PSPH Antibody (N-term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, E |
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Primary Accession | P78330 |
Other Accession | Q5M819, Q99LS3, NP_004568.2 |
Reactivity | Human, Mouse |
Predicted | Rat |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 25008 Da |
Antigen Region | 7-36 aa |
Gene ID | 5723 |
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Other Names | Phosphoserine phosphatase, PSP, PSPase, L-3-phosphoserine phosphatase, O-phosphoserine phosphohydrolase, PSPH |
Target/Specificity | This PSPH antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 7-36 amino acids from the N-terminal region of human PSPH. |
Dilution | WB~~1:8000 |
Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | PSPH Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | PSPH (HGNC:9577) |
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Function | Catalyzes the last irreversible step in the biosynthesis of L-serine from carbohydrates, the dephosphorylation of O-phospho-L- serine to L-serine (PubMed:12213811, PubMed:14673469, PubMed:15291819, PubMed:25080166, PubMed:9222972). 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 (PubMed:14673469). May also act on O-phospho-D-serine (Probable). |
Cellular Location | Cytoplasm, cytosol. |
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Provided below are standard protocols that you may find useful for product applications.
Background
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.
References
Lamesch, P., et al. Genomics 89(3):307-315(2007)
Ewing, R.M., et al. Mol. Syst. Biol. 3, 89 (2007) :
Peeraer, Y., et al. Eur. J. Biochem. 271(16):3421-3427(2004)
Veiga-da-Cunha, M., et al. Eur. J. Hum. Genet. 12(2):163-166(2004)
Peeraer, Y., et al. Acta Crystallogr. D Biol. Crystallogr. 59 (PT 6), 971-977 (2003) :
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