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Citations & References (75)
Invitrogen™
EnzChek™ Phosphate Assay Kit
The EnzChek™ Phosphate Assay Kit provides a fast and sensitive spectrophotometric method for the quantification of inorganic phosphate in solutionRead more
| Catalog Number | Quantity |
|---|---|
| E6646 | 100 Assays |
Catalog number E6646
Price (CNY)
6,341.00
Each
Quantity:
100 Assays
Price (CNY)
6,341.00
Each
The EnzChek™ Phosphate Assay Kit provides a fast and sensitive spectrophotometric method for the quantification of inorganic phosphate in solution and for phosphate released during ATPase or GTPase enzymatic reactions.Sensitivity of 2 to 150 μM phosphate Spectrophotometric microplate-based assay detects a change in absorbance maximum from 330 nm to 360 nm Continuous monitoring of phosphate generated by ATPase or GTPase activity
See our complete line of Fluorescence Microplate assays.
In the presence of inorganic phosphate, the 2-amino-6-mercapto-7-methylpurine riboside (MESG) substrate is converted by the purine nucleoside phosphorylase (PNP) enzyme to the ribose 1-phosphate and 2-amino-6-mercapto-7-methylpurine product. This enzymatic conversion of MESG results in a spectrophotometric shift in maximum absorbance from 330 nm for the substrate to 360 nm for the product.
Sensitivity of the assay is in the range of 2 to 150 μM inorganic phosphate (2 to 150 nanomoles phosphate in a 1 mL volume), and the reaction can be performed over a pH range of 6.5 to 8.5. The EnzChek™ phosphate reaction is sufficiently fast and quantitative for use in stopped-flow kinetic experiments.
For Research Use Only. Not for use in diagnostic procedures.
Specifications
Detection MethodColorimetric
Dye TypeMESG
FormatTube(s)
Quantity100 Assays
Shipping ConditionRoom Temperature
ColorUltraviolet
For Use With (Application)Phosphate Assay
For Use With (Equipment)Spectrophotometer
Product LineEnzChek
Product TypeEnzChek Assay Kit
Unit SizeEach
Contents & Storage
Store in freezer -5°C to -30°C.
Citations & References (75)
Citations & References
Abstract
Regulation of vascular smooth muscle tone by N-terminal region of caldesmon. Possible role of tethering actin to myosin.
Journal:J Biol Chem
PubMed ID:10652307
'To assess the functional significance of tethering actin to myosin by caldesmon in the regulation of smooth muscle contraction, we investigated the effects of synthetic peptides, containing the myosin-binding sequences in the N-terminal region of caldesmon, on force directly recorded from single permeabilized smooth muscle cells of ferret portal vein.
Reduction precedes cytidylyl transfer without substrate channeling in distinct active sites of the bifunctional CDP-ribitol synthase from Haemophilus influenzae.
Journal:Biochemistry
PubMed ID:11305920
'CDP-ribitol synthase is a bifunctional reductase and cytidylyltransferase that catalyzes the transformation of D-ribulose 5-phosphate, NADPH, and CTP to CDP-ribitol, a repeating unit present in the virulence-associated polysaccharide capsules of Haemophilus influenzae types a and b [Follens, A., et al. (1999) J. Bacteriol. 181, 2001]. In the work described here,
The role of Mg2+ cofactor in the guanine nucleotide exchange and GTP hydrolysis reactions of Rho family GTP-binding proteins.
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
The antibacterial peptide pyrrhocoricin inhibits the ATPase actions of DnaK and prevents chaperone-assisted protein folding.
Journal:Biochemistry
PubMed ID:11258915
'Recently, we documented that the short, proline-rich antibacterial peptides pyrrhocoricin, drosocin, and apidaecin interact with the bacterial heat shock protein DnaK, and peptide binding to DnaK can be correlated with antimicrobial activity. In the current report we studied the mechanism of action of these peptides and their binding sites to
The EntF and EntE adenylation domains of Escherichia coli enterobactin synthetase: sequestration and selectivity in acyl-AMP transfers to thiolation domain cosubstrates.
Journal:Proc Natl Acad Sci U S A
PubMed ID:10688898
'Enterobactin, the tris-(N-(2,3-dihydroxybenzoyl)serine) trilactone siderophore of Escherichia coli, is synthesized by a three-protein (EntE, B, F) six-module nonribosomal peptide synthetase (NRPS). In this work, the 142-kDa four-domain protein EntF was bisected into two double-domain fragments: a 108-kDa condensation and adenylation construct, EntF C-A, and a 37-kDa peptidyl carrier protein (PCP)