Recombinant Human PDXP Protein

Name: Recombinant Human PDXP Protein
Brand: Beta LifeScience
SKU: BLA-6827P
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Host Species	Human
Accession	Q96GD0
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 Human PDXP Protein was expressed in E.coli. It is a Full length protein
Source	E.coli
AA Sequence	MGSSHHHHHHSSGLVPRGSHMARCERLRGAALRDVLGRAQGVLFDCDGVL WNGERAVPGAPELLERLARAGKAALFVSNNSRRARPELALRFARLGFGGL RAEQLFSSALCAARLLRQRLPGPPDAPGAVFVLGGEGLRAELRAAGLRLA GDPSAGDGAAPRVRAVLVGYDEHFSFAKLREACAHLRDPECLLVATDRDP WHPLSDGSRTPGTGSLAAAVETASGRQALVVGKPSPYMFECITENFSIDP ARTLMVGDRLETDILFGHRCGMTTVLTLTGVSRLEEAQAYLAAGQHDLVP HYYVESIADLTEGLED
Molecular Weight	34 kDa including tags
Purity	>95% purity as determined by 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 and store at -20°C or -80°C. Avoid repeated 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	HGNC: 30259 OMIM: 609246 KEGG: hsa:57026 STRING: 9606.ENSP00000215904 UniGene: Hs.632762
Tissue Specificity	Ubiquitously expressed (at protein level). 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.

Gene Functions References

Chronophin has a role in coordinating cell leading edge dynamics by controlling active cofilin levels PMID: 26324884
Splicing of SH3BP1 and CIN gene loci produces the novel brain specific splice variant BGIN. PMID: 23223568
analysis of pyridoxal phosphatase cloning, expression and tissue distribution PMID: 14522954
We report the biochemical isolation of chronophin (CIN), a unique cofilin-activating phosphatase of the haloacid dehalogenase (HAD) superfamily and an important novel regulator of cofilin-mediated actin reorganization. PMID: 15580268
analysis of brain pyridoxal-5'-phosphate phosphatase PMID: 16336786
Results suggest that the transduction of the PEP-1-PLPP fusion protein can be one mode of PLP level regulation, and to replenish this enzyme in the various neurological disorders related to vitamin B(6). PMID: 18510874
Study demonstrates the ATP-sensitive interaction of the cofilin phosphatase chronophin (CIN) with the chaperone hsp90 to form a biosensor that mediates cofilin/actin rod formation. PMID: 19000834

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.