Rabbit Polyclonal Phosphoserine antibody - conjugated to HRP. Suitable for ELISA, WB and reacts with Modified Amino Acid samples. Cited in 12 publications. Immunogen corresponding to Chemical / Small Molecule corresponding to Phosphoserine.
pH: 6 - 8
Constituents: Tris buffered saline
ELISA | WB | |
---|---|---|
Modified Amino Acid | Expected | Tested |
Species | Dilution info | Notes |
---|---|---|
Species Modified Amino Acid | Dilution info Use at an assay dependent concentration. | Notes - |
Species | Dilution info | Notes |
---|---|---|
Species Modified Amino Acid | Dilution info - | Notes To block use 3%BSA with 0.1% gelatin (do not use milk). We recommend that the antibody solution should contain 0.5% BSA to prevent non-specific binding. |
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PS, pSER, phospho-Ser
Rabbit Polyclonal Phosphoserine antibody - conjugated to HRP. Suitable for ELISA, WB and reacts with Modified Amino Acid samples. Cited in 12 publications. Immunogen corresponding to Chemical / Small Molecule corresponding to Phosphoserine.
pH: 6 - 8
Constituents: Tris buffered saline
Specifically recognizes both free-phosphoserine, serine-phosphorylated peptide and proteins.
Does not cross-react with ATP, phosphotyrosine, peptidyl phosphothreonine and serine.
Has slight cross-reactivity with free phosphothreonine.
Readily reacts to known phosphoproteins such as phosvitin and alpha casein.
Immunoaffinity chromatography with phosphoserine-agarose.
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.
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.
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.
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Terms & Conditions.
Western blotting of mouse brain extract with ab9334 at a 1/200 dilution on a 12% SDS gel. 50 µg protein loaded in each lane. Antibody incubated for 2 hours incubation at room temperature.
All lanes: Western blot - HRP Anti-Phosphoserine antibody (ab9334)
Developed using the ECL technique.
Performed under reducing conditions.
Exposure time: 5min
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