Search
Citations & References (6)
Invitrogen™
RediPlate™ 96 EnzChek™ Tyrosine Phosphatase Assay Kit
The RediPlate 96 EnzChek Tyrosine Phosphatase Assay Kit is a ready-to-use, fluorescence-based microplate assay for detecting tyrosine phosphatases (PTPase) andRead more
| Catalog Number | Quantity |
|---|---|
| R22067 | 1 x 96-well plate |
Catalog number R22067
Price (BRL)
-
Quantity:
1 x 96-well plate
The RediPlate 96 EnzChek Tyrosine Phosphatase Assay Kit is a ready-to-use, fluorescence-based microplate assay for detecting tyrosine phosphatases (PTPase) and their corresponding modulators and inhibitors. Each RediPlate 96-well microplate has removable lanes, enabling researchers to perform only as many assays as needed for each experiment or to perform high-throughput analysis.
For Research Use Only. Not for use in diagnostic procedures.
Specifications
Detection MethodFluorescence Intensity
Dye TypeDiFMU
Quantity1 x 96-well plate
Shipping ConditionRoom Temperature
SubstrateDiFMUP
Substrate PropertiesChemical Substrate
Substrate TypePhosphatase Substrate
Target EnzymeTyrosine Phosphatases
Emission358/452
For Use With (Application)Phosphatase Assay
For Use With (Equipment)Microplate Reader
Product LineEnzChek
Product TypePhosphatase Assay
Unit SizeEach
Contents & Storage
Store in freezer -5°C to -30°C and protect from light.
Citations & References (6)
Citations & References
Abstract
Negative regulation of EGFR signalling through integrin-alpha1beta1-mediated activation of protein tyrosine phosphatase TCPTP.
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
Differential coupling of M1 muscarinic and alpha7 nicotinic receptors to inhibition of pemphigus acantholysis.
Journal:J Biol Chem
PubMed ID:18073210
'The mechanisms mediating and regulating assembly and disassembly of intercellular junctions is a subject of intensive research. The IgG autoantibodies produced in patients with the immunoblistering skin disease pemphigus vulgaris (PV) can induce keratinocyte (KC) dyshesion (acantholysis) via mechanisms that involve signaling kinases targeting intercellular adhesion molecules, thus providing a
Protein tyrosine phosphatase: enzymatic assays.
Journal:Methods
PubMed ID:15588980
Activity assays for tyrosine phosphatases are based on the hydrolysis of a arylphosphate moiety from a synthetic substrate yielding a spectroscopically active product. Many different substrates can be used for these assays with p-nitrophenyl phosphate (pNPP), fluorescein diphosphate (FDP), and 6,8-difluoro-4-methylumbellyferyl phosphate (DiFMUP) being the most efficient and versatile. Equally,
Chaperone release and unfolding of substrates in type III secretion.
Journal:Nature
PubMed ID:16208377
Type III protein secretion systems are essential virulence factors of many bacteria pathogenic to humans, animals and plants. These systems mediate the transfer of bacterial virulence proteins directly into the host cell cytoplasm. Proteins are thought to travel this pathway in a largely unfolded manner, and a family of customized
Development of fluorescence-based selective assays for serine/threonine and tyrosine phosphatases.
Journal:Comb Chem High Throughput Screen
PubMed ID:12769677
A number of aromatic substrates were evaluated for their ability to detect tyrosine phosphatase and serine/threonine phosphatase activity. Results demonstrated that the fluorinated coumarin DiFMUP is the most sensitive substrate for detecting LAR and PP-2A activity. Using this substrate, selective high-throughput screening assays for serine/threonine and tyrosine phosphatases were developed.