Abcam, ab9335, Biotin Anti-Phosphoserine antibody

Size: 50µg
Rabbit Polyclonal Phosphoserine antibody - conjugated to Biotin. Suitable for IP, ELISA, WB and reacts with Modified Amino Acid samples. Cited in 4 publications. Immunogen corresponding to Chemical / Small Molecule corresponding to Phosphoserine.
Key facts
Host species:Rabbit,
Clonality:Polyclonal,
Isotype:IgG,
Conjugation:Biotin,
Carrier free:No,
Applications:ELISA, IP, WBSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Specificity:Specifically recognizes both free-phosphoserine, serine-phosphorylated peptide and proteins. Does not cross-react with ATP, phosphotyrosine, peptidyl phosphothreonine and serine. Slight cross-reactivity with free phosphothreonine. Readily reacts to known phosphoproteins such as phosvitin and alpha casein.

Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification Immunogen, Purification notes-Immunoaffinity chromatography with phosphoserine-agarose., Storage buffer-pH: 6 - 8Preservative: 0.02% Sodium azide, 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, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Phosphoserine often referred to by its common alternate name "P-Ser" represents a phosphorylated form of the amino acid serine. This small molecule under a molecular mass of near 166 Daltons plays an important role in cellular signaling. It is expressed widely across various cell types particularly in tissues with high cell turnover. Phosphoserine results from the action of kinases which transfer a phosphate group from ATP to the serine's hydroxyl group. This phosphorylation process provides a critical modulatory mechanism that impacts protein function and cellular pathways.
Biological function summary
Phosphorylated serine residues are involved in controlling a multitude of cellular processes including cell cycle regulation and apoptosis. These phosphorylated regions form parts of protein kinases phosphatases and glycoproteins acting as switches for cellular signaling. Phosphoserine is often part of multi-protein complexes binding to other proteins and influencing their activity through changes in conformation. This active participation in biological pathways signifies its significant influence in maintaining cellular homeostasis.
Pathways
Phosphoserine plays a significant role in the MAPK signaling and PI3K/AKT pathways both important for cell growth and survival. It interacts with proteins like AKT and MAPK facilitating cellular responses to extracellular stimuli. This phosphorylation state dictates the activation or inactivation of these proteins effectively regulating key steps in signal transduction and transcriptional control. Such pathways highlight the importance of phosphoserine in coordinating complex cellular activities.
Aberrations in phosphoserine activity have been linked to conditions such as cancer and neurodegenerative diseases. In cancer dysregulation in its phosphorylation status may lead to uncontrolled cellular proliferation and resistance to apoptosis. Proteins such as p53 which plays a pivotal role in DNA repair and cell cycle arrest often show altered phosphorylation patterns in the presence of disease. Similarly in neurodegenerative disorders improper phosphorylation of tau proteins is a hallmark of conditions like Alzheimer's disease pointing to the critical involvement of phosphoserine and its associated pathways in disease pathology.