Sequestosome 1 (SQSTM1, p62) is a ubiquitin binding protein involved in cell signaling, oxidative stress, and autophagy. It was first identified as a protein that binds to the SH2 domain of p56Lck and independently found to interact with PKCζ. SQSTM1 was subsequently found to interact with ubiquitin, providing a scaffold for several signaling proteins and triggering degradation of proteins through the proteasome or lysosome. Interaction between SQSTM1 and TRAF6 leads to the K63-linked polyubiquitination of TRAF6 and subsequent activation of the NF-κB pathway. Protein aggregates formed by SQSTM1 can be degraded by the autophagosome. SQSTM1 binds autophagosomal membrane protein LC3/Atg8, bringing SQSTM1-containing protein aggregates to the autophagosome. Lysosomal degradation of autophagosomes leads to a decrease in SQSTM1 levels during autophagy; conversely, autophagy inhibitors stabilize SQSTM1 levels. Studies have demonstrated a link between SQSTM1 and oxidative stress. SQSTM1 interacts with KEAP1, which is a cytoplasmic inhibitor of NRF2, a key transcription factor involved in cellular responses to oxidative stress. Thus, accumulation of SQSTM1 can lead to an increase in NRF2 activity.

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

q13501

Human,Mouse

WB,IHC,IF,ICC

WB 1:5000-1:10000
IHC 1:50-1:200
IF 1:50-1:200
ICC 1:100-1:400

~ 56 kDa

Rabbit

This antibody detects endogenous levels of SQSTM1 protein.

Synthetic peptide, corresponding to Human SQSTM1.

Polyclonal

Rabbit IgG

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).

PBS with 0.02% sodium azide, 50% glycerol, pH7.2

1mg/ml

Store at 4℃ short term,and store at -20℃ long term. Avoid freeze-thaw cycles.