Phosphoserine

Protein phosphorylation is a complex biochemical process that ultimately influences the mechanism by which a cell responds to a particular stimulus. A class of enzymes referred to as protein kinases regulates this process; these enzymes catalyze the transfer of the ã-P of ATP to a recipient protein that acts as a substrate.\nThis post-translational modification is primarily directed onto serine and threonine amino acid residues within a protein. It has been noted that changes in the phosphorylation status of these phosphoproteins can alter the biological function of a protein. Additionally, aberrations in signal transduction cascade have been linked to a number of diseases, including cancer, diabetes, heart disease, inflammation and neurological disorders.\n\nPositive Control: Mouse brain extract for Western Blotting. Synthetic phosphopeptide or phosvitin for ELISA.\n\nApplications: \nSuitable for use in ELISA, Western Blot, Immunoprecipitation and Immunohistochemistry. Other applications not tested.\n\nRecommended Dilution:\nOptimal dilutions to be determined by the researcher.\n\nStorage and Stability:\nMay be stored at 4 degrees C for short-term only. For long-term storage and to avoid repeated freezing and thawing, aliquot Store at -20 degrees C. Aliquots are stable for at least 12 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

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SPECIFICATIONS

Catalog Number

P4076-50B

Size

400ul

Applications

ELISA, IHC, IP, WB

Hosts

Rabbit

Form

Supplied as a liquid in PBS, pH 7.2.

P Type

Pab

Purity

Purified by immunoaffinity chromatography.

Isotype

IgG

References

Gravel A et al. Human Herpesvirus 6 immediate-early 1 protein is a sumoylated nuclear phosphoprotein colocalizing with promyelocytic leukemia protein-associated nuclear bodies. J Biol Chem 277:19679-87 (2002). <PUBMED:11901159>Davis PJ et al. Thyroxine promotes association of mitogen-activated protein kinase and nuclear thyroid hormone receptor (TR) and causes serine phosphorylation of TR. J Biol Chem 275:38032-9 (2000). <PUBMED:10982791>

Additional Info

Specifically recognizes both free-phosphoserine, serine-phosphorylated peptide and proteins. Does not crossreact with ATP, phosphotyrosine, peptidyl phosphothreonine and serine. Slight crossreactivity with free phosphothreonine. Readily reacts to known phosphoproteins such as phosvitin and alpha casein.