Recombinant Human PSPH Protein

Name: Recombinant Human PSPH Protein
Brand: Beta LifeScience
SKU: BLA-7442P
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Host Species	Human
Synonym	EC 3.1.3.3 L 3 phosphoserine phosphatase L-3-phosphoserine phosphatase O phosphoserine phosphohydrolase O-phosphoserine phosphohydrolase Phosphoserine phosphatase Phosphoserine phosphatase deficiency, included PSP PSPase Psph PSPHD SERB_HUMAN
Description	Recombinant Human PSPH Protein was expressed in E.coli. It is a Full length protein
Source	E.coli
AA Sequence	MVSHSELRKL FYSADAVCFD VDSTVIREEG IDELAKICGV EDAVSEMTRR AMGGAVPFKA ALTERLALIQ PSREQVQRLI AEQPPHLTPG IRELVSRLQE RNVQVFLISG GFRSIVEHVA SKLNIPATNV FANRLKFYFN GEYAGFDETQ PTAESGGKGK VIKLLKEKFH FKKIIMIGDG ATDMEACPPA DAFIGFGGNV IRQQVKDNAK WYITDFVELL GELEE
Purity	>95% SDS-PAGE.Recombinant human PSPH was overexpressed in E. coli and purified by conventional chromatography.
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. Avoid freeze / thaw cycle.

Target Details

Target Function	Catalyzes the last irreversible step in the biosynthesis of L-serine from carbohydrates, the dephosphorylation of O-phospho-L-serine to L-serine. L-serine can then be used in protein synthesis, to produce other amino acids, in nucleotide metabolism or in glutathione synthesis, or can be racemized to D-serine, a neuromodulator. May also act on O-phospho-D-serine (Probable).
Subcellular Location	Cytoplasm, cytosol.
Protein Families	HAD-like hydrolase superfamily, SerB family
Database References	HGNC: 9577 OMIM: 172480 KEGG: hsa:5723 STRING: 9606.ENSP00000275605 UniGene: Hs.512656
Associated Diseases	Phosphoserine phosphatase deficiency (PSPHD)

Gene Functions References

PSPH expression is a novel biomarker for poor prognosis and could play an important role in tumor progression of colorectal cancer. PMID: 28476802
We further uncovered that phosphoserine phosphatase (PSPH), the final rate-limiting enzyme of the SSP pathway, is critical for cMyc-driven cancer progression both in vitro and in vivo PMID: 25793315
study of an intellectual disability family from Pakistan; identified a variant in PSPH: chr7:56088803C>T, NM_004577.3 c.103G>A; p.Ala35Thr (hg19) which segregated in homozygous form with the phenotype in both branches of the family PMID: 25080166
phosphoserine phosphatase deficiency is associated with Neu-Laxova syndrome. PMID: 25152457
status of PSPH in normal skin epidermis and skin tumors along with its sub-cellular localization in epidermal keratinocytes and its requirement for squamous cell carcinoma proliferation PMID: 21726982
purification, crystallization and preliminary X-ray diffraction analysis PMID: 11752790
description of the first crystal structures of the HPSP in complexes with the competitive inhibitor 2-amino-3-phosphonopropionic a PMID: 12213811
human phosphoserine phosphatase structure now shows a sevenfold coordinated Ca(2+) ion in the active site that might explain the inhibitory effect of Ca(2+) on the enzyme PMID: 15291819

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.