Anti-Multi Ubiquitin mAb

  • Applications
    • WB
  • Target Ubiquitin
  • Host Species Mouse
  • Species Reactivities Human
  • Code # D058-3
  • Size 100 μg
  • Price
    $306.33
Specifications

Background

Ubiquitin is a polypeptide of 76 amino acid residues, and widely distributed protein in eukaryotic cells. This protein is also highly conserved among eukaryotic cells. Recently several reports showed that intracellular abnormal and short-lived proteins are degradated through an ubiquitin dependent proteolytic pathway. In the ubiquitin dependent pathway, a target protein is tagged with multi-ubiquitin molecules.
  • Antibody Type:
    Monoclonal
  • Application:
    WB
  • Clone Number:
    FK2
  • Concentration:
    1 mg/mL
  • Conjugate:
    Unlabeled
  • Description:
    Monoclonal antibody of 100 μg targeting Ubiquitin for WB.
  • Formulation:
    100 μg IgG in 100 μl volume of PBS containing 50% glycerol, pH 7.2. No preservative iscontained.
  • Host Species:
    Mouse
  • Immunogen:
    Lysozyme - poly-ubiquitin was purified crude
  • Isotype:
    IgG1
  • Product Type:
    Antibody
  • Reactivity:
    This antibody reacts with multiubiquitin chains, but it doesn’t react with mono ubiquitinand free ubiquitin on Western blotting.
  • Research Area:
    Autophagy
  • Short Description:
    Ubiquitin Monoclonal Antibody.
  • Size:
    100 μg
  • Species Reactivity:
    Human
  • Storage Temperature:
    -20°C
  • Target:
    Ubiquitin
Citations
  1. Broering TJ et al. Carboxyl-proximal regions of reovirus nonstructural protein muNS necessary and sufficient for forming factory-like inclusions. J Virol. 79, 6194-6206 (2005),
  2. Choi UY et al. Polyubiquitin chain-dependent protein degradation in TRIM30 cytoplasmic bodies. Exp. Mol.Med. 47, e159 (2015),
  3. Ebina M et al. Myeloma overexpressed 2 (Myeov2) regulates L11 subnuclear localization through Nedd8 modification. PLoS One. 8, e65285 (2013),
  4. Furuya N et al. PARK2/Parkin-mediated mitochondrial clearance contributes to proteasome activation during slow-twitch muscle atrophy via NFE2L1 nuclear translocation. Autophagy 10, 631-41 (2014),
  5. Gitcho MA et al. VCP mutations causing frontotemporal lobar degeneration disrupt localization of TDP-43 and induce cell death. J Biol Chem. 284, 12384-98 (2009),
  6. Hosokawa H et al. Regulation of Th2 cell development by Polycomb group gene bmi-1 through the stabilization of GATA3. J Immunol. 177, 7656-64 (2006),
  7. Hwang GW et al. Overexpression of Rad23 confers resistance to methylmercury in saccharomyces cerevisiae via inhibition of the degradation of ubiquitinated proteins. Mol Pharmacol. 68, 1074-8 (2005),
  8. Inukai N et al. A novel hydrogen peroxide-induced phosphorylation and ubiquitination pathway leading to RNA polymerase II proteolysis. J Biol Chem. 279, 8190-5 (2004),
  9. Ishioka T et al. Impairment of the ubiquitin-proteasome system by cellular FLIP. Genes Cells 12, 735-44 (2007),
  10. Katoh K et al. The ALG-2-interacting protein Alix associates with CHMP4b, a human homologue of yeast Snf7 that is involved in multivesicular body sorting. J Biol Chem. 278, 39104-13 (2003),
  11. Komatsu M et al. Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice. Cell 131, 1149-1163 (2007),
  12. Masuda Y et al. ADRP/adipophilin is degraded through the proteasome-dependent pathway during regression of lipid-storing cells. J Lipid Res. 47, 87-98 (2006),
  13. Nakamura M et al. Clathrin anchors deubiquitinating enzymes, AMSH and AMSH-like protein, on early endosomes. Genes Cells 11, 593-606 (2006),
  14. Seino H et al. Two ubiquitin-conjugating enzymes, UbcP1/Ubc4 and UbcP4/Ubc11, have distinct functions for ubiquitination of mitotic cyclin. Mol Cell Biol. 23, 3497-3505 (2003),
  15. Shi W et al. Disassembly of MDC1 foci is controlled by ubiquitin-proteasome-dependent degradation. J Biol Chem. 283, 31608-16 (2008),
  16. Yamashita M et al. Ras-ERK MAPK cascade regulates GATA3 stability and Th2 differentiation through ubiquitin-proteasome pathway. J Biol Chem. 280, 29409-19 (2005)
References
  1. Ishioka, T., et al., Genes Cells 12, 735-744 (2007)
  2. Hosokawa, H., et al., J. Immunol. 177, 7656-7664 (2006)
  3. Masuda, Y., et al., J. Lipid Res. 47, 87-98 (2006)
  4. Nakamura, M., et al., Genes Cells 11, 593-606 (2006)
  5. Yamashita, M., et al., J. Biol. Chem. 280, 29409-29419 (2005)
  6. Hwang, G-W., et al., Mol. Pharmacol. 68, 1074-1078 (2005)
  7. Broering, T. J., et al., J. Virol. 79, 6194-6206 (2005)
  8. Inukai, N., et al., J. Biol. Chem. 279, 8190-8195 (2004)
  9. Katoh, K., et al., J. Biol. Chem. 278, 39104-39113 (2003)
  10. Seino, H., et al., Mol. Cell Biol. 23, 3497-3505 (2003)
  11. Yokosawa, N., et al., J. Virol. 76, 12683-12690 (2002)
  12. Takada, K., et al., Eur. J. Biochem. 233, 42-47 (1995)
  13. Fujimuro, M., et al., FEBS Lett. 349, 173-180 (1994)