Abcam, ab117253, Anti-Phospho - (Ser/Thr) antibody

Size: 1000µL
Anti-Phospho - (Ser/Thr) antibody (ab117253) is a rabbit polyclonal antibody detecting Phospho - (Ser/Thr) in ELISA, Dot Blot . - Over 20 publications
Key facts
Host species:Rabbit,
Clonality:Polyclonal,
Isotype:IgG,
Carrier free:No,
Applications:ELISA, DotSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.

Product details:
Anti-Phospho - (Ser/Thr) antibody (ab117253) is a rabbit polyclonal antibody and is validated for use in Dot blot, ELISA in human, rat samples.
Anti-Phospho - (Ser/Thr) antibody (ab117253) has been cited over 20 times in peer reviewed journals and is trusted by the scientific community.
Abcam's high quality validation processes ensure Anti-Phospho - (Ser/Thr) antibody (ab117253) has high sensitivity and specificity.
Anti-Phospho - (Ser/Thr) antibody (ab117253) specifically detects Phospho - (Ser/Thr) (UniProt ID: ; Molecular weight: kDa) and is sold in 1000 µL selling sizes.
Buffers and proteins which contain phosphate should be avoided with this antibody. Certain proteins known to contain phosphorylated serine and threonine may not be detected by this antibody due to steric hindrance.
The immunogen used is Phosphoserine and phosphothreonine conjugated with R-PE.

Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification Protein A, Storage buffer-pH: 7.4Preservative: 0.05% Sodium azideConstituents: 0.88% Sodium chloride, 0.16% Tris HCl, 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.
Phospho - (Ser/Thr) refers to phosphorylation on serine or threonine residues an important post-translational modification regulating numerous cellular functions. This process is essential in controlling protein activity localization and interaction with other cellular molecules. Phosphorylation events on serine or threonine residues are detected by specific antibodies such as anti-phospho antibodies anti-phosphoserine anti-phosphothreonine. These antibodies help in elucidating the dynamic state of proteins during phosphorylation events. Phospho-Ser/Thr sites are expressed across various tissues and cell types reflecting their universal role in cell signaling.
Biological function summary
Phosphorylation on serine and threonine is critical for enabling proteins to participate in various signaling cascades. These phosphorylation sites often form part of larger protein complexes where they serve as regulatory sites for modifying protein activity. Such modifications can impact a protein's role in processes like cell cycle regulation transcription and cellular metabolism. Phospho-serine and phospho-threonine residues influence the structural conformation of proteins affecting their interaction with other cellular components.
Pathways
These phosphorylated residues play a vital role in signaling pathways such as the MAPK/ERK pathway and the PI3K/AKT pathway. These pathways are important for transmitting signals from receptors on the cell surface to the DNA in the nucleus impacting gene expression and cellular responses. Proteins like Protein Kinase A (PKA) and Protein Kinase B (AKT) are often involved in these pathways directly interacting with phosphorylated serine and threonine residues to mediate cellular effects.
Abnormal phosphorylation on serine and threonine can contribute to conditions like cancer and diabetes. Dysregulated kinase activity can lead to overactive signaling pathways such as the overactivation of the ERK pathway in cancer promoting unchecked cell proliferation. Similarly disrupted phosphorylation patterns affect insulin signaling pathways contributing to insulin resistance in diabetes. Proteins such as MAPK and insulin receptor substrates often interact with phosphorylated sites linking these modifications to disease-related alterations in signaling pathways.