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Purified Mouse Anti-p62 Ick ligand
Purified Mouse Anti-p62 Ick ligand

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.

Purified Mouse Anti-p62 Ick ligand

Immunofluorescence staining on FHs cells (normal human fetal lung fibroblasts; ATCC HTB-157)

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)

Product Details
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BD Transduction Laboratories™
Zeta Interacting Protein (ZIP); SQSMT1
Human (QC Testing)
Mouse IgG1, κ
Human p62 lck ligand aa. 257-437
Western blot (Routinely Tested), Immunofluorescence (Tested During Development), Immunohistochemistry, Immunoprecipitation (Not Recommended)
62 kDa
250 µg/ml
AB_398152
Aqueous buffered solution containing BSA, glycerol, and ≤0.09% sodium azide.
RUO


Preparation And Storage

Store undiluted at -20°C. The monoclonal antibody was purified from tissue culture supernatant or ascites by affinity chromatography.

Product Notices

  1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
  2. Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
  3. Source of all serum proteins is from USDA inspected abattoirs located in the United States.
  4. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
610833 Rev. 2
Antibody Details
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3/P62 LCK LIGAND

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.

610833 Rev. 2
Format Details
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Purified
Tissue culture supernatant is purified by either protein A/G or affinity purification methods. Both methods yield antibody in solution that is free of most other soluble proteins, lipids, etc. This format provides pure antibody that is suitable for a number of downstream applications including: secondary labeling for flow cytometry or microscopy, ELISA, Western blot, etc.
Purified
610833 Rev.2
Citations & References
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Development References (5)

  1. 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). View Reference
  2. 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). View Reference
  3. 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). View Reference
  4. 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). View Reference
  5. 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). View Reference
View All (5) View Less
610833 Rev. 2

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Comparisons, where applicable, are made against older BD Technology, manual methods or are general performance claims.  Comparisons are not made against non-BD technologies, unless otherwise noted.

For Research Use Only. Not for use in diagnostic or therapeutic procedures.