PDXP recombinant protein

PDXP, 1-296aa, Human, His tag, E Coli

Cat. Num. AAA203739

• Gene Names: PDXP; CIN; PLP; dJ37E16.5
• Applications: SDS-Page
• Purity: > 95% by SDS-PAGE
• Synonyms: PDXP; 1-296aa; Human; His tag; E Coli; Pyridoxal phosphate phosphatase; CIN; PLP; PLPP; PDXP recombinant protein

• Host: E Coli
• Purity/Purification: > 95% by SDS-PAGE
• Form/Format: Liquid. In 20mM Tris-HCl Buffer (pH 8.0) containing 1mM DTT, 20% glycerol, 0.1M NaCl
• Concentration: 1 mg/ml (determined by Bradford assay) (varies by lot)
• Sequence: MGSSHHHHHH SSGLVPRGSH MARCERLRGA ALRDVLGRAQ GVLFDCDGVL WNGERAVPGA PELLERLARA GKAALFVSNN SRRARPELAL RFARLGFGGL RAEQLFSSAL CAARLLRQRL PGPPDAPGAV FVLGGEGLRA ELRAAGLRLA GDPSAGDGAA PRVRAVLVGY DEHFSFAKLR EACAHLRDPE CLLVATDRDP WHPLSDGSRT PGTGSLAAAV ETASGRQALV VGKPSPYMFE CITENFSIDP ARTLMVGDRL ETDILFGHRC GMTTVLTLTG VSRLEEAQAY LAAGQHDLVP HYYVESIADL TEGLED
• Sequence Length: 296

• Applicable Applications for PDXP recombinant protein: SDS-PAGE
• Antigen Species: Human
• Tag Information: His-tag
• Preparation and Storage: Can be stored at 4 degree C short term (1-2 weeks).; For long term storage, aliquot and store at -20 degree C or -70 degree C.; Avoid repeated freezing and thawing cycles.

SDS-Page

Related Product Information for PDXP recombinant protein

Pyridoxal phosphate phosphatase, also known as PDXP is the enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. PDXP catalyzes the dephosphorylation of pyridoxal 5'-phosphate and exhibits a high level of expression various parts of the central nervous system, especially the brain. PDXP activity is catalyzed by haloacid dehalogenase (HAD), and it is the cofactor of both aromatic L-amino acid decarboxylase and glutamate decarboxylase. Recombinant human PDXP protein, fused to His-tag at N-terminus, was expressed in E Coli and purified by using conventional chromatography techniques

Product Categories/Family for PDXP recombinant protein

Metabolism

References

Jang YM., et al. (1992) J Biol Chem. 278 (50):50040-6.; Fonda ML., et al. (1992) J Biol Chem. 267 (22):15978-83.;

NCBI and Uniprot Product Information

• NCBI GI #: 10092677
• NCBI GeneID: 57026
• NCBI Accession #: NP_064711
• NCBI GenBank Nucleotide #: NM_020315.4
• UniProt Accession #: Q96GD0; Q9UGY2
• Molecular Weight: 33.8 kDa (316aa) confirmed by MALDI-TOF
• NCBI Official Full Name: pyridoxal phosphate phosphatase
• NCBI Official Synonym Full Names: pyridoxal phosphatase
• NCBI Official Symbol: PDXP
• NCBI Official Synonym Symbols: CIN; PLP; dJ37E16.5
• NCBI Protein Information: pyridoxal phosphate phosphatase
• UniProt Protein Name: Pyridoxal phosphate phosphatase
• Protein Family: Pyridoxal phosphate phosphatase
• UniProt Gene Name: PDXP
• UniProt Synonym Gene Names: CIN; PLP; PLPP; PLP phosphatase

NCBI Description

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 [PubMed 14522954]).[supplied by OMIM, Mar 2008]

Uniprot Description

Protein serine phosphatase that dephosphorylates 'Ser-3' in cofilin and probably also dephosphorylates phospho-serine residues in DSTN. Regulates cofilin-dependent actin cytoskeleton reorganization. Required for normal progress through mitosis and normal cytokinesis. Does not dephosphorylate phospho-threonines in LIMK1. Does not dephosphorylate peptides containing phospho-tyrosine (PubMed:15580268). 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 (PubMed:14522954).