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HOME > Product search results > Code No. MK-11-3 Anti-Ubiquitin mAb

Code No. MK-11-3

Anti-Ubiquitin mAb

Availability (in Japan)

10 or more

(In Japan at 00:05,
Sep 20, 2018 in JST)

Size

100 µg/100 µL

This antibody (Clone 1B3) does not react with multi ubiquitin.
Data
  • Western Blotting

Clonality Monoclonal Clone 1B3
Isotype (Immunized Animal) Mouse IgG1
Applications
WB
5 µg/mL  
IC*
reported.  (PMID: 16877356 / 12388748
IH*
reported.  (PMID: 16625204 / 15866887 / 14684739
Other(EM)
reported.  (PMID: 15866887
Immunogen (Antigen) Bovine erythrocyte ubiquitin
Reactivity [Gene ID]

Human, Mouse*(16625204/15866887), Bovine*(10339540)

Storage buffer 1 mg/mL in PBS/50% glycerol, pH 7.2
Storage temp. -20°C Conjugate Unlabeled Manufacturer MBL
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. There are several reports showed that intracellular abnormal and short-lived proteins are degraded through an ubiquitin dependent proteolytic pathway. In the ubiquitin dependent pathway, a target protein is tagged with multi-ubiquitin molecules.
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CM003-3 Anti-CHIP mAb
Citations

Western Blotting

  1. Hatakeyama S et al. Ubiquitin-dependent degradation of IkappaBalpha is mediated by a ubiquitin ligase Skp1/Cul 1/F-box protein FWD1. PNAS 96, 3859-63 (1999)(PMID:10097128)
  2. Yamanaka A et al. Cell cycle-dependent expression of mammalian E2-C regulated by the anaphase-promoting complex/cyclosome. Mol Biol Cell 11, 2821-2831 (2000)(PMID:10930472)
  3. Miyazaki K et al. NEDL1, a novel ubiquitin-protein isopeptide ligase for dishevelled-1, targets mutant superoxide dismutase-1. J Biol Chem. 279, 11327-35 (2004)(PMID:14684739)
  4. Uchida D et al. AIRE functions as an E3 ubiquitin ligase. J. Exp. Med. 199, 167-172 (2004)(PMID:14734522)
  5. Zhang HF et al. Cullin 3 promotes proteasomal degradation of the topoisomerase I-DNA covalent complex. Cancer Res. 64, 1114-21 (2004)(PMID:14871846)
  6. Akiyoshi H et al. Subcellular expression of autoimmune regulator is organized in a spatiotemporal manner. J Biol Chem. 279, 33984-91 (2004)(PMID:15150263)
  7. Hatakeyama S et al. Interaction of U-box-type ubiquitin-protein ligases (E3s) with molecular chaperones. Genes Cells. 9, 533-548 (2004)(PMID:15189447)
  8. Okumura F et al. Functional regulation of FEZ1 by the U-box-type ubiquitin ligase E4B contributes to neuritogenesis. J Biol Chem. 279, 53533-43 (2004)(PMID:15466860)
  9. Komatsu M et al. Impairment of starvation-induced and constitutive autophagy in Atg7-deficient mice. J. Cell Biol. 169, 425-34 (2005)(PMID:15866887)
  10. Waguri S, Komatsu M. Biochemical and morphological detection of inclusion bodies in autophagy-deficient mice. Methods Enzymol. 453, 181-96 (2009)(PMID:19216907)

Immunocytochemistry

  1. Nakamichi I et al. Formation of Mallory body-like inclusions and cell death induced by deregulated expression of keratin 18. Mol Biol Cell. 13, 3441-51 (2002)(PMID:12388748)
  2. Tanji K et al. NUB1 suppresses the formation of Lewy body-like inclusions by proteasomal degradation of synphilin-1. Am J Pathol. 169, 553-65 (2006)(PMID:16877356)

Immunohistochemistry

  1. Miyazaki K et al. NEDL1, a novel ubiquitin-protein isopeptide ligase for dishevelled-1, targets mutant superoxide dismutase-1. J Biol Chem. 279, 11327-35 (2004)(PMID:14684739)
  2. Komatsu M et al. Impairment of starvation-induced and constitutive autophagy in Atg7-deficient mice. J. Cell Biol. 169, 425-34 (2005)(PMID:15866887)
  3. Hara T et al. Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice. Nature 441, 885-9 (2006)(PMID:16625204)
  4. Mori F et al. Valosin-containing protein immunoreactivity in tauopathies, synucleinopathies, polyglutamine diseases and intranuclear inclusion body disease. Neuropathology 33, 637-44 (2013)(PMID:23782134)
  5. Kon T et al. ALS-associated protein FIG4 is localized in Pick and Lewy bodies, and also neuronal nuclear inclusions, in polyglutamine and intranuclear inclusion body diseases. Neuropathology 34, 19-26 (2014)(PMID:23888880)
  6. Mori F et al. G protein-coupled receptor 26 immunoreactivity in intranuclear inclusions associated with polyglutamine and intranuclear inclusion body diseases. Neuropathology 36, 50-5 (2016)(PMID:26303144)
  7. Shin H et al. The formation of multivesicular bodies in activated blastocysts is influenced by autophagy and FGF signaling in mice. Sci Rep. 7, 41986 (2017)(PMID:28155881)
  8. Mori F et al. Immunohistochemical localization of exoribonucleases (DIS3L2 and XRN1) in intranuclear inclusion body disease. Neurosci Lett. 662, 389-394 (2018)(PMID:29100804)

Other(EM)

  1. Nakamichi I et al. Formation of Mallory body-like inclusions and cell death induced by deregulated expression of keratin 18. Mol Biol Cell. 13, 3441-51 (2002)(PMID:12388748)
  2. Komatsu M et al. Impairment of starvation-induced and constitutive autophagy in Atg7-deficient mice. J. Cell Biol. 169, 425-34 (2005)(PMID:15866887)
Product category
Research area
Autophagy
Ubiquitin proteasome
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  • The availability is based on the information in Japan at 00:05, Sep 20, 2018 in JST.
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  • Abbreviations for applications:
    WB: Western Blotting, IH: Immunohistochemistry, IC: Immunocytochemistry, IP: Immunoprecipitation
    FCM: Flow Cytometry, NT: Neutralization, IF: Immunofluorescence, RIP: RNP Immunoprecipitation
    ChIP: Chromatin Immunoprecipitation, CoIP: Co-Immunoprecipitation
  • For applications and reactivity:
    *: The use is reported in a research article (Not tested by MBL). Please check the data sheet for detailed information.
    **: The use is reported from the licenser (Under evaluation or not tested by MBL).
  • For storage temparature: RT: room temparature
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