|Calculated MW||62 KDa|
|Other Names||Sequestosome-1, EBI3-associated protein of 60 kDa, EBIAP, p60, Phosphotyrosine-independent ligand for the Lck SH2 domain of 62 kDa, Ubiquitin-binding protein p62, SQSTM1, ORCA, OSIL|
|Target/Specificity||Synthetic phospho-peptide corresponding to amino acid residues surrounding Thr269/Ser272 conjugated to KLH.|
|Format||Prepared from rabbit serum by affinity purification via sequential chromatography on phospho- and dephosphopeptide affinity columns.|
|Antibody Specificity||Specific for the ~62k p62 protein phosphorylated at Thr269 and Ser272.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Phospho-Thr269/Ser272 p62 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
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Provided below are standard protocols that you may find useful for product applications.
The protein scaffold and signaling regulator p62 (also known as sequestosome1 (SQSTM1)) is important in critical cellular functions, including bone homeostasis, obesity, and cancer, because of its interactions with various signaling intermediaries. p62 is overexpressed in many human cancers and is induced during cell transformation. cdk1 phosphorylates p62 in vitro and in vivo at T269 and S272, which is necessary for the maintenance of appropriate cyclin B1 levels and the levels of cdk1 activity necessary to allow cells to properly enter and exit mitosis (Moscat et al., 2011). The lack of cdk1-mediated phosphorylation of p62 leads to a faster exit from mitosis, translating into enhanced ell proliferation and tumorigenesis in response to Ras-induced transformation (Moscat et al., 2011).
Moscat J, Linares JF, Amanchy R, Diaz-Meco MT (2011) Phosphorylation of p62 by cdk1 Controls the Timely Transit of Cells through Mitosis and Tumor Cell Proliferation. Mol Cell Biol. 1:105-17.
Pankiv S, Lamark T, Bruun JA, Øvervatn A, Bjørkøy G, and Johansen (2010). Nucleocytoplasmic Shuttling of p62/SQSTM1 and Its Role in Recruitment of Nuclear Polyubiquitinated Proteins to Promyelocytic Leukemia Bodies. J Biol Chem. 8: 5941-53
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