Recombinant Human PSP Protein (C-6His)

Name: Recombinant Human PSP Protein (C-6His)
Brand: Beta LifeScience
SKU: BL-1265NP
Availability: InStock

BL-1265NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

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.

Product Overview

Description	Recombinant Human Phosphoserine Phosphatase is produced by our E.coli expression system and the target gene encoding Met1-Glu225 is expressed with a 6His tag at the C-terminus.
Accession	P78330
Synonym	Phosphoserine Phosphatase; PSP; PSPase; L-3-Phosphoserine Phosphatase; O-Phosphoserine Phosphohydrolase; PSPH
Gene Background	Phosphoserine phosphatase (PSP) is an enzyme that belongs to the serB family. PSPH catalyzes magnesium-dependent hydrolysis of L-phosphoserine and is also involved in an exchange reaction between L-serine and L-phosphoserine. The reaction mechanism proceeds via the formation of a phosphoryl-enzyme intermediates. Deficiency of this protein is thought to be linked to Williams syndrome. A disorder that results in pre- and postnatal growth retardation, moderate psychomotor retardation and facial features suggestive of Williams syndrome.
Molecular Mass	26.07 KDa
Apmol Mass	25-30 KDa, reducing conditions
Formulation	Supplied as a 0.2 μm filtered solution of 20mM Tris-HCl, 4M Urea, 5mM EDTA, pH 8.0.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution
Storage	Store at ≤-70°C, stable for 6 months after receipt. Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.
Shipping	The product is shipped on dry ice/polar packs. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

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.