The identification of protein phosphorylation as a regulatory mechanism originated from studies by Fischer and Krebs in the mid 1950s that later earned them the 1992 Nobel prize. It is the major mechanism for the regulation of diverse cellular processes including cell division, protein synthesis, transcriptional regulation and neurotransmission. The steady state phosphorylation of any given substrate is governed by the opposing activities of kinases and phosphatases. It is now believed that a third of all eukaryotic cellular proteins are phosphorylated and that the majority of all phosphorylation events occur on serine and threonine residues (>95%).
This antibody recognizes serine-phosphorylated proteins from all species.
Phosphoserine coupled to KLH.
Detect Phosphoserine using this Anti-Phosphoserine Antibody, clone 4A4 (mouse IgG1) validated for use in ELISA, FC, IF, IH(P) & WB.
Research Sub Category
General Post-translation Modification
Routinely evaluated by Western Blot analysis on lysate from Calyculin A/Okadaic-treated human A431 carcinoma cells.
Western Blot Analysis:
0.5–2 μg/mL of this lot detected serinephosphorylated proteins in a lysate from either insulin or Calyculin A/Okadaic-treated human A431 carcinoma cells.
Dependent upon the molecular weight of the serine phosphorylated protein being detected.
Protein G-Sepharose Chromatography
Purified mouse monoclonal IgG1 in buffer containing PBS with 0.1% sodium azide and 30% glycerol.
Storage and Stability
Stable for 1 year at -20ºC from date of receipt.
For maximum recovery, centrifuge the original vial prior to cap removal. If the product has accidentally been frozen and thawed, spin it at 13,000 x g for 10 minutes at 2-8°C.
Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
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