913588
O-(2-Nitrobenzyl)-L-tyrosine hydrochloride
≥95%
동의어(들):
(S)-2-Amino-3-(4-((2-nitrobenzyl)oxy)phenyl)propanoic acid hydrochloride, NBY, ONBY, Photo-controlled amino acid, Photocaged amino acid, Photocleavable tyrosine derivative
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모든 사진(1)
About This Item
실험식(Hill 표기법):
C16H17ClN2O5
CAS Number:
Molecular Weight:
352.77
MDL number:
UNSPSC 코드:
12352209
추천 제품
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![[2,2′-Bipyridine]-6-carboxylic acid hydrochloride](/deepweb/assets/sigmaaldrich/product/structures/130/786/b0e8142b-94b7-4abd-8a9a-0db3780a9f3d/640/b0e8142b-94b7-4abd-8a9a-0db3780a9f3d.png)
분석
≥95%
양식
powder
재고 정보
available only in USA
mp
205 °C (decomp.)
저장 온도
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 key
DRUCEARMIBXBOJ-UQKRIMTDSA-N
애플리케이션
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)
기타 정보
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
관련 제품
제품 번호
설명
가격
신호어
Danger
유해 및 위험 성명서
Hazard Classifications
Self-react. C
Storage Class Code
5.2 - Organic peroxides and self-reacting hazardous materials
WGK
WGK 3
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
가장 최신 버전 중 하나를 선택하세요:
Lei Wang et al.
Angewandte Chemie (International ed. in English), 44(1), 34-66 (2004-12-16)
Although chemists can synthesize virtually any small organic molecule, our ability to rationally manipulate the structures of proteins is quite limited, despite their involvement in virtually every life process. For most proteins, modifications are largely restricted to substitutions among the
Jana K Böcker et al.
Angewandte Chemie (International ed. in English), 54(7), 2116-2120 (2015-01-06)
Cyclic peptides are important natural products and hold great promise for the identification of new bioactive molecules. The split-intein-mediated SICLOPPS technology provides a generic access to fully genetically encoded head-to-tail cyclized peptides and large libraries thereof (SICLOPPS=split-intein circular ligation of
Light-activated gene editing with a photocaged zinc-finger nuclease.
Chungjung Chou et al.
Angewandte Chemie (International ed. in English), 50(30), 6839-6842 (2011-06-15)
Evolution of amber suppressor tRNAs for efficient bacterial production of proteins containing nonnatural amino acids.
Jiantao Guo et al.
Angewandte Chemie (International ed. in English), 48(48), 9148-9151 (2009-10-27)
Thomas Bridge et al.
Angewandte Chemie (International ed. in English), 58(50), 17986-17993 (2019-10-15)
Antibodies have found applications in several fields, including, medicine, diagnostics, and nanotechnology, yet methods to modulate antibody-antigen binding using an external agent remain limited. Here, we have developed photoactive antibody fragments by genetic site-specific replacement of single tyrosine residues with
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