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Citations & References (37)
Invitrogen™
MUP (4-Methylumbelliferyl Phosphate, Free Acid)
MUP is a fluorescent substrate for alkaline phosphatases. Alkaline phosphatase mediated hydrolysis of its phosphate substituent yields the blue-fluorescent 4-methylumbelliferylRead more
| Catalog Number | Quantity |
|---|---|
| M6491 | 1 g |
Catalog number M6491
Price (MXN)
-
Quantity:
1 g
MUP is a fluorescent substrate for alkaline phosphatases. Alkaline phosphatase mediated hydrolysis of its phosphate substituent yields the blue-fluorescent 4-methylumbelliferyl (excitation/emission ∼386/448 nm).
For Research Use Only. Not for use in diagnostic procedures.
Specifications
Excitation/Emission360⁄449
For Use With (Equipment)Fluorometer, Microplate Reader
Label or DyeMUP (4-methylumbelliferyl phosphate)
Quantity1 g
Shipping ConditionRoom Temperature
SubstratePhosphatase Substrate
Detection MethodFluorescence
FormPowder
Substrate PropertiesChemical Substrate
Target EnzymeAlkaline Phosphatase
Unit SizeEach
Contents & Storage
Store in freezer (-5 to -30°C).
Citations & References (37)
Citations & References
Abstract
Enzyme-linked immunosorbent assay for an octapeptide based on a genetically engineered fusion protein.
Journal:Anal Chem
PubMed ID:8503503
Traditional chemical means of preparing enzyme-ligand conjugates for use in enzyme-linked immunosorbent assays (ELISAs) lead to the production of multisubstituted enzyme-ligand conjugates with a high degree of variability in the site of ligand attachment. A genetically engineered fusion protein was prepared in order to investigate the feasibility of controlled production
Rapid characterisation and identification of mycobacteria using fluorogenic enzyme tests.
Journal:Zentralbl Bakteriol
PubMed ID:8061408
'Sixty representatives of selected Mycobacterium and Nocardia species were examined for their ability to cleave 79 fluorogenic synthetic enzyme substrates based on the fluorophores 7-amino-4-methylcoumarin and 4-methylumbelliferone. The resultant data were analysed using the simple matching coefficient and clustering achieved using the unweighted pair group method with arithmetic averages algorithm.
Fluorogenic selective and differential medium for isolation of fecal streptococci.
Journal:Appl Environ Microbiol
PubMed ID:6830220
'Of 44 fluorogenic substrates tested for their ability to differentiate species of fecal streptococci, four yielded species-differentiating reactions. The remaining substrates either yielded uniformly positive, negative, or variable strain-dependent reactions. One substrate, 4-methylumbelliferone-alpha-D-galactoside, was hydrolyzed by Streptococcus bovis and S. faecium and its biotypes. 4-Methylumbelliferone-alpha-D-galactoside and a colorimetric starch substrate
Enhanced sensitivity and precision in an enzyme-linked immunosorbent assay with fluorogenic substrates compared with commonly used chromogenic substrates.
Journal:Anal Biochem
PubMed ID:16137635
'Quantitative enzyme-linked immunosorbent assay (ELISA) is a widely used tool for analyzing biopharmaceutical and vaccine products. The superior sensitivity of the ELISA format is conferred by signal amplification through the enzymatic oxidation or hydrolysis of substrates to products with enhanced color or fluorescence. The extinction coefficient for a colored product
Sensitive fluorogenic enzyme immunoassay on nitrocellulose membranes for quantitation of virus.
Journal:J Virol Methods
PubMed ID:3146582
'A highly sensitive fluorogenic enzyme-linked immunosorbent assay (FELISA), which utilizes nitrocellulose membranes as solid phase support, has been developed for the detection and identification of virus in clinical samples. Reagents were standardized and, using purified Newcastle disease virus (NDV) as a model, the theoretical lower limits of test sensitivity of