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Western blot analysis of p62 Ick ligand on a HCT-8 (human colorectal adenocarcinoma; ATCC CCL-244) cell lysate. Lane 1: 1:500, lane 2: 1:1000, lane 3: 1:2000 dilution of the anti- p62 Ick ligand antibody.
Immunofluorescence staining on FHs cells (normal human fetal lung fibroblasts; ATCC HTB-157)
BD Transduction Laboratories™ Purified Mouse Anti-p62 Ick ligand
BD Transduction Laboratories™ Purified Mouse Anti-p62 Ick ligand
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제품 고시
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
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관련 제품
p62 lck ligand (zeta-interacting protein (ZIP)) is a cytoplasmic protein that binds to the SH2 domain of lck (a T cell src tyrosine kinase) in the absence of a phosphotyrosine in either protein. The ubiquitously expressed p62 lck ligand contains a cysteine rich region that is similar to a zinc finger domain, a G protein binding region, a PEST sequence, and several phosphorylation sites. Deletion of the p62 lck ligand N-terminal domain has been reported to abrogate its binding to lck. However, mutation of the tyrosine did not have an effect. In addition, p62 lck ligand binds to the pseudosubstrate region of the PKCζ catalytic domain. In turn, PKCζ phosphorylates p62. p62 lck ligand binds to the dimerization region of PKCζ, thereby inhibiting PKCζ-PKCζ interaction. This suggests that p62 lck ligand may compete with PKCζ. However, it requires PKCζ for proper subcellular localization. These data suggest that p62 lck ligand may be part of the protein bridge that links PKCζ to the tyrosine kinases involved in signaling pathways.
개발 참고 자료 (5)
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Bjørkøy G, Lamark T, Pankiv S, Øvervatn A, Brech A, Johansen T. Monitoring autophagic degradation of p62/SQSTM1. Methods Enzymol. 2009; 452:181-197. (Clone-specific: Western blot). 참조 보기
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Cariou B, Perdereau D, Cailliau K, et al. The adapter protein ZIP binds Grb14 and regulates its inhibitory action on insulin signaling by recruiting protein kinase Czeta. Mol Cell Biol. 2002; 22(20):6959-6970. (Biology: Western blot). 참조 보기
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Joung I, Strominger JL, Shin J. Molecular cloning of a phosphotyrosine-independent ligand of the p56lck SH2 domain. Proc Natl Acad Sci U S A. 1996; 93(12):5991-5995. (Biology). 참조 보기
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Puls A, Schmidt S, Grawe F, Stabel S. Interaction of protein kinase C zeta with ZIP, a novel protein kinase C-binding protein. Proc Natl Acad Sci U S A. 1997; 94(12):6191-6196. (Biology). 참조 보기
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Wooten MW, Seibenhener ML, Mamidipudi V, Diaz-Meco MT, Barker PA, Moscat J. The atypical protein kinase C-interacting protein p62 is a scaffold for NF-kappaB activation by nerve growth factor. J Biol Chem. 2001; 276(11):7709-7712. (Biology: Immunoprecipitation, Western blot). 참조 보기
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