DiFMUP (6,8-Difluoro-4-Methylumbelliferyl Phosphate)
DiFMUP (6,8-Difluoro-4-Methylumbelliferyl Phosphate)
Invitrogen™

DiFMUP (6,8-Difluoro-4-Methylumbelliferyl Phosphate)

DiFMUP is a fluorinated 4-methylumbelliferyl phosphate (MUP) derivative that has a lower pKa than that of MUP, making DiFMUP anRead more
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Catalog NumberQuantity
D65675mg
D2206510 x 10mg
Catalog number D6567
Price (KRW)
255,000
キャンペーン価格
Ends: 31-Dec-2025
300,000
Save 45,000 (15%)
Each
Add to cart
Quantity:
5mg
Price (KRW)
255,000
キャンペーン価格
Ends: 31-Dec-2025
300,000
Save 45,000 (15%)
Each
Add to cart
DiFMUP is a fluorinated 4-methylumbelliferyl phosphate (MUP) derivative that has a lower pKa than that of MUP, making DiFMUP an excellent substrate for continuously assaying acid phosphatases at low pH. The reaction product of DiFMUP has excitation/emission maxima of ∼358/450 nm. DiFMUP is also available packaged in ten vials of 10 mg each (D-22065).
For Research Use Only. Not for use in diagnostic procedures.
Specifications
ColorBlue
Excitation/Emission358⁄455
For Use With (Equipment)Microplate Reader
Label or DyeDiFMU
Quantity5mg
Shipping ConditionRoom Temperature
SubstratePhosphatase Substrate
Detection MethodFluorescence
FormPowder
Substrate PropertiesChemical Substrate
Target EnzymePhosphatases
Unit SizeEach
Contents & Storage
Store in freezer (-5 to -30°C).

Citations & References (33)

Citations & References
Abstract
Surface phosphophilicity of aluminum-containing adjuvants probed by their efficiency for catalyzing the P--O bond cleavage with chromogenic and fluorogenic substrates.
Authors:Zhao Q, Sitrin R
Journal:Anal Biochem
PubMed ID:11476547
'Aluminum-containing adjuvants are widely used in a variety of vaccine products, such as recombinant proteins, virus-like particles, conjugated polysaccharides, and recently DNA vaccines. Aluminum-containing adjuvants are also known to have a high affinity to inorganic phosphate and its mono- or diesters. Since phosphate groups are present in many antigens as ... More
Negative regulation of EGFR signalling through integrin-alpha1beta1-mediated activation of protein tyrosine phosphatase TCPTP.
Authors:Mattila E, Pellinen T, Nevo J, Vuoriluoto K, Arjonen A, Ivaska J
Journal:Nat Cell Biol
PubMed ID:15592458
'Integrin-mediated cell adhesion regulates a multitude of cellular responses, including proliferation, survival and cross-talk between different cellular signalling pathways. So far, integrins have been mainly shown to convey permissive signals enabling anchorage-dependent receptor tyrosine kinase signalling. Here we show that a collagen-binding integrin alpha(1)beta(1) functions as a negative regulator of ... More
Discovery of a novel shp2 protein tyrosine phosphatase inhibitor.
Authors:Chen L, Sung SS, Yip ML, Lawrence HR, Ren Y, Guida WC, Sebti SM, Lawrence NJ, Wu J
Journal:Mol Pharmacol
PubMed ID:16717135
'Shp2 is a nonreceptor protein tyrosine phosphatase (PTP) encoded by the PTPN11 gene. It is involved in growth factorinduced activation of mitogen-activated protein (MAP) kinases Erk1 and Erk2 (Erk1/2) and has been implicated in the pathogenicity of the oncogenic bacterium Helicobacter pylori. Moreover, gain-of-function Shp2 mutations have been found in ... More
Loss of phosphatase activity in Ptp69D alleles supporting axon guidance defects.
Authors:Marlo JE, Desai CJ
Journal:J Cell Biochem
PubMed ID:16514605
'PTP69D is a receptor protein tyrosine phosphatase that was identified as a key regulator of neuromuscular axon guidance in Drosophila, and has subsequently been shown to play a similar role in the central nervous system and retina. Three Ptp69D alleles with mutations involving catalytically important residues exhibit a high degree ... More
High yield expression of serine/threonine protein phosphatase type 5, and a fluorescent assay suitable for use in the detection of catalytic inhibitors.
Authors:Ni L, Swingle MS, Bourgeois AC, Honkanen RE,
Journal:Assay Drug Dev Technol
PubMed ID:17939754
'Protein phosphatase type 5 (PP5) belongs to the PPP family of serine/threonine protein phosphatases and is expressed in most, if not all, human tissues. Although the physiological roles played by PP5 are not yet clear, PP5 is found in association with several proteins that influence intracellular signaling networks initiated by ... More