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Phosphoserine Phosphatase, Recombinant, Human (PSP, PSPase)

Cat no: P4076-83

Phosphoserine Phosphatase, Recombinant, Human (PSP, PSPase)

Human Phosphoserine phosphatase (hPSP) is an important enzyme in the phosphorylated pathway of serine biosynthesis, which contributes a major portion of the endogenous L-serine. Similar to known L-3-phosphoserine phosphatases, it catalyzed the Mg2+-dependent hydrolysis of L-phosphoserine and an exchange reaction between L-serine and L-phosphoserine. Recently, its complex structures reveal that the open-closed environmental change of the active site, generated -helical bundle domain, is important to substrate by local rearrangement of the recognition and hydrolysis.\n\nDescription: \nRecombinant Phosphoserine Phosphatase produced in E.Coli is a single,non-glycosylated polypeptide chain conjtaining 225 amino acids and having a molecular mass of 25kD. Recombinant human PSP was overexpressed in E. coli and purified by conventional chromatography.\n\nSequence: \nMVSHSELRKL FYSADAVCFD VDSTVIREEG IDELAKICGV EDAVSEMTRR AMGGAVPFKA ALTERLALIQ PSREQVQRLI AEQPPHLTPG IRELVSRLQE RNVQVFLISG GFRSIVEHVA SKLNIPATNV FANRLKFYFN GEYAGFDETQ PTAESGGKGK VIKLLKEKFH FKKIIMIGDG ATDMEACPPA DAFIGFGGNV IRQQVKDNAK WYITDFVELL GELEE\n\nStability: \nStore at 4 degrees C if entire vial will be used within 2-4 weeks. Store, frozen at -20 degrees C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

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SPECIFICATIONS

Catalog Number

P4076-83

Size

5ug

Form

Supplied as a liquid in 20mM HEPES, pH 7.5, 1mM DTT and 100mM KCl2.

Purity

(same/more than) 95% as determined by RP-HPLC, anion-exchange FPLC and/or reducing and non-reducing SDS-PAGE Silver Stained gel.

References

1. How calcium inhibits the magnesium-dependent enzyme human phosphoserine phosphatase.\n\nEur J Biochem 2004 Aug;271(16):3421-7\n\n2. A plasmid-encoded class 1 integron carrying sat, a putative phosphoserine phosphatase gene and aadA2 from enterotoxigenic Escherichia coli O159 isolated in Japan.\n\nFEMS Microbiol Lett 2004 Jun 15;235(2):243-8\n\n3. High-re solution structure of human phosphoserine phosphatase in open conformation.\n\nActa Crystallogr D Biol Crystallogr 2003 Jun;59(Pt 6):971-7\n\n4. Molecular basis for the local conformati onal rearrangement of human phosphoserine phosphatase.\n\nJ Biol Chem 2002 Nov 29;277(48):46651-8\n\n5. Structural characterization of the reaction pathway in phosphoserine phosphatase: crystallographic \" snapshots \" of intermediate states.\n\nJ Mol Biol 2002 May 31;319(2):421-31\n\n6. Purification, crystallization and preliminary X-ray diffraction analysis of human phosphoserine phosphatase.\n\nActa Crystallogr D Biol Crystallogr 2002 Jan;58(Pt 1):133-4

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Applications

ELISA

Reactivities

Hum

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Applications

IF

Hosts

Mouse

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Applications

ELISA, WB

Hosts

Mouse

Reactivities

Hum

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Applications

ELISA, FC, WB

Hosts

Mouse

Reactivities

Hum

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Applications

ELISA, FC, IHC, WB

Hosts

Mouse

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Applications

IHC, WB

Hosts

Rabbit

Reactivities

Hum

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Applications

ELISA, WB

Hosts

Rabbit

Reactivities

Hum

More info
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