E1158
EPHB3 (585-end), active, GST tagged human
PRECISIO® Kinase, recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution
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Synonym(s):
Cek10, ETK2, HEK2, Mdk5, TYRO6
UNSPSC Code:
12352200
NACRES:
NA.32
recombinant
expressed in baculovirus infected Sf9 cells
Quality Level
product line
PRECISIO® Kinase
Assay
≥70% (SDS-PAGE)
form
buffered aqueous glycerol solution
specific activity
22-30 nmol/min·mg
mol wt
~68 kDa
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... EPHB3(2049)
Biochem/physiol Actions
EPHB3 is a member of the Ephrin receptor family and is expressed during embryonic development in multiple regions of the central nervous system. In adult brain, EPHB3 is expressed in the cerebellum, raphe pallidus, hippocampus, entorhinal cortex, and both motor and sensory cortices. EPHB3 is involved in the maintenance of mature neuronal connections and/or re-arrangement of synaptic connections during late stages of development. EPHB3 plays a role in the regulation of cell adhesion and migration, and the catalytic activity of EPHB3 is required for inhibition of integrin-mediated cell adhesion.
Physical form
Supplied in 50 mM Tris-HCl, pH 7.5, with 150 mM NaCl, 0.2 5mM DTT, 0.1 mM EGTA, 0.1 mM EDTA, 0.1 mM PMSF, and 25% glycerol.
Legal Information
PRECISIO is a registered trademark of Merck KGaA, Darmstadt, Germany
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
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Christopher A Willson et al.
Journal of molecular histology, 37(8-9), 369-380 (2006-11-15)
Eph receptors and ligands are two families of proteins that control axonal guidance during development. Their expression was originally thought to be developmentally regulated but recent work has shown that several EphA receptors are expressed postnatally. The EphB3 receptors are
Hui Miao et al.
The Journal of biological chemistry, 280(2), 923-932 (2004-11-13)
Genetic studies have shown that Eph receptor tyrosine kinases have both kinase-dependent and kinase-independent functions through incompletely understood mechanisms. We report here that ephrin-B1 stimulation of endogenous EphB kinases in LS174T colorectal epithelial cells inhibited integrin-mediated adhesion and HGF/SF-induced directional
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