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AB96414

Anti-PSPH antibody

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(4 Publications)

Rabbit Polyclonal PSPH antibody. Suitable for WB, ICC/IF and reacts with Human samples. Cited in 4 publications. Immunogen corresponding to Recombinant Fragment Protein within Human Phosphoserine phosphatase aa 1-200.

View Alternative Names

Phosphoserine phosphatase, PSP, PSPase, L-3-phosphoserine phosphatase, O-phosphoserine phosphohydrolase, PSPH

1 Images
Immunocytochemistry/ Immunofluorescence - Anti-PSPH antibody (AB96414)
  • ICC/IF

Unknown

Immunocytochemistry/ Immunofluorescence - Anti-PSPH antibody (AB96414)

Immunofluorescence analysis of paraformaldehyde-fixed A549 using ab96414 at 1 : 200 dilution : (1) without DNA probe, (2) merged with a DNA probe.

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

ICC/IF, WB

applications

Immunogen

Recombinant Fragment Protein within Human Phosphoserine phosphatase aa 1-200. The exact immunogen used to generate this antibody is proprietary information.

P78330

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 7 Preservative: 0.01% Thimerosal (merthiolate) Constituents: 10% Glycerol (glycerin, glycerine), 1.21% Tris, 0.75% Glycine
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Phosphoserine phosphatase (PSPH) also known as O-phosphoserine phosphohydrolase plays an essential role in serine biosynthesis by catalyzing the conversion of O-phospho-L-serine to L-serine. PSPH is a protein with a molecular weight of approximately 25 kDa. It is expressed across a wide range of tissues with notable expression in the liver kidney and brain. The enzyme activity of PSPH ensures the availability of serine a non-essential amino acid involved in multiple biochemical processes.
Biological function summary

Phosphoserine phosphatase contributes significantly to cellular metabolism and growth by its involvement in the serine biosynthesis pathway. This pathway is important for providing serine which acts as a precursor for proteins nucleotides and other biologically important molecules. PSPH does not function as part of a larger complex; however its enzymatic action is critical for maintaining levels of serine when dietary intake is low. In addition to its role in metabolism PSPH influences cell proliferation and differentiation through providing the necessary serine reserves.

Pathways

Phosphoserine phosphatase integrates into the serine biosynthesis pathway and shows a connection to the glycolytic pathway. The enzyme catalyzes one of the final steps in the phosphorylated serine synthesis process that branches from glycolysis. This pathway features interactions with enzymes like 3-phosphoglycerate dehydrogenase (PHGDH) and phosphoserine aminotransferase 1 (PSAT1) which work sequentially to produce 3-phosphoserine from 3-phosphoglycerate. PSPH follows these enzymes completing the conversion to serine and connects the serine biosynthesis cycle to broader metabolic activities.

Altered expression or function of phosphoserine phosphatase associates with conditions such as cancer and neurodegenerative diseases. Within oncogenesis elevated activity of PSPH can supply cancer cells with serine needed for rapid proliferation and this enzyme interplays with other metabolic proteins like PHGDH in cancer metabolism. In neurodegenerative disorders deficient PSPH activity disrupts serine availability leading to harmful effects on the nervous system. Understanding PSPH's role in these conditions can provide insights into therapeutic strategies targeting serine metabolism.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

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).
See full target information Phosphoserine phosphatase

Publications (4)

Recent publications for all applications. Explore the full list and refine your search

The Journal of cell biology 224: PubMed40608049

2025

Sphingolipid synthesis maintains nuclear membrane integrity and genome stability during cell division.

Applications

Unspecified application

Species

Unspecified reactive species

Sunyoung Hwang,William Russo,Jaylah Cormier,Jillian Johnson,Sara Martin,Marica Rosaria Ippolito,Sara Cordone,Rui Li,Lihua Julie Zhu,Stefano Santaguida,Eduardo M Torres

Nature communications 12:6176 PubMed34702840

2021

The impact of physiological metabolite levels on serine uptake, synthesis and utilization in cancer cells.

Applications

Unspecified application

Species

Unspecified reactive species

Marc Hennequart,Christiaan F Labuschagne,Mylène Tajan,Steven E Pilley,Eric C Cheung,Nathalie M Legrave,Paul C Driscoll,Karen H Vousden

Nature communications 12:366 PubMed33446657

2021

Serine synthesis pathway inhibition cooperates with dietary serine and glycine limitation for cancer therapy.

Applications

Unspecified application

Species

Unspecified reactive species

Mylène Tajan,Marc Hennequart,Eric C Cheung,Fabio Zani,Andreas K Hock,Nathalie Legrave,Oliver D K Maddocks,Rachel A Ridgway,Dimitris Athineos,Alejandro Suárez-Bonnet,Robert L Ludwig,Laura Novellasdemunt,Nikolaos Angelis,Vivian S W Li,Georgios Vlachogiannis,Nicola Valeri,Nello Mainolfi,Vipin Suri,Adam Friedman,Mark Manfredi,Karen Blyth,Owen J Sansom,Karen H Vousden

Molecular carcinogenesis 57:1342-1357 PubMed29873416

2018

EWS-FLI1 reprograms the metabolism of Ewing sarcoma cells via positive regulation of glutamine import and serine-glycine biosynthesis.

Applications

Unspecified application

Species

Unspecified reactive species

Nirmalya Sen,Allison M Cross,Philip L Lorenzi,Javed Khan,Berkley E Gryder,Suntae Kim,Natasha J Caplen
View all publications

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