The nucleotide analog MANT GDP 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.
Specifications
Labeling MethodChemical Labeling, Direct Labeling
Label or DyeMANT (N-Methylanthraniloyl)
Product TypeMANT-GDP
Quantity400 μL
Shipping ConditionWet Ice
Concentration5 mM
Unit SizeEach
Contents & Storage
Store in freezer -5°C to -30°C and protect from light.
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Citations & References
Abstract
Authors:
Journal:
PubMed ID:11063593
The role of Mg2+ cofactor in the guanine nucleotide exchange and GTP hydrolysis reactions of Rho family GTP-binding proteins.
Authors:Zhang B, Zhang Y, Wang Z, Zheng Y
Journal:J Biol Chem
PubMed ID:10843989
'The biological activities of Rho family GTPases are controlled by their guanine nucleotide binding states in cells. Here we have investigated the role of Mg(2+) cofactor in the guanine nucleotide binding and hydrolysis processes of the Rho family members, Cdc42, Rac1, and RhoA. Differing from Ras and Rab proteins, which ... More
Kinetics of Cdc42 membrane extraction by Rho-GDI monitored by real-time fluorescence resonance energy transfer.
Authors:Nomanbhoy TK, Erickson JW, Cerione RA
Journal:Biochemistry
PubMed ID:10026253
'The mechanisms underlying the ability of the Rho-GDP dissociation inhibitor (RhoGDI) to elicit the release of Rho-related GTP-binding proteins from membranes is currently unknown. In this report, we have set out to address this issue by using fluorescence resonance energy transfer approaches to examine the functional interactions of the RhoGDI ... More
Biochemical analysis of SopE from Salmonella typhimurium, a highly efficient guanosine nucleotide exchange factor for RhoGTPases.
'RhoGTPases are key regulators of eukaryotic cell physiology. The bacterial enteropathogen Salmonella typhimurium modulates host cell physiology by translocating specific toxins into the cytoplasm of host cells that induce responses such as apoptotic cell death in macrophages, the production of proinflammatory cytokines, the rearrangement of the host cell actin cytoskeleton ... More
Alanine scan mutagenesis of the switch I domain of the Caulobacter crescentus CgtA protein reveals critical amino acids required for in vivo function.
Authors:Lin B, Skidmore JM, Bhatt A, Pfeffer SM, Pawloski L, Maddock JR
Journal:Mol Microbiol
PubMed ID:11251813
'The Caulobacter crescentus CgtA protein is a member of the Obg/GTP1 subfamily of monomeric GTP-binding proteins. In vitro, CgtA displays moderate affinity for both GDP and GTP and displays rapid exchange rate constants for either nucleotide, indicating that the guanine nucleotide-binding and exchange properties of CgtA are different from those ... More