PSPH Human

Phosphoserine Phosphatase Human Recombinant
Cat. No.
BT1182
Source
Escherichia Coli.
Synonyms
Phosphoserine phosphatase, EC 3.1.3.3, PSP, O-phosphoserine phosphohydrolase, PSPase, L-3-phosphoserine phosphatase, PSPH.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

Phosphoserine Phosphatase Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 225 amino acids and having a molecular mass of 25 kDa.
PSP was overexpressed in E. coli and purified by conventional chromatography.

Product Specs

Introduction
Human Phosphoserine phosphatase (hPSP) is a key enzyme involved in the serine biosynthesis pathway, specifically in the phosphorylated pathway. This pathway is a major contributor to the production of endogenous L-serine. hPSP, similar to other L-3-phosphoserine phosphatases, catalyzes the Mg2+-dependent hydrolysis of L-phosphoserine. It also facilitates an exchange reaction between L-serine and L-phosphoserine. Recent studies and complex structure analysis have revealed that the active site of hPSP undergoes open-closed conformational changes. This dynamic behavior, driven by a -helical bundle domain, is crucial for substrate recognition and hydrolysis through local rearrangements.
Description
Recombinant Human Phosphoserine Phosphatase, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 225 amino acids. It has a molecular weight of 25 kDa. The production process involves overexpression in E. coli followed by purification using standard chromatographic techniques.
Physical Appearance
A clear, colorless solution that has been sterilized through filtration.
Formulation
The protein is supplied in a buffer consisting of 20mM Hepes (pH 7.5), 1mM DTT, and 100mM KCl2.
Stability
For short-term storage (2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to freeze the product at -20°C. To further enhance long-term stability, adding a carrier protein like HSA or BSA (0.1%) is advisable. Repeated freezing and thawing cycles should be avoided.
Purity
The purity is determined to be greater than 95.0% based on the following analyses: (a) Reverse-phase high-performance liquid chromatography (RP-HPLC) and (b) Sodium dodecyl-sulfate polyacrylamide gel electrophoresis (SDS-PAGE).
Synonyms
Phosphoserine phosphatase, EC 3.1.3.3, PSP, O-phosphoserine phosphohydrolase, PSPase, L-3-phosphoserine phosphatase, PSPH.
Source
Escherichia Coli.
Amino Acid Sequence
MVSHSELRKL FYSADAVCFD VDSTVIREEG IDELAKICGV EDAVSEMTRR AMGGAVPFKA ALTERLALIQ PSREQVQRLI AEQPPHLTPG IRELVSRLQE RNVQVFLISG GFRSIVEHVA SKLNIPATNV FANRLKFYFN GEYAGFDETQ PTAESGGKGK VIKLLKEKFH FKKIIMIGDG ATDMEACPPA DAFIGFGGNV IRQQVKDNAK WYITDFVELL GELEE.

Product Science Overview

Gene and Protein Information

The PSPH gene is located on chromosome 7 in humans and encodes the phosphoserine phosphatase protein . The protein consists of 225 amino acids and has a calculated molecular mass of approximately 25 kDa . It is expressed in various tissues, including the epidermis and hair follicles, and is highly induced in certain skin tumors .

Function and Mechanism

Phosphoserine phosphatase catalyzes the irreversible dephosphorylation of O-phospho-L-serine to L-serine . This reaction is crucial for maintaining adequate levels of L-serine in the body, which can then be used for protein synthesis, nucleotide metabolism, and other vital processes . The enzyme also participates in an exchange reaction between L-serine and L-phosphoserine .

Clinical Significance

Deficiency in phosphoserine phosphatase activity has been linked to various disorders, including Williams syndrome . Additionally, the enzyme’s expression is altered in certain cancers, such as squamous cell carcinoma (SCC), where it plays a role in cell proliferation and tumor growth .

Recombinant Human PSPH

Recombinant human phosphoserine phosphatase is produced using DNA sequences encoding the human PSPH gene, which are expressed and purified in host systems such as E. coli . The recombinant protein is used in various research applications, including studies on enzyme function, metabolic pathways, and disease mechanisms .

Storage and Stability

Recombinant human PSPH is typically provided as a lyophilized powder and should be stored under sterile conditions at -20°C to -80°C . It is recommended to avoid repeated freeze-thaw cycles to maintain the protein’s stability and activity .

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