Anti-SQSTM1 / p62 (phospho Thr269 + Ser272) Antibody (A283325)

Anti-SQSTM1 / p62 (phospho Thr269 + Ser272) Antibody

Rabbit polyclonal antibody to SQSTM1 / p62 (phospho Thr269 + Ser272).

This antibody recognises ubiquitin-binding protein p62, also known as sequestosome-1 and EBI3-associated protein of 60 kDa (EBIAP), when phosphorylated at threonine 269 and serine 272. p62 is important in regulating critical cellular functions, including bone homeostasis, obesity, and cancer via its interactions with various signaling intermediaries. The SQSTM1 gene encodes a multifunctional protein that binds ubiquitin and regulates activation of the nuclear factor kappa-B (NF-?B) signaling pathway. p62 functions as a scaffolding/adaptor protein in concert with TNF receptor-associated factor 6 to mediate activation of NF-?B in response to upstream signals. p62 plays an important role in bone remodeling, regulating this process through its role in a chemical signaling pathway that promotes the formation of osteoclasts. p62 may be involved autophagy , the self-destruction of cells (apoptosis), and the body's immune responses and inflammatory reactions. p62 is an integral component of inclusions in brains of various neurodegenerative disorders, including Alzheimer disease (AD) neurofibrillary tangles (NFTs) and Lewy bodies in Parkinson disease. p62 plays an important role in the protection of cells from the toxicity of misfolded proteins by enhancing aggregate formation especially in the later stages. p62 is overexpressed inmany 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. The lack of cdk1-mediated phosphorylation of p62 leads to a faster exit from mitosis, translating into enhanced cell proliferation and tumorigenesis in response to Ras-induced transformation.

WB: 1:1,000

Human, Primate

Phosphopeptide corresponding to amino acid residues surrounding the phospho-Thr269/Ser272 region of human p62.

Rabbit

Polyclonal

IgG

Unconjugated

Lot Specific

Approximately 62 kDa in Jurkat cell lysate

Supplied in HEPES Buffered Saline with 1% BSA, 50% Glycerol and 0.09% Sodium Azide.

Shipped at ambient temperature. Upon delivery aliquot and store at -20°C. When thawed, aliquot the sample as needed. Short term (up to 4 weeks): store at 4°C. Long term: store at -20°C. Avoid freeze / thaw cycles. Storage in frost free freezers is not recommended.

Rabbit anti p62 (pThr269/pSer272) antibody recognizes ubiquitin-binding protein p62, also known as sequestosome-1 and EBI3-associated protein of 60 kDa (EBIAP), when phosphorylated at threonine 269 and serine 272. p62 is important in regulating critical cellular functions, including bone homeostasis, obesity, and cancer via its interactions with various signaling intermediaries. The SQSTM1 gene encodes a multifunctional protein that binds ubiquitin and regulates activation of the nuclear factor kappa-B (NF-?B) signaling pathway. p62 functions as a scaffolding/adaptor protein in concert with TNF receptor-associated factor 6 to mediate activation of NF-?B in response to upstream signals. p62 plays an important role in bone remodeling, regulating this process through its role in a chemical signaling pathway that promotes the formation of osteoclasts. p62 may be involved autophagy (Zhang et al. 2016), the self-destruction of cells (apoptosis), and the body's immune responses and inflammatory reactions. p62 is an integral component of inclusions in brains of various neurodegenerative disorders, including Alzheimer disease (AD) neurofibrillary tangles (NFTs) and Lewy bodies in Parkinson disease (Kurosawa et al. 2016). p62 plays an important role in the protection of cells from the toxicity of misfolded proteins by enhancing aggregate formation especially in the later stages(Wang et al. 2014). 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 (Linares et al. 2011). The lack of cdk1-mediated phosphorylation of p62 leads to a faster exit from mitosis, translating into enhanced cell proliferation and tumorigenesis in response to Ras-induced transformation.

A170, DMRV, EBI 3 associated protein of 60 kDa, EBI 3 associated protein p60, EBI3 associated protein of 60 kDa, EBI3 associated protein p60, EBI3-associated protein of 60 kDa, EBIAP, FTDALS3, MGC127197, ORCA, OSF-6, Osi, OSIL, Oxidative stress induced like, p60, p62, p62B, Paget disease of bone 3, PDB 3, PDB3, Phosphotyrosine independent ligand for the Lck SH2 domain of 62 kDa, Phosphotyrosine independent ligand for the Lck SH2 domain p62, Phosphotyrosine-independent ligand for the Lck SH2 domain of 62 kDa, PKC-zeta-interacting protein, Protein kinase C-zeta-interacting protein, Sequestosome 1, Sequestosome-1, SQSTM 1, Sqstm1, SQSTM_HUMAN, STAP, STONE14, Ubiquitin binding protein p62, Ubiquitin-binding protein p62, ZIP, ZIP 3, ZIP3