免疫印迹, 酶联免疫吸附测定, 酶免疫法
PSPH; Phosphoserine phosphatase Human; PSPase; PSP; EC 184.108.40.206; O-phosphoserine phosphohydrolase; L-3-phosphoserine phosphatase; Phosphoserine phosphatase; L 3 phosphoserine phosphatase; O phosphoserine phosphohydrolase; Phosphoserine phosphatase deficiency; included
phosphoserine phosphatase; Phosphoserine phosphatase; phosphoserine phosphatase; L-3-phosphoserine phosphatase; O-phosphoserine phosphohydrolase; PSPase; phosphoserine phosphatase; L-3-phosphoserine phosphatase; O-phosphoserine phosphohydrolase
By protein-G affinity chromatography
Can be stored at 4 degree C. For long term storage, aliquot and store at -20 degree C. Avoid repeated freezing and thawing cycles.
ELISA (EIA), Western Blot (WB) (Cell lysate)
The antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:1,000 ~ 2,000. Recommended starting dilution is 1:1,000.
Antigen Species: Human. Clone: Anti-human PSP mAb, clone 3G12, is derived from hybridization of mouse SP2/0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human PSP protein. Immunogen: Recombinant human PSP (1-225aa) purified from E Coli
Human phosphoserine phosphatase (HPSP), specific for D- and L- phosphoserine, has been identified in all human tissues. HPSP is a Mg(2+)-dependent phosphoserine phosphatase. The three dimensional structure of HPSP reveals the structural and functional role of the divalent cation in the active site of phosphatases. In particular, the complex structures reveal that the open-closed environmental change of the active site, generated by local rearrangement of the alpha-helical bundle domain, is important for the substrate recognition and hydrolysis.
Moro-Furlani, et al., (1980) Ann Hum Genet 43(4):323-3233 kim HY, et al., (2002) J Biol Chem 277(48):46651-46658 Peeraer Y, et al., (2004) Eur J Biochem 271(16):3421-3427
NCBI GI登录号 :
Amino Acid Synthesis And Interconversion (transamination) Pathway (106173); Biosynthesis Of Amino Acids Pathway (790012); Biosynthesis Of Amino Acids Pathway (795174); Carbon Metabolism Pathway (814926); Carbon Metabolism Pathway (817567); Glycine, Serine And Threonine Metabolism Pathway (82949); Glycine, Serine And Threonine Metabolism Pathway (313); Metabolic Pathways (132956); Metabolism Pathway (477135); Metabolism Of Amino Acids And Derivatives Pathway (106169)
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. [provided by RefSeq, Jul 2008]
PSPH: Catalyzes the last step in the biosynthesis of serine from carbohydrates. The reaction mechanism proceeds via the formation of a phosphoryl-enzyme intermediates. Defects in PSPH are the cause of phosphoserine phosphatase deficiency (PSPHD)[MIM:614023]. A disorder that results in pre- and postnatal growth retardation, moderate psychomotor retardation and facial features suggestive of Williams syndrome. Belongs to the SerB family. Protein type: EC 220.127.116.11; Hydrolase; Amino Acid Metabolism - glycine, serine and threonine; Motility/polarity/chemotaxis. Chromosomal Location of Human Ortholog: 7p11.2. Cellular Component: neuron projection; cytoplasm; cytosol. Molecular Function: protein homodimerization activity; phosphoserine phosphatase activity; magnesium ion binding; calcium ion binding. Biological Process: response to nutrient levels; L-serine biosynthetic process; dephosphorylation; response to mechanical stimulus; L-serine metabolic process; amino acid biosynthetic process; response to testosterone stimulus. Disease: Phosphoserine Phosphatase Deficiency
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San Diego, CA 92195-3308