|Application:||IHC-P, ICC, WB|
Data & Images
|Product Name||Anti-SQSTM1/p62 Antibody|
|Description||Rabbit IgG polyclonal antibody for Sequestosome-1(SQSTM1) detection. Tested with WB, IHC-P, ICC in Human;Mouse;Rat.|
|Cite This Product||Anti-SQSTM1/p62 Antibody (Boster Biological Technology, Pleasanton CA, USA, Catalog # PA1955)|
|Replacement Item||This antibody may replace the following items: sc-10117|sc-25575|sc-28359|sc-48402 from Santa Cruz Biotechnology.|
|Validated Species||Human, Mouse, Rat|
*This antibody is predicted to react with the above species based on antigen sequence similarities. Our Boster Guarantee covers the use of this product with the above species.
|Application||IHC-P, ICC, WB
*Our Boster Guarantee covers the use of this product in the above tested applications.
**For positive and negative control design, consult "Tissue specificity" under Protein Target Info.
|Recommended Detection Systems||Boster recommends Enhanced Chemiluminescent Kit with anti-Rabbit IgG (EK1002) for Western blot, and HRP Conjugated anti-Rabbit IgG Super Vision Assay Kit (SV0002-1) for IHC(P) and ICC.
*Blocking peptide can be purchased at $50. Contact us for more information
**Boster also offers various secondary antibodies for Immunoflourescecne and IHC. Take advantage of the buy 1 primary antibody get 1 secondary antibody for free promotion for the entire year 2017!
|Immunogen||A synthetic peptide corresponding to a sequence at the N-terminus of human SQSTM1(91-110aa KDDIFRIYIKEKKECRRDHR), different from the related rat and mouse sequences by one amino acid.|
|Cross Reactivity||No cross reactivity with other proteins|
|Contents||Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg Thimerosal, 0.05mg NaN3.
*carrier free antibody available upon request.
|Concentration||Add 0.2ml of distilled water will yield a concentration of 500ug/ml.|
|Storage||At -20˚C for one year. After reconstitution, at 4˚C for one month. It can also be aliquotted and stored frozen at -20˚C for a longer time.Avoid repeated freezing and thawing.|
|Purification||Immunogen affinity purified.|
Protein Target Info (Source: Uniprot.org)
You can check the tissue specificity below for information on selecting positive and negative control.
|Molecular Weight||47687 MW|
|Protein Function||Autophagy receptor that interacts directly with both the cargo to become degraded and an autophagy modifier of the MAP1 LC3 family. Required both for the formation and autophagic degradation of polyubiquitin-containing bodies, called ALIS (aggresome-like induced structures) and links ALIS to the autophagic machinery. Involved in midbody ring degradation. May regulate the activation of NFKB1 by TNF-alpha, nerve growth factor (NGF) and interleukin- 1. May play a role in titin/TTN downstream signaling in muscle cells. May regulate signaling cascades through ubiquitination. Adapter that mediates the interaction between TRAF6 and CYLD (By similarity). May be involved in cell differentiation, apoptosis, immune response and regulation of K(+) channels. .|
|Tissue Specificity||Ubiquitously expressed. .|
|Sequence Similarities||Contains 1 PB1 domain.|
|Subcellular Localization||Cytoplasm. Late endosome. Lysosome. Cytoplasmic vesicle, autophagosome. Nucleus. Endoplasmic reticulum. Cytoplasm, P-body. Sarcomere (By similarity). In cardiac muscles localizes to the sarcomeric band (By similarity). Commonly found in inclusion bodies containing polyubiquitinated protein aggregates. In neurodegenerative diseases, detected in Lewy bodies in Parkinson disease, neurofibrillary tangles in Alzheimer disease, and HTT aggregates in Huntington disease. In protein aggregate diseases of the liver, found in large amounts in Mallory bodies of alcoholic and nonalcoholic steatohepatitis, hyaline bodies in hepatocellular carcinoma, and in SERPINA1 aggregates. Enriched in Rosenthal fibers of pilocytic astrocytoma. In the cytoplasm, observed in both membrane-free ubiquitin- containing protein aggregates (sequestosomes) and membrane- surrounded autophagosomes. Colocalizes with TRIM13 in the perinuclear endoplasmic reticulum. Co-localizes with TRIM5 in the cytoplasmic bodies. .|
|Alternative 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;|
|Research Areas|||signal transduction|signaling pathway|nuclear signaling|nfkb pathway| signal transduction|protein trafficking|vesicle transport|regulation| epigenetics and nuclear signaling|transcription|polymerase associated factors|pol ii transcription| cardiovascular|heart|autophagy|autophagosome| metabolism|pathways and processes|metabolism processes|autophagy and mitophagy| cancer|cell death||
Background for Sequestosome-1
Dilution Ratios/Recommended Concentrations
At Boster we strive to provide the best Anti-SQSTM1/p62 Antibody by testing all applications on non-spiked tissues and cell lines to ensure that the affinity of the antibody is enough to react to the endogenouse level of the target protein. Read more about our QC panel here.
|Recommended dilution ratios are listed below:|
Immunocytochemistry , 0.5-1μg/ml, Human, Mouse, Rat|
Immunohistochemistry(Paraffin-embedded Section), 0.5-1μg/ml, Human, Rat, Mouse, By Heat
Western blot, 0.1-0.5μg/ml, Human, Rat, Mouse
**Boster provides high sensitivity secondary antibody kits for Western blotting and IHC. For more info see Related Products below.
Anti-SQSTM1/p62 Antibody Images
Click the images to enlarge.
Lane 1: Rat Brain Tissue Lysate
Lane 2: HELA Cell Lysate
Lane 3: U87 Cell Lysate
Lane 4: A549 Cell Lysate
IHC(P): Human Intestinal Cancer Tissue
ICC: Hela Cell
1. Post-translational modification:phosphorylation, methylation, glycosylation etc. These modifications prevent SDS molecules from binding to the target protein and thus make the band size appear larger than expected
2. Post-translational cleavage: this can cause smaller bands and or multiple bands
3. Alternative splicing: the same gene can have alternative splicing patterns generating different size proteins, all with reactivities to the antibody.
4. Amino Acid R chain charge: SDS binds to positive charges. The different size and charge of the Amino Acid side chains can affect the amount of SDS binding and thus affect the observed band size.
5. Multimers: Multimers are usually broken up in reducing conditions. However if the interactions between the multimers are strong, the band may appear higher.,