Recombinant Human Phosphoserine phosphatase Protein

Name: Recombinant Human Phosphoserine phosphatase Protein
Brand: Beta LifeScience
SKU: BLPSN-3811
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	N/A
Host Species	Human
Accession	P78330
Synonym	PSP, PSPHD
Background	Phosphoserine phosphatase (PSPH) belongs to a subfamily of the phosphotransferases. PSPH is the rate-limiting enzyme in l-serine biosynthesis. It has previously been found that Phosphoserine phosphatase (PSPH) plays a role in epidermal homeostasis. Phosphoserine phosphatase (PSP) catalyzes the hydrolysis of phosphoserine to serine. Phosphoserine phosphatase (PSPH) expression has been examined in human-mouse somatic cell hybrids retaining different combination of human chromosomes. Phosphoserine phosphatase (PSPH) is expressed throughout the proliferative layer of the epidermis and hair follicles in rodent and human skin and is highly induced in SCC. In keratinocytes, Phosphoserine phosphatase (PSPH) is a cytoplasmic protein that primarily localizes to endosomes and is present primarily as a homodimer. Knock down of Phosphoserine phosphatase (PSPH) dramatically diminished SCC cell proliferation and cyclin D1 levels in the presence of exogenous of l-serine production suggesting a non-canonical role for Phosphoserine phosphatase (PSPH) in epithelial carcinogenesis. Phosphoserine phosphatase (PSPH) is highly induced in proliferative normal keratinocytes and in skin tumors. Phosphoserine phosphatase (PSPH) appears to be critical for the proliferation of SCC cells; however, this phenomenon may not involve the phosphoserine metabolic pathway.
Description	A DNA sequence encoding the human PSPH (P78330) (Met 1-Glu 225) was expressed and purified.
Source	E.coli
Predicted N Terminal	Met 1
AA Sequence	Met 1-Glu 225
Molecular Weight	The recombinant human PSPH consists of 225 a.a. and has a calculated molecular mass of 25KD. It migrates as an approximately 28KDa band in SDS-PAGE under reducing conditions.
Purity	>84% as determined by SDS-PAGE
Endotoxin	Please contact us for more information.
Bioactivity	Please contact us for detailed information
Formulation	Lyophilized from sterile PBS, pH 7.5.
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

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.