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Details for Product No. ABIN152476

Ubiquitin antibody

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CG11624, DmUb, DmUbi-p63E, Dmel\\CG11624, Ub, Ubi-P63e, Ubi-p, Ubi63E, Ubi63p, Ubip, Ubiq, Ubp, ubi, ubi-p63E, ubi63E, CG18282, CG32744, CR32744, DmUbi-p5E, Dmel\\CG32744, ubiquitin, si:dz180g5.5, si: ... show more
»Alternatives Cow (Bovine), Caenorhabditis elegans (C. elegans), Chicken, Fruit Fly (Drosophila melanogaster), Human, Mouse (Murine), Plant
»Alternatives Mouse
Clonality (Clone) Monoclonal ()
»Alternatives Un-conjugated
»Alternatives Immunohistochemistry (Frozen Sections) (IHC (fro)), ELISA, Immunocytochemistry (ICC), Immunofluorescence (IF), Western Blotting (WB), Immunohistochemistry (Paraffin-embedded Sections) (IHC (p))
Pubmed 14 references available
Catalog no. ABIN152476
Quantity 50 µL
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Immunogen Purified ubiquitin conjugated to keyhole limpet hemocyanin with glutaraldehyde.
Clone Ubi-1
Isotype IgG1
Specificity ABIN152476 specifically recognizes ubiquitinated cytoplasmic inclusion bodies. Species Reactivity: ABIN152476 reacts with human, bovine, mouse, chicken, Drosophila, C. elegans, andArabidopsis thaliana (plant) ubiquitin and ubiquitinated proteins in ELISA reactions. Thisantibody recognizes polyubiquitin chains much more strongly than monoubiquitinatedmolecules or free ubiquitin.
Purification Ascites
Background Ubiquitin is a highly conserved protein of about 8.5 kDa molecular weight, which has anormal role in the targeting of proteins for proteolytic degradation. To perform thisfunction, the protein to be degraded is first covalently attached to the C-terminus ofubiquitin, and the ubiquitinated complex is then recognized by a complex of degradativeenzymes. Interestingly, ubiquitin also becomes covalently bonded to many types ofpathological inclusions, which appear to be resistant to normal degradation. Therefore,ubiquitin antibodies are very useful for studies of these inclusions. For example, theneurofibrillary tangles and paired helical filaments diagnostic of Alzheimer's disease,Lewy bodies seen in Parkinson's disease, and Pick bodies found in Pick's disease areall heavily ubiquitinated and can be readily visualized with ubiquitin antibodies. Alternate Names: anti-60S ribosomal protein L40 antibody, anti-HUBCEP52 antibody, anti-RPL40antibody, anti-Ubiquitin 52 amino acid fusion protein antibody, anti-Ubiquitin A52 residueribosomal protein fusion product 1 antibody, anti-Ubiquitin carboxyl extension protein 52antibody, anti-Ubiquitin CEP52 antibody.
Gene ID 6233, 22190
Research Area Neurology, Proteolysis / Ubiquitin, Alzheimer's Disease, Proteases, Amino Acids
Application Notes Immunohistochemistry 1:1000,Western Blot 1:5000,Immunohistochemistry-Paraffin 1:1000,Immunohistochemistry-Frozen 1:1000
Restrictions For Research Use only
Format Liquid
Concentration 5 mg/ml
Buffer Preservative: 5 mM sodium azide.
Preservative Sodium azide
Storage 4 °C
Hirano, Kimoto, Shimoyama et al.: "Identification of a neural alpha-catenin as a key regulator of cadherin function and multicellular organization." in: Cell, Vol. 70, Issue 2, pp. 293-301, 1992 (PubMed).

Shaw, Chau: "Ubiquitin and microtubule-associated protein tau immunoreactivity each define distinct structures with differing distributions and solubility properties in Alzheimer brain." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 85, Issue 8, pp. 2854-8, 1988 (PubMed).

Perry, Friedman, Shaw et al.: "Ubiquitin is detected in neurofibrillary tangles and senile plaque neurites of Alzheimer disease brains." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 84, Issue 9, pp. 3033-6, 1987 (PubMed).

Sternsdorf, Jensen, Will: "Evidence for covalent modification of the nuclear dot-associated proteins PML and Sp100 by PIC1/SUMO-1." in: The Journal of cell biology, Vol. 139, Issue 7, pp. 1621-34, 1998 (PubMed).

Cuervo, Hu, Lim et al.: "IkappaB is a substrate for a selective pathway of lysosomal proteolysis." in: Molecular biology of the cell, Vol. 9, Issue 8, pp. 1995-2010, 1998 (PubMed).

Verdier, Chruetien, Muller et al.: "Proteasomes regulate erythropoietin receptor and signal transducer and activator of transcription 5 (STAT5) activation. Possible involvement of the ubiquitinated Cis protein." in: The Journal of biological chemistry, Vol. 273, Issue 43, pp. 28185-90, 1998 (PubMed).

Laroia, Cuesta, Brewer et al.: "Control of mRNA decay by heat shock-ubiquitin-proteasome pathway." in: Science (New York, N.Y.), Vol. 284, Issue 5413, pp. 499-502, 1999 (PubMed).

Sternsdorf, Puccetti, Jensen et al.: "PIC-1/SUMO-1-modified PML-retinoic acid receptor alpha mediates arsenic trioxide-induced apoptosis in acute promyelocytic leukemia." in: Molecular and cellular biology, Vol. 19, Issue 7, pp. 5170-8, 1999 (PubMed).

Marti, Wirbelauer, Scheffner et al.: "Interaction between ubiquitin-protein ligase SCFSKP2 and E2F-1 underlies the regulation of E2F-1 degradation." in: Nature cell biology, Vol. 1, Issue 1, pp. 14-9, 1999 (PubMed).

Lichtenfels, Kellner, Atkins et al.: "Identification of metabolic enzymes in renal cell carcinoma utilizing PROTEOMEX analyses." in: Biochimica et biophysica acta, Vol. 1646, Issue 1-2, pp. 21-31, 2003 (PubMed).

Cripps, Thomas, Jeng et al.: "Alzheimer disease-specific conformation of hyperphosphorylated paired helical filament-Tau is polyubiquitinated through Lys-48, Lys-11, and Lys-6 ubiquitin conjugation." in: The Journal of biological chemistry, Vol. 281, Issue 16, pp. 10825-38, 2006 (PubMed).

Watson, Lagow, Xu et al.: "A drosophila model for amyotrophic lateral sclerosis reveals motor neuron damage by human SOD1." in: The Journal of biological chemistry, Vol. 283, Issue 36, pp. 24972-81, 2008 (PubMed).

Dayal, Sparks, Jacob et al.: "Suppression of the deubiquitinating enzyme USP5 causes the accumulation of unanchored polyubiquitin and the activation of p53." in: The Journal of biological chemistry, Vol. 284, Issue 8, pp. 5030-41, 2009 (PubMed).

Stuttmann, Lechner, Guuerois et al.: "COP9 signalosome- and 26S proteasome-dependent regulation of SCFTIR1 accumulation in Arabidopsis." in: The Journal of biological chemistry, Vol. 284, Issue 12, pp. 7920-30, 2009 (PubMed).

Alternatives for antigen "Ubiquitin", type "Antibodies"
Hosts (115), (100), (5), (3)
Reactivities (146), (80), (48), (47), (13), (11), (10), (7), (7), (7), (5), (5), (4), (4), (4), (4), (4), (4), (3), (3), (3), (3), (2), (2), (1), (1), (1)
Applications (159), (88), (86), (44), (38), (30), (26), (18), (15), (13), (4), (2), (2), (1)
Conjugates (4), (2), (1), (1), (1), (1), (1)
Epitopes (7), (5), (4), (2), (2), (2), (1), (1), (1), (1), (1), (1)