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AB97953

Recombinant Human PDXP protein (His tag N-Terminus)

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(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

1 Images
SDS-PAGE - Recombinant Human PDXP protein (AB97953)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human PDXP protein (AB97953)

15% SDS-PAGE showing ab97953 at approximately 33.8kDa (3μg).

Key facts

Purity

>95% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE, Mass Spec

applications

Biologically active

No

Accession

Q96GD0

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 20% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.316% Tris HCl, 0.0154% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "Mass Spec": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMARCERLRGAALRDVLGRAQGVLFDCDGVLWNGERAVPGAPELLERLARAGKAALFVSNNSRRARPELALRFARLGFGGLRAEQLFSSALCAARLLRQRLPGPPDAPGAVFVLGGEGLRAELRAAGLRLAGDPSAGDGAAPRVRAVLVGYDEHFSFAKLREACAHLRDPECLLVATDRDPWHPLSDGSRTPGTGSLAAAVETASGRQALVVGKPSPYMFECITENFSIDPARTLMVGDRLETDILFGHRCGMTTVLTLTGVSRLEEAQAYLAAGQHDLVPHYYVESIADLTEGLED","proteinLength":"Full Length","predictedMolecularWeight":"33.8 kDa","actualMolecularWeight":null,"aminoAcidEnd":296,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"Q96GD0","tags":[{"tag":"His","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

The protein pyridoxal phosphate phosphatase also known as PDXP serves as an important enzyme in the regulation of vitamin B6 bioavailability. It carries a mass of approximately 32 kDa. PDXP dephosphorylates pyridoxal 5'-phosphate (PLP) which is the active form of vitamin B6 to pyridoxal (PL). Primarily the expression of PDXP occurs in the cytoplasm and has been detected in various tissues such as brain and liver suggesting its diverse role across different biological systems.
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.

Pyridoxal phosphate phosphatase dysregulation can influence neurological and metabolic disorders. For instance altered PDXP activity has been connected to neurological conditions such as epilepsy where it may affect neurotransmitter levels due to insufficient pyridoxal phosphate. Furthermore mutations in genes related to PDXP or its interacting partners such as pyridoxal kinase could contribute to metabolic syndromes due to disrupted vitamin B6 homeostasis.

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

Product protocols

Target data

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).
See full target information PDXP

Publications (2)

Recent publications for all applications. Explore the full list and refine your search

Cell death & disease 12:37 PubMed33414453

2021

PLPP/CIN-mediated NF2-serine 10 dephosphorylation regulates F-actin stability and Mdm2 degradation in an activity-dependent manner.

Applications

Unspecified application

Species

Unspecified reactive species

Ji-Eun Kim,Duk-Shin Lee,Tae-Hyun Kim,Hana Park,Min-Ju Kim,Tae-Cheon Kang

Experimental neurology 331:113383 PubMed32561413

2020

PLPP/CIN-mediated Mdm2 dephosphorylation increases seizure susceptibility via abrogating PSD95 ubiquitination.

Applications

Unspecified application

Species

Unspecified reactive species

Ji-Eun Kim,Duk-Shin Lee,Tae-Hyun Kim,Hana Park,Min-Ju Kim,Tae-Cheon Kang
View all publications

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