between antibodies and antigens.
-
Protocol for Yeast Two-Hybrid (Y2H) Assay
The yeast two-hybrid assay detects binary protein-protein interactions by separating a transcription factor into a DNA-binding domain fused to a "bait" protein and a transcriptional activation domain fused to a "prey" protein; if bait and prey interact in yeast, the transcription factor is reconstituted and activates reporter genes such as HIS3, ADE2, lacZ, MEL1, or other selectable/readable reporters. The readout is yeast growth on selective medium and/or reporter activity, which reflects proximity-dependent transcriptional activation in the yeast nucleus rather than direct biochemical binding in the original mammalian, tumor, neuronal, macrophage, or organoid context. Because yeast two-hybrid can generate false positives and false negatives, interaction claims should be validated using independent assays such as co-immunoprecipitation, Western blot, immunofluorescence colocalization, BiFC, pull-down, or mammalian two-hybrid assays.
-
How to Choose the Right Model Animal
Choosing the right model animal is a validity-driven decision in which the species, strain, sex, age, genetic background, disease-induction method, outcome measures, and welfare burden must match the scientific question rather than laboratory tradition or convenience. A model should be selected by judging face validity, construct validity, and predictive validity: whether it resembles the human phenotype, whether it reproduces relevant mechanisms, and whether results are likely to predict human biology or treatment response. Animal studies often fail to translate because of species differences, weak disease resemblance, poor experimental design, inadequate reporting, publication bias, and underuse of randomization, blinding, and sample-size justification. Unresolved questions include how to rank competing models objectively, how much human-disease complexity must be reproduced for a given objective, and when non-animal systems such as organoids, ex vivo tissue, or computational models
純度とドキュメンテーション
参考文献
[1]. Kondo K, et al., Hepta-Histidine Inhibits Tau Aggregation. ACS Chem Neurosci. 2021 Aug 18;12(16):3015-3027. [Content Brief]
[2]. Imamura T, et al., Identification of hepta-histidine as a candidate drug for Huntington's disease by in silico-in vitro- in vivo-integrated screens of chemical libraries. Sci Rep. 2016 Sep 22;6:33861. [Content Brief]
Calculators
濃度 (開始) × 体積 (開始) = 濃度 (終了) × 体積 (終了)