推荐产品
化驗
≥95%
形狀
powder
存貨情形
available only in USA
mp
205 °C (decomp.)
儲存溫度
2-8°C
InChI
1S/C16H16N2O5.ClH/c17-14(16(19)20)9-11-5-7-13(8-6-11)23-10-12-3-1-2-4-15(12)18(21)22;/h1-8,14H,9-10,17H2,(H,19,20);1H/t14-;/m0./s1
InChI 密鑰
DRUCEARMIBXBOJ-UQKRIMTDSA-N
應用
O-(2-Nitrobenzyl)-L-tyrosine hydrochloride (NBY) is a tyrosine derivative with an o-nitrobenzyl photocage that can be cleaved with 365 nm irradiation. NBY has been genetically encoded into multiple proteins, providing an ″on switch″ for regulation. Photocaged amino acids such as these are also useful in the synthesis of photocleavable chemical tools for spatial and temporal control over released molecules in biological applications.
Product can be used with our line of photoreactors: Including Penn PhD (Z744035) & SynLED 2.0 (Z744080)
Product can be used with our line of photoreactors: Including Penn PhD (Z744035) & SynLED 2.0 (Z744080)
其他說明
Site-Specific Encoding of Photoactivity in Antibodies Enables Light-Mediated Antibody-Antigen Binding on Live Cells
Time-resolved protein activation by proximal decaging in living systems
Crystal structure of a domain-swapped photoactivatable sfGFP variant provides evidence for GFP folding pathway
Light-control of the ultra-fast Gp41-1 split intein with preserved stability of a genetically encoded photo-caged amino acid in bacterial cells
Rapid and Inexpensive Evaluation of Nonstandard Amino Acid Incorporation in Escherichia coli
Time-resolved protein activation by proximal decaging in living systems
Crystal structure of a domain-swapped photoactivatable sfGFP variant provides evidence for GFP folding pathway
Light-control of the ultra-fast Gp41-1 split intein with preserved stability of a genetically encoded photo-caged amino acid in bacterial cells
Rapid and Inexpensive Evaluation of Nonstandard Amino Acid Incorporation in Escherichia coli
相關產品
产品编号
说明
价格
訊號詞
Danger
危險聲明
危險分類
Self-react. C
儲存類別代碼
5.2 - Organic peroxides and self-reacting hazardous materials
水污染物質分類(WGK)
WGK 3
閃點(°F)
Not applicable
閃點(°C)
Not applicable
Journal of the American Chemical Society, 130(29), 9268-9281 (2008-06-26)
In vivo incorporation of isotopically labeled unnatural amino acids into large proteins drastically reduces the complexity of nuclear magnetic resonance (NMR) spectra. Incorporation is accomplished by coexpressing an orthogonal tRNA/aminoacyl-tRNA synthetase pair specific for the unnatural amino acid added to
Chemical communications (Cambridge, England), 52(55), 8529-8532 (2016-06-10)
We developed two tightly regulated, light-activated Cre recombinase enzymes through site-specific incorporation of two genetically-encoded photocaged amino acids in human cells. Excellent optical off to on switching of DNA recombination was achieved. Furthermore, we demonstrated precise spatial control of Cre
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