Anti-phospho-p62 (Ser24)

Not available outside of the UK & Ireland.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Immunogen

Linear peptide corresponding to 8 amino acids surrounding phosphoserine 24 in the N-terminal region of human p62.

Physical form

Purified rabbit polyclonal antibody in PBS with 0.02% sodium azide.

Reconstitution

Please refer to lot specific datasheet.

Specificity

This rabbit polyclonal antibody specifically detects Sequestosome-1 (p62) phosphorylated on serine 24.

Storage and Stability

Stable for 1 year at 2-8°C from date of receipt.

Target description

Sequestosome-1 (UniProt: Q13501; also known as EBI3-associated protein of 60 kDa, EBIAP, p60, Phosphotyrosine-independent ligand for the Lck SH2 domain of 62 kDa, Ubiquitin-binding protein p62) is encoded by the SQSTM1 (also known as ORCA, OSIL) gene (Gene ID: 8878) in human. p62, also known as SQSTM1, is a multi-domain signaling scaffold protein that is Ubiquitously expressed and is involved in numerous critical cellular functions such as autophagy, apoptosis and inflammation. It serves as an autophagy receptor that participates in selective macroautophagy and acts as a bridge between polyubiquitinated cargo and autophagosomes. It acts as a cargo receptor by detecting ubiquitinated substrates using its UBA domain, aggregating them through PB1-mediated homo-polymerization and attaching them to the autophagosome by association with LC3. p62 can undergo phosphorylation at multiple sites by various kinases. Phosphorylation at serine 24 in the PB1 domain by PKA is shown to regulate p62 polymerization and interaction partner binding profile. Mutations in SQSTM1 gene have been linked to Paget disease of bone that is characterized by increased bone turnover affecting one or more sites throughout the skeleton and makes them more susceptible to fractures. (Ref: Christian, F., et al. (2014). Biochim. Biophys Acta. 1843(11); 2765-2774).