추천 제품
분석
≥95% (HPLC)
Quality Level
양식
solid
반응 적합성
reaction type: click chemistry
solubility
10 mM Tris-HCl, pH 7.5: soluble
배송 상태
wet ice
저장 온도
−20°C
SMILES string
O[C@@H]([C@H]1O)[C@@H](COP(O)(OP(O)(OP(O)(O)=O)=O)=O)O[C@@H]1N2C=NC3=C2N=CN=C3NCC#C
InChI
1S/C13H18N5O13P3/c1-2-3-14-11-8-12(16-5-15-11)18(6-17-8)13-10(20)9(19)7(29-13)4-28-33(24,25)31-34(26,27)30-32(21,22)23/h1,5-7,9-10,13,19-20H,3-4H2,(H,24,25)(H,26,27)(H,14,15,16)(H2,21,22,23)/t7-,9-,10-,13?/m1/s1
InChI key
MUOIWXPACQCYQC-RJNFYWFKSA-N
애플리케이션
N6-Propargyl-ATP is suitable for in vitro AMPylation of proteins as well as in vitro polyadenylation of RNA. The resulting alkyne-functionalized protein or RNA can be processed using Cu(I)-catalyzed click chemistry to attach azide-labeled molecules. This gives options such as introduction of a biotin group for purification tasks, introduction of a fluorescent group for detection, or crosslinking to other azide-functionalized biomolecules.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
이미 열람한 고객
Journal of the American Chemical Society, 133(43), 17103-17105 (2011-09-29)
Protein AMPylation is an emerging post-translational modification, which plays key roles in bacterial pathogenesis and cell biology. Enzymes with AMPylation activity, referred to as AMPylators, have been identified in several bacterial pathogens and eukaryotes. To facilitate the study of this
A new chemical handle for protein AMPylation at the host-pathogen interface.
Chembiochem : a European journal of chemical biology, 13(2), 183-185 (2012-01-04)
Chembiochem : a European journal of chemical biology, 13(8), 1112-1115 (2012-04-20)
A versatile "clickable" nucleoside: Metabolic labeling of cells is useful in studying the dynamics of biological molecules. N(6) pA can be utilized by all three mammalian RNA polymerases, as well as poly(A) polymerase. Because of its alkyne modification, RNA labeled
Nucleic acids research, 47(17), e102-e102 (2019-07-19)
Terminal deoxynucleotidyl transferase (TdT), which mediates template-independent polymerization with low specificity for nucleotides, has been used for nucleotide extension of DNA oligomers. One concern is that it is difficult to control the number of incorporated nucleotides, which is a limitation
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