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BRAND / VENDOR: Abcam

Abcam, ab306577, Anti-PSPH antibody [EPR26995-88A]

CATALOG NUMBER: ab306577
Precio habitual$0.99
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Product Description

Size: 20µL / 100µL / 1mL
Rabbit Recombinant Monoclonal PSPH antibody. Suitable for IHC-P, WB and reacts with Human samples.
Key facts
Host species:Rabbit,
Clonality:Monoclonal,
Clone number:EPR26995-88A,
Isotype:IgG,
Carrier free:No,
Reacts with:Human,
Applications:WB, IHC-PSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Immunogen:The exact immunogen used to generate this antibody is proprietary information.

Product details:
Patented technology
Our RabMAb
technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to
RabMAb® patents
What are the advantages of a recombinant monoclonal antibody?
This product is a recombinant monoclonal antibody, which offers several advantages including:
- High batch-to-batch consistency and reproducibility
- Improved sensitivity and specificity
- Long-term security of supply
- Animal-free batch production
For more information, read more on
recombinant antibodies

Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification Protein A, Storage buffer-pH: 7.2 - 7.4Preservative: 0.01% Sodium azideConstituents: PBS, 40% Glycerol (glycerin, glycerine), 0.05% BSA, Shipped at conditions-Blue Ice, Appropriate short-term storage duration-1-2 weeks, 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.


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Collaboration

Tony Tang

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