catalog number :
MBS9424162
products type :
Recombinant Protein
products full name :
Recombinant Human Pyridoxal phosphate phosphatase (PDXP)
products short name :
[Pyridoxal phosphate phosphatase (PDXP)]
other names :
[pyridoxal phosphate phosphatase; Pyridoxal phosphate phosphatase; pyridoxal phosphate phosphatase; pyridoxal phosphatase; Chronophin]
products gene name :
[PDXP]
other gene names :
[PDXP; PDXP; CIN; PLP; dJ37E16.5; CIN; PLP; PLPP; PLP phosphatase]
sequence positions :
[Full Length, 1-296aa]
sequence :
MARCERLRGAALRDVLGRAQGVLFDCDGVLWNGERAVPG
APELLERLARAGKAALFVSNNSRRARPELALRFARLGFG
GLRAEQLFSSALCAARLLRQRLPGPPDAPGAVFVLGGEG
LRAELRAAGLRLAGDPSAGDGAAPRVRAVLVGYDEHFSF
AKLREACAHLRDPECLLVATDRDPWHPLSDGSRTPGTGS
LAAAVETASGRQALVVGKPSPYMFECITENFSIDPARTL
MVGDRLETDILFGHRCGMTTVLTLTGVSRLEEAQAYLAA
GQHDLVPHYYVESIADLTEGLED
purity :
Greater than 90% as determined by SDS-PAGE.
form :
Tris-based buffer, 50% glycerol
storage stability :
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20 degree C/-80 degree C. The shelf life of lyophilized form is 12 months at -20 degree C/-80 degree C.
image1 heading :
SDS-PAGE
other info1 :
Target Name: PDXP
other info2 :
Tag Info: N-terminal 6xHis-tagged
products 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. Pyridoxal phosphate phosphatase. Has some activity towards pyridoxal 5'-phosphate (PLP), pyridoxine 5'-phosphate (PMP) and pyridoxine 5'-phosphate (PNP), with a highest activity with PLP followed by PNP.
ncbi acc num :
NP_064711.1
ncbi gb acc num :
NM_020315.4
ncbi mol weight :
33.7 kDa
ncbi summary :
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 summary :
PDXP: 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. Pyridoxal phosphate phosphatase. Has some activity towards pyridoxal 5'-phosphate (PLP), pyridoxine 5'-phosphate (PMP) and pyridoxine 5'-phosphate (PNP), with a highest activity with PLP followed by PNP. Homodimer. Ubiquitous. Highly expressed in all the regions of central nerve system except the spinal cord. Also expressed at high level in liver and testis. In fetus, it is weakly expressed in all organs except brain. Inhibited by NaF, Zn(2+), Ca(2+), Mn(2+) and EDTA. Belongs to the HAD-like hydrolase superfamily. Protein type: Cell cycle regulation; Cofactor and Vitamin Metabolism - vitamin B6; EC 3.1.3.3; EC 3.1.3.74; Protein phosphatase, Ser/Thr (non-receptor). Chromosomal Location of Human Ortholog: 22q13.1. Cellular Component: actin cytoskeleton; cleavage furrow; cytosol; lamellipodium; midbody; plasma membrane. Molecular Function: heat shock protein binding; magnesium ion binding; phosphoprotein phosphatase activity; protein binding; pyridoxal phosphatase activity. Biological Process: actin rod formation; positive regulation of actin filament depolymerization; protein amino acid dephosphorylation; pyridoxal phosphate catabolic process; regulation of cytokinesis; regulation of mitosis