Recombinant Mouse PDXP Protein (Tagged)

Beta LifeScience SKU/CAT #: BLA-10011P

Recombinant Mouse PDXP Protein (Tagged)

Beta LifeScience SKU/CAT #: BLA-10011P
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

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Product Overview

Host Species Mouse
Accession P60487
Synonym Chronophin CIN Pdxp PLP PLP phosphatase PLPP PLPP_HUMAN Pyridoxal (pyridoxine, vitamin B6) phosphatase Pyridoxal phosphate phosphatase Rbp1 Reg I binding protein 1 RP1 37E16.5
Description Recombinant Mouse PDXP Protein (Tagged) was expressed in E.coli. It is a Full length protein
Source E.coli
AA Sequence MARCERLRGAALRDVLGQAQGVLFDCDGVLWNGERIVPGAPELLQRLARA GKNTLFVSNNSRRARPELALRFARLGFAGLRAEQLFSSALCAARLLRQRL SGPPDASGAVFVLGGEGLRAELRAAGLRLAGDPGEDPRVRAVLVGYDEQF SFSRLTEACAHLRDPDCLLVATDRDPWHPLSDGSRTPGTGSLAAAVETAS GRQALVVGKPSPYMFQCITEDFSVDPARTLMVGDRLETDILFGHRCGMTT VLTLTGVSSLEEAQAYLTAGQRDLVPHYYVESIADLMEGLED
Molecular Weight 48 kDa including tags
Purity >90% SDS-PAGE.
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Formulation Liquid Solution
Stability The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution See related COA
Unit Definition For Research Use Only
Storage Buffer Shipped at 4°C. Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.

Target Details

Target 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. 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.
Subcellular Location Cytoplasm, cytosol. Cytoplasm, cytoskeleton. Cell projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection, lamellipodium membrane; Peripheral membrane protein; Cytoplasmic side. Cell membrane; Peripheral membrane protein; Cytoplasmic side.
Protein Families HAD-like hydrolase superfamily
Database References
Tissue Specificity Ubiquitous. highly expressed in brain (at protein level).

Gene Functions References

  1. Results provided novel evidence that PLPP is involved in controlling dendritic spine as well as synaptic plasticity. It showed also for the first time the role of PLPP in GluN functionality via regulation of GluN2A interaction with postsynaptic proteins. These findings suggest that PLPP/CIN may play an important role in information storage and recall capacity, which manifests as a learning memory. PMID: 27212638
  2. Evolutionary and structural analyses of mammalian haloacid dehalogenase-type phosphatases AUM and chronophin provide insight into the basis of their different substrate specificities. PMID: 24338473
  3. Dimer formation is essential for an intermolecular arginine-arginine-tryptophan stacking interaction that positions a critical histidine residue in the substrate specificity loop of chronophin for PLP coordination. PMID: 24338687
  4. analysis of pyridoxal phosphatase cloning, expression and tissue distribution PMID: 14522954

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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