Product Details
Alternative Name: | Sequestosome-1, EBI3-associated protein of 60 kDa |
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MW: | ~74.4kDa |
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Source: | Produced in E. coli. Human p62 (1-440 aa) is fused to a N-terminal GST-tag. |
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UniProt ID: | Q13501 |
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Formulation: | Liquid. In 1M PBS containing 100mM GSH and 15% glycerol. |
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Purity: | ≥90% (SDS-PAGE) |
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Shipping: | Blue Ice |
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Short Term Storage: | -20°C |
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Long Term Storage: | -20°C |
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Use/Stability: | Stable for at least 12 months after receipt when stored at -20°C. |
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Handling: | Avoid freeze/thaw cycles. After opening, prepare aliquots and store at -20°C. |
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Scientific Background: | The p62 protein functions as a ubiquitin (Ub)-binding scaffold, which regulates a diverse range of signalling pathways leading to activation of the nuclear factor kappa B (NF-κB) family of transcription factors. p62 also plays an important role in the control of induced osteoclastogenesis,and mutations affecting the SQSTM1 gene are commonly found in patients with the skeletal disorder Paget's disease of bone (PDB). The vast majority of the PDB associated mutations identified cluster within the UBA domain, impairing p62's ability to bind Ub and resulting in dysregulated NF-κB signalling.
p62 is a critical regulator of the degradation of ubiquitinated proteins by macroautophagy.The p62 protein has a domain structure consistent with its participation in multiple signalling complexes, including a C-terminal Ub-associated (UBA) domain through which p62 binds non-covalently to Ub and a LC3 interacting region (LIR), facilitating simultaneous binding to ubiquitinylated proteins and the autophagic machinery via LC3/GABARAP. As a result p62 acts as an important substrate receptor for selective autophagy. |
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Regulatory Status: | RUO - Research Use Only |
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Western Blot analysis of ENZ-PRT120.
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Product Literature References
Autophagy Controls CSL/RBPJκ Stability through a p62/SQSTM1-Dependent Mechanism: S. Goruppi, et al.; Cell Rep.
24, 3108 (2018),
Abstract;
Full Text
General Literature References
A role for ubiquitin in selective autophagy: V. Kirkin, et al.; Mol.Cell.
34, 259 (2009),
Abstract;
NBR1 and p62 as cargo receptors for selective autophagy of ubiquitinated targets: T. Lamark, et al.; Cell Cycle
8, 1986 (2009),
Abstract;
p62 at the crossroads of autophagy, apoptosis, and cancer: J. Moscat, et al.; Cell 137, 1001 (2009),
The molecular pathogenesis of Paget disease of bone: R. Layfield; Expert. Rev. Mol. Med.
9, 1 (2007),
Abstract;
Loss of ubiquitin-binding associated with Paget's disease of bone p62 (SQSTM1) mutations: J. R. Cavey, et al.; J. Bone Miner. Res.
20, 619 (2005),
Abstract;
The atypical PKC-interacting protein p62 is an important mediator of RANK-activated osteoclastogenesis: A. Duran, et al.; Dev. Cell. 6, 303 (2004),
Structure of the ubiquitin-associated domain of p62 (SQSTM1) and implications for mutations that cause Paget's disease of bone: B. Ciani, et al.; J. Biol .Chem. 278, 37409 (2003),
Structure and functional properties of the ubiquitin binding protein p62: T. Geetha & M.W. Wooten; FEBS Lett.
512, 19 (2002),
Abstract;