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P0068

Sigma-Aldrich

Anti-p62/SQSTM1 (C-terminal) antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Synonym(s):

Anti-Sequestosome 1, Anti-Ubiquitin-binding protein p62

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~62 kDa

species reactivity

rat, mouse, human

concentration

~1.0 mg/mL

technique(s)

immunoprecipitation (IP): 2-4 μg using whole extract of NIH-3T3 cells
western blot: 2-4 μg/mL using whole extracts of rat PC12 cells
western blot: 4-8 μg/mL using whole extracts of human A549 cells.

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... SQSTM1(8878)
mouse ... Sqstm1(18412)
rat ... Sqstm1(113894)

Related Categories

General description

The p62 protein/sequestosome 1 (SQSTM1) comprises a Phox and Bem1p (PB1) domain at the NH2-terminal, a ZZ type zinc finger domain, a Pro, Glu, Ser, and Thr (PEST) region consisting of putative phosphorylation sites, and a ubiquitin-associated (UBA) domain at the COOH-terminal. The SQSTM1 gene is mapped to the human chromosome location 5q35.3.

Specificity

Anti-p62/SQSTM1 (C-terminal) recognizes human, rat, and mouse p62/SQSTM1.

Application

Rabbit polyclonal anti-SQSTM1 antibody has been used:
  • in immunoblotting
  • in immunoprecipitation
  • as a probe to determine the presence and roles of p62 protein/sequestosome 1 in processes such as autophagy

Biochem/physiol Actions

The p62 protein/sequestosome 1 (SQSTM1) is a multifunctional protein, which binds to ubiquitin. It acts as a scaffold protein for the nuclear factor kappa-B (NF-ΚB) signaling pathway. SQSTM1 also regulates apoptosis and autophagy. Mutations in this gene lead to sporadic and familial Paget disease of bone. It is also associated with protein aggregation diseases, such as Lewy bodies in Parkinson′s disease, neurofibrillary tangles in Alzheimer′s disease, and huntingtin aggregates. SQSTM1 is commonly found in inclusion bodies containing polyubiquitinated protein aggregates that accumulate in several degenerative diseases. p62 polymerizes through its N-terminal Phox and Bem1p (PB1) domain and interacts with polyubiquitinated proteins through its C-terminal ubiquitin-associated (UBA) domain. p62 acts as a linker between protein aggregates and the autophagy machinery.

Physical form

Solution in 0.01 M phosphate buffered saline pH 7.4, containing 15 mM sodium azide.

Storage and Stability

For continuous use, store at 2–8 °C for up to one month. For extended storage freeze in working aliquots. Repeated freezing and thawing is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilution samples should be discarded if not used within 12 hours.

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.

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Storage Class Code

10 - Combustible liquids

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Christine Knies et al.
ChemistryOpen, 5(2), 129-141 (2016-06-17)
We report on the synthesis of two series of canonical purine ß-d-ribonucleoside nucleolipids derived from inosine and adenosine, which have been characterized by elemental analyses, electrospray ionization mass spectrometry (ESI MS) as well as by (1)H and (13)C NMR, and pH-dependent
Geir Bjørkøy et al.
Autophagy, 2(2), 138-139 (2006-07-29)
In eukaryotic cells short-lived proteins are degraded in a specific process by the ubiquitin-proteasome system (UPS), whereas long-lived proteins and damaged organelles are degraded by macroautophagy (hereafter referred to as autophagy). A growing body of evidence now suggests that autophagy
Stuart H Ralston et al.
Lancet (London, England), 372(9633), 155-163 (2008-07-16)
Paget's disease of bone is a common disease characterised by focal areas of increased bone turnover, affecting one or several bones throughout the skeleton. Paget's disease is often asymptomatic but can be associated with bone pain and other complications such
Frédéric Gros et al.
Autophagy, 8(7), 1113-1123 (2012-04-24)
Macroautophagy was recently shown to regulate both lymphocyte biology and innate immunity. In this study we sought to determine whether a deregulation of autophagy was linked to the development of autoimmunity. Genome-wide association studies have pointed out nucleotide polymorphisms that
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