PLP phosphatase Protein, Mouse (P.pastoris, His)

The PLP phosphatase protein plays a dual role as a pyridoxal phosphate (PLP) phosphatase and a protein serine phosphatase. Its enzymatic activity in vitamin B6 metabolism involves the dephosphorylation of PLP, PNP and PMP. PLP phosphatase Protein, Mouse (P.pastoris, His) is the recombinant mouse-derived PLP phosphatase protein, expressed by P. pastoris , with N-His labeled tag. The total length of PLP phosphatase Protein, Mouse (P.pastoris, His) is 292 a.a., with molecular weight of ~33.5 kDa.

PLP phosphatase protein serves a dual function by acting as a pyridoxal phosphate (PLP) phosphatase, catalyzing the dephosphorylation of pyridoxine 5'-phosphate (PNP) and pyridoxamine 5'-phosphate (PMP) with a substrate preference order of PLP > PNP > PMP. This dual enzymatic activity positions it as a key player in vitamin B6 metabolism. Additionally, PLP phosphatase functions as a protein serine phosphatase, specifically targeting 'Ser-3' in proteins of the actin-depolymerizing factor (ADF)/cofilin family, including CFL1 and DSTN. This regulation of cofilin-dependent actin cytoskeleton reorganization is crucial for normal progression through mitosis and cytokinesis. Notably, PLP phosphatase does not dephosphorylate phosphothreonines in LIMK1, and it does not act on peptides containing phosphotyrosine. The multifaceted role of PLP phosphatase highlights its importance in both vitamin B6 metabolism and the dynamic regulation of the actin cytoskeleton, contributing to essential cellular processes.

Mouse

P. pastoris

N-His

P60487 (1M-292D)

57028  [NCBI]

MARCERLRGAALRDVLGQAQGVLFDCDGVLWNGERIVPGAPELLQRLARAGKNTLFVSNNSRRARPELALRFARLGFAGLRAEQLFSSALCAARLLRQRLSGPPDASGAVFVLGGEGLRAELRAAGLRLAGDPGEDPRVRAVLVGYDEQFSFSRLTEACAHLRDPDCLLVATDRDPWHPLSDGSRTPGTGSLAAAVETASGRQALVVGKPSPYMFQCITEDFSVDPARTLMVGDRLETDILFGHRCGMTTVLTLTGVSSLEEAQAYLTAGQRDLVPHYYVESIADLMEGLED

Approximately 33.5 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.