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Related Concept Videos

Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...

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Related Experiment Video

Updated: Jul 11, 2026

Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

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Phosphosite-Specific Antibodies: A Brief Update on Generation and Applications.

Kathy Brumbaugh1, Wen-Chie Liao2, J P Houchins2

  • 1Bio-Techne, Inc., 614 McKinley Place NE, Minneapolis, MN, 55413, USA. Kathy.brumbaugh@bio-techne.com.

Methods in Molecular Biology (Clifton, N.J.)
|February 11, 2017
PubMed
Summary

Phosphorylation, a key protein modification, impacts protein function. Phosphosite-specific antibodies are crucial tools for studying these changes in research and disease diagnostics.

Keywords:
AntibodyELISAFlow cytometryImmunocytochemistryMultiplexPhosphosite-specificSimple WesternWestern blotting

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Immunology

Background:

  • Post-translational modification (PTM) of proteins, such as phosphorylation, significantly alters intracellular protein activity and function.
  • Understanding protein phosphorylation is critical for elucidating cellular signaling pathways and disease mechanisms.

Purpose of the Study:

  • To discuss the generation and validation of phosphosite-specific antibodies.
  • To highlight the importance of antibody specificity in various biological applications.

Main Methods:

  • Generation of polyclonal and monoclonal phosphosite-specific antibodies using different animal species.
  • Validation of antibody specificity through multiple techniques.
  • Application of validated antibodies in techniques like arrays, flow cytometry, and imaging.

Main Results:

  • Both polyclonal and monoclonal antibody approaches have distinct advantages and disadvantages for generating phosphosite-specific antibodies.
  • Rigorous validation is essential to confirm the specificity of these antibodies.
  • Validated antibodies enable precise detection and quantification of protein phosphorylation.

Conclusions:

  • Phosphosite-specific antibodies are indispensable tools for proteomics and disease profiling.
  • Ensuring antibody specificity is paramount for accurate biological interpretation and diagnostic applications.
  • These antibodies facilitate advancements in understanding protein function and disease pathogenesis.