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Pyridoxal 5-prime-phosphate (PLP) is the active form of vitamin B6 that acts as a coenzyme in maintaining biochemical homeostasis. Additionally we are shipping PDXP Antibodies (28) and PDXP Proteins (9) and many more products for this protein.
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In non-adherent glioblastoma cell lines cultured in serum-free medium, chronophin knockdown induces phenotypic changes, e.g. in colony formation and transcription, but these are highly dependent on the cellular background. CIN knockdown in the glioblastoma cell lines NCH421k and NCH644 increased active vitamin B6 levels.
Chronophin has a role in coordinating cell leading edge dynamics by controlling active cofilin levels
Splicing of SH3BP1 and CIN gene loci produces the novel brain specific splice variant BGIN.
analysis of pyridoxal phosphatase cloning, expression and tissue distribution
We report the biochemical isolation of chronophin (CIN), a unique cofilin-activating phosphatase of the haloacid dehalogenase (HAD) superfamily and an important novel regulator of cofilin-mediated actin reorganization.
analysis of brain pyridoxal-5'-phosphate phosphatase
Results suggest that the transduction of the PEP-1-PLPP fusion protein can be one mode of PLP level regulation, and to replenish this enzyme in the various neurological disorders related to vitamin B(6).
Study demonstrates the ATP-sensitive interaction of the cofilin phosphatase chronophin (CIN) with the chaperone hsp90 to form a biosensor that mediates cofilin/actin rod formation.
Results provided novel evidence that PLPP is involved in controlling dendritic spine as well as synaptic plasticity. It showed also for the first time the role of PLPP in GluN functionality via regulation of GluN2A interaction with postsynaptic proteins. These findings suggest that PLPP/CIN may play an important role in information storage and recall capacity, which manifests as a learning memory.
Evolutionary and structural analyses of mammalian haloacid dehalogenase-type phosphatases AUM and chronophin provide insight into the basis of their different substrate specificities.
Dimer formation is essential for an intermolecular arginine-arginine-tryptophan stacking interaction that positions a critical histidine residue in the substrate specificity loop of chronophin for PLP coordination.
Pyridoxal 5-prime-phosphate (PLP) is the active form of vitamin B6 that acts as a coenzyme in maintaining biochemical homeostasis. The preferred degradation route from PLP to 4-pyridoxic acid involves the dephosphorylation of PLP by PDXP (Jang et al., 2003
, pyridoxal phosphate phosphatase
, pyridoxal phosphatase
, reg I binding protein I
, reg I-binding protein 1