|Application ||WB, E|
|Other Accession||NP_004568, 5723, 100678 (mouse), 304429 (rat)|
|Calculated MW||25008 Da|
|Other Names||Phosphoserine phosphatase, PSP, PSPase, 18.104.22.168, L-3-phosphoserine phosphatase, O-phosphoserine phosphohydrolase, PSPH|
|Format||0.5 mg IgG/ml in Tris saline (20mM Tris pH7.3, 150mM NaCl), 0.02% sodium azide, with 0.5% bovine serum albumin|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Goat Anti-PSPH Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Catalyzes the last step in the biosynthesis of serine from carbohydrates. The reaction mechanism proceeds via the formation of a phosphoryl-enzyme intermediates.|
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Provided below are standard protocols that you may find useful for product applications.
The protein encoded by this gene belongs to a subfamily of the phosphotransferases. This encoded enzyme is responsible for the third and last step in L-serine formation. It catalyzes magnesium-dependent hydrolysis of L-phosphoserine and is also involved in an exchange reaction between L-serine and L-phosphoserine. Deficiency of this protein is thought to be linked to Williams syndrome.
Large-scale mapping of human protein-protein interactions by mass spectrometry. Ewing RM, et al. Mol Syst Biol, 2007. PMID 17353931.
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Gerhard DS, et al. Genome Res, 2004 Oct. PMID 15489334.
How calcium inhibits the magnesium-dependent enzyme human phosphoserine phosphatase. Peeraer Y, et al. Eur J Biochem, 2004 Aug. PMID 15291819.
Complete sequencing and characterization of 21,243 full-length human cDNAs. Ota T, et al. Nat Genet, 2004 Jan. PMID 14702039.
Mutations responsible for 3-phosphoserine phosphatase deficiency. Veiga-da-Cunha M, et al. Eur J Hum Genet, 2004 Feb. PMID 14673469.
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