Recombinant Human PDXP protein (His tag N-Terminus)
Be the first to review this product! Submit a review
|
(2 Publications)
Recombinant Human PDXP protein (His tag N-Terminus) is a Human Full Length protein, in the 1 to 296 aa range, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE, Mass Spec.
View Alternative Names
CIN, PLP, PLPP, PDXP, Chronophin, Pyridoxal phosphate phosphatase, PLP phosphatase
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human PDXP protein (AB97953)
15% SDS-PAGE showing ab97953 at approximately 33.8kDa (3μg).
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Pyridoxal phosphate phosphatase affects many cellular processes by maintaining the balance of pyridoxal 5'-phosphate levels. This enzyme is essential for the regulation of processes that depend on pyridoxal phosphate as a cofactor including amino acid metabolism neurotransmitter synthesis and lipid metabolism. It functions independently rather than being part of a large protein complex allowing its activity to directly influence the availability of pyridoxal phosphate for biochemical reactions.
Pathways
The role of pyridoxal phosphate phosphatase spans significant metabolic pathways such as the amino acid catabolic pathway. Here it functions alongside enzymes that require pyridoxal 5'-phosphate for activity including transaminases and decarboxylases. Additionally PDXP interacts with proteins like pyridoxal kinase which phosphorylates pyridoxal to replenish PLP maintaining the balance between synthesis and degradation in the metabolic flux.
Specifications
Form
Liquid
Additional notes
ab97953 is purified using conventional chromatography techniques.
General info
Function
Functions as a pyridoxal phosphate (PLP) phosphatase, which also catalyzes the dephosphorylation of pyridoxine 5'-phosphate (PNP) and pyridoxamine 5'-phosphate (PMP), with order of substrate preference PLP > PNP > PMP and therefore plays a role in vitamin B6 metabolism (PubMed : 14522954, PubMed : 8132548). Also functions as a protein serine phosphatase that specifically dephosphorylates 'Ser-3' in proteins of the actin-depolymerizing factor (ADF)/cofilin family like CFL1 and DSTN. Thereby, regulates cofilin-dependent actin cytoskeleton reorganization, being required for normal progress through mitosis and normal cytokinesis. Does not dephosphorylate phosphothreonines in LIMK1. Does not dephosphorylate peptides containing phosphotyrosine (PubMed : 15580268).
Sequence similarities
Belongs to the HAD-like hydrolase superfamily.
Subcellular localisation
Cytoskeleton
Target data
Publications (2)
Recent publications for all applications. Explore the full list and refine your search
Cell death & disease 12:37 PubMed33414453
2021
Applications
Unspecified application
Species
Unspecified reactive species
Experimental neurology 331:113383 PubMed32561413
2020
Applications
Unspecified application
Species
Unspecified reactive species
Product promise
Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.
For licensing inquiries, please contact partnerships@abcam.com