Abcam, ab238305, Anti-Phosphothreonine antibody [RM102]

Size: 100µg
Rabbit Monoclonal Phosphothreonine antibody. Suitable for IP, ELISA, WB, ICC/IF and reacts with Modified Amino Acid samples. Cited in 2 publications.
Key facts
Host species:Rabbit,
Clonality:Monoclonal,
Clone number:RM102,
Isotype:IgG,
Carrier free:No,
Applications:ICC/IF, WB, IP, ELISASee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Specificity:ab238305 reacts threonine-phosphorylated proteins. No cross reactivity with nonphosphorylated threonine, phosphoserine, and phosphotyrosine. It shows slight cross-reactivity with a few phospho-serine-containing peptides.

Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification Protein A, Purification notes-Purified from an animal origin–free culture supernatant., Storage buffer-Preservative: 0.09% Sodium azideConstituents: PBS, 50% Glycerol (glycerin, glycerine), 1% 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.
Phosphothreonine often called phospho-threonine refers to a modified amino acid where a phosphate group attaches to threonine. It usually forms during protein post-translational modifications. This modification commonly occurs in eukaryotic cells and plays a significant role in regulating protein function. The mass of phosphothreonine itself is approximately 181 Da. Phosphothreonine residues are found in various proteins where they serve as important components for controlling multiple cellular processes.
Biological function summary
Phosphorylation of threonine residues influences protein activity localization and interactions. These phosphorylated threonine residues often exist as part of a larger protein complex influencing the dynamics of protein interactions. In cellular signal transduction they act as key regulatory switches. The modification is a reversible process which allows dynamic control over protein functionality in response to cellular signals.
Pathways
Signaling cascades often rely on phosphorylation events involving threonine which includes pathways like MAPK and PI3K/AKT. These pathways are essential for cellular responses to external stimuli and involve several other proteins such as RAS and AKT themselves. Through such pathways the phosphorylation state of threonine residues affects decisions about cell survival proliferation or differentiation.
Dysregulation of threonine phosphorylation links to conditions like cancer and diabetes. Abnormal phosphorylation patterns can lead to unregulated cell growth and survival common in tumorigenesis. Proteins such as p53 and insulin receptor substrates interact with phosphorylated threonine residues in these contexts. Investigating these interactions provides insights into the pathological mechanisms and potential therapeutic targets.