Abcam, ab9344, Anti-Phosphothreonine-Proline / Phosphoserine-Proline antibody

Size: 100µg
Rabbit Polyclonal Phosphothreonine-Proline / Phosphoserine-Proline antibody. Suitable for ELISA, WB and reacts with Modified Amino Acid samples. Cited in 14 publications. Immunogen corresponding to Chemical / Small Molecule corresponding to Phosphothreonine-Proline / Phosphoserine-Proline.
Key facts
Host species:Rabbit,
Clonality:Polyclonal,
Isotype:IgG,
Carrier free:No,
Applications:ELISA, WBSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Specificity:This antibody specifically reacts to proteins containing phosphothreonine-proline motifs, it also reacts to the phosphoserine-proline motif to a similar degree (pT-P and pS-P motif). The antibody does not react to phosphothreonine, phosphoserine or phosphotyrosine. The antibody will selectively recognize the phosphothreonine-proline motif of MBP, which is the site of phosphorylation by ERK1/ERK2.

Product details:
The antigen is based on N-acetyl-pT-K-pY-NH2. The pT-X-pY sequence is considered to be the motif for some active MAPKs.

Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification Immunogen, Purification notes-Immunoaffinity chromatography with phosphothreonine-proline on agarose, then immuno-absorption with threonine-proline-NH2 on 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.
Phosphothreonine-Proline and Phosphoserine-Proline are key post-translational modifications often involved in signaling pathways. These sites are characterized by the addition of a phosphate group to the hydroxyl group of threonine or serine residues adjacent to proline creating unique recognition motifs. They are especially significant in cell cycle regulation and various cellular processes. These motifs are recognized by specialized proteins like proline-directed kinases and peptidyl-prolyl isomerases. Expression occurs widely in tissues where active signal transduction is essential. The exact molecular mass varies depending on the protein context in which these motifs occur.
Biological function summary
These phosphorylation motifs play roles in regulating protein function and stability. Phosphothreonine-Proline and Phosphoserine-Proline facilitate interactions with proteins such as Pin1 a well-known peptidyl-prolyl isomerase. This interaction modulates protein folding and function. These motifs influence cell cycle progression apoptosis and cellular differentiation showing involvement in complex signal transduction networks. Their presence can alter the conformation and thereby the activity of signaling proteins.
Pathways
Phosphothreonine-Proline and Phosphoserine-Proline modifications integrate into major pathways like MAPK and PI3K/Akt. They regulate activities of proteins such as cyclin-dependent kinases (CDKs) and Akt impacting cellular responses to external signals. These signaling pathways are essential for cellular growth survival and metabolism. Modifications on threonine and serine residues can influence the phosphorylation status and activity of these downstream effectors creating a dynamic and responsive signaling network.
Alterations in these phosphorylation sites contribute to conditions like cancer and neurodegenerative diseases. Over- or under-phosphorylation can lead to disrupted cell cycle control and apoptosis conditions often linked to tumors. Abnormal phosphorylation patterns may also relate to pathologies like Alzheimer’s disease where proteins such as Tau show abnormal phosphorylation states. This highlights the connection between these phosphorylation motifs and protein dysfunctions associated with disease progression.