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Citações e referências (82)
Invitrogen™
MANT-ATP (2'-(or-3')-O-(N-Methylanthraniloyl) Adenosine 5'-Triphosphate, Trisodium Salt)
The nucleotide analog MANT ATP is modified on the ribose moiety. The compact mature of the MANT fluorophore and itsLeia mais
| Número do catálogo | Quantity |
|---|---|
| M12417 | 400 μL |
Número do catálogo M12417
Preço (BRL)
3.512,60
Each
Quantity:
400 μL
Preço (BRL)
3.512,60
Each
The nucleotide analog MANT ATP is modified on the ribose moiety. The compact mature of the MANT fluorophore and its attachment position results in nucleotide analogs that induce minimal perturbation of nucleotide-protein interactions. Because MANT fluorescence is sensitive to the environment of the fluorophore, nucleotide-protein interactions may be directly detectable. MANT nucleotides are valuable probes of the structure and enzymatic activity of nucleotide-binding proteins.
For Research Use Only. Not for use in diagnostic procedures.
Especificações
Label or DyeMANT (N-Methylanthraniloyl)
Product TypeMANT-ATP
Quantity400 μL
Shipping ConditionWet Ice
Concentration5 mM
Unit SizeEach
Conteúdo e armazenamento
Store in freezer -5°C to -30°C and protect from light.
Citações e referências (82)
Citações e referências
Abstract
Journal:
PubMed ID:11063593
A mechanistic model for Ncd directionality.
Journal:J Biol Chem
PubMed ID:11278404
Ncd is a kinesin-related protein that drives movement to the minus-end of microtubules. Pre-steady-state kinetic experiments have been employed to investigate the cooperative interactions between the motor domains of the MC1 dimer and to establish the ATPase mechanism. Our results indicate that the active sites of dimeric Ncd free in
Moving a microtubule may require two heads: a kinetic investigation of monomeric Ncd.
Journal:Biochemistry
PubMed ID:10684615
'Ncd is a minus-end-directed microtubule motor and a member of the kinesin superfamily. The Ncd dimer contains two motor domains, and cooperative interactions between the heads influence the interactions of each respective motor domain with the microtubule. The approach we have taken to understand the cooperativity between the two motor
Interactions of nucleotide cofactors with the Escherichia coli replication factor DnaC protein.
Journal:Biochemistry
PubMed ID:11041861
'Quantitative analyses of the interactions of nucleotide cofactors with the Escherichia coli replicative factor DnaC protein have been performed using thermodynamically rigorous fluorescence titration techniques. This approach allowed us to obtain stoichiometries of the formed complexes and interaction parameters, without any assumptions about the relationship between the observed signal and
The sequence of the myosin 50-20K loop affects Myosin's affinity for actin throughout the actin-myosin ATPase cycle and its maximum ATPase activity.
Journal:Biochemistry
PubMed ID:10090768
'We are interested in the role that solvent-exposed, proteolytically sensitive surface loops play in myosin function. The 25-50K loop, or loop 1, is near the ATP binding site, while the 50-20K loop (loop 2) is in the actin binding site. Through chimeric studies, we have found that loop 1 affects