Ubiquitin

Ubiquitin is a highly conserved globular 76 amino acid protein of about 8.5kD molecular weight. It has a important role in the targeting of proteins for proteolytic degradation. Proteins to be degraded are covalantly coupled to the C-terminus of ubiquitin by means of ubiquitin ligases. The ubiquitin itself is frequently also ubiquitinated, producing a polyubiquitin chain. The polyubquitinated complex is then recognized by a complex of degradative enzymes which together form the proteosome. Interestingly, ubiquitin also becomes covalently bonded to many types of pathological inclusions seen in serious human disease states which appear to be resistant to normal degradation, so that ubiquitin antibodies are very useful for studies of these inclusions. For example the neurofibrillary tangles and paired helical filaments diagnostic of Alzheimer's disease, the Lewy bodies seen in Parkinson's disease, and Pick bodies found in Pick's disease are all heavily ubiquitinated and can all be readily visualized with ubiquitin antibodies of appropriate specificity.\n\nApplications:\nSuitable for use in Immunocytochemistry, Immunofluorescence and Western Blot. Other applications not tested.\n\nRecommended Dilution:\nImmunocytochemistry (ABC): 1:1000\nImmunofluorescence: 1:500\nOptimal dilutions to be determined by the researcher.\n\nStorage and Stability:\nMay be stored at 4 degrees C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Aliquots are stable for 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

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SPECIFICATIONS

Catalog Number

031435

Size

100ul

Applications

ICC, IF, WB

Hosts

Mouse

Reactivities

Hum, Rat, Bov, Ch/Bird, Dro/Arth

Form

Supplied as a liquid in 10mM sodium azide.

P Type

Mab

Purity

Ascites

Isotype

IgG1,k

References

Perry, G. et al. Proc. Natl. Acad. Sci. USA 84, 3033-3036 (1987)\nShaw, G. and Chau, V. Proc. Natl. Acad. Sci. USA 85, 2854-2858 (1988)\nHirano, S., et al. Cell 70: 293-301 (1992) \nCuervo, A.M., et al. Mol. Biol. 9: 1995-2010 (1995)\nSternsdorf, T., et al. J. Cell Biol. 139: 1621-1634 (1997)\nTae-Wan Kim, et al. J. Biol. Chem. 272: 11006-11010 (1997)\nVerdier, F., et al. J. Cell Biol. 273: 28185-28190 (1998)\nLaroia, G., et al. Science 284: 499-502 (1999)\nMarti, A., et al. Nature Cell Biol. 1: 14-19 (1999)\nSternsdorf, T., et al. Mol. Cell Biol. 19: 5170-5178 (1999)\n\nFortun J, Go JC, Li J, Amici SA, Dunn WA Jr, Notterpek L. Alterations in degradative pathways and protein aggregation in a neuropathy model based on PMP22 overexpression. Neurobiol Dis. 22:153-164 (2006).\n\nBoutajangout A, Authelet M, Blanchard V, Touchet N, Tremp G, Pradier L, Brion JP. Characterisation of cytoskeletal abnormalities in mice transgenic for wild-type human tau and familial Alzheimer's disease mutants of APP and presenilin-1. Neurobiol Dis. 15:47-60 (2004).\n\nWang DS, Bennett DA, Mufson EJ, Mattila P, Cochran E, Dickson DW. Contribution of changes in ubiquitin and myelin basic protein to age-related cognitive decline. Neurosci. Res. 48:93-100 (2004).\n\nHe CZ, Hays AP. Expression of peripherin in ubiquinated inclusions of amyotrophic lateral sclerosis. J. Neurol. Sci. 217:47-54 (2004).\n\nUngureanu D, Saharinen P, Junttila I, Hilton DJ, Silvennoinen O. Regulation of Jak2 through the ubiquitin-proteasome pathway involves phosphorylation of Jak2 on Y1007 and interaction with SOCS-1. Mol Cell Biol. 22:3316-26 (2002).\n\nWirbelauer C, Sutterluty H, Blondel M, Gstaiger M, Peter M, Reymond F, Krek W. The F-box protein Skp2 is a ubiquitylation target of a Cul1-based core ubiquitin ligase complex: evidence for a role of Cul1 in the suppression of Skp2 expression in quiescent fibroblasts. EMBO J. 19:5362-75 (2000).\n\nHarris KF, Shoji I, Cooper EM, Kumar S, Oda H, Howley PM. Ubiquitin-mediated degradation of active Src tyrosine kinase. Proc Natl Acad Sci U S A. 96:13738-43 (1999).\n\nSternsdorf T, Puccetti E, Jensen K, Hoelzer D, Will H, Ottmann OG, Ruthardt M. PIC-1/SUMO-1-modified PML-retinoic acid receptor alpha mediates arsenic trioxide-induced apoptosis in acute promyelocytic leukemia. Mol Cell Biol. 19:5170-8 (1999).\n\nMarti A, Wirbelauer C, Scheffner M, Krek W. Interaction between ubiquitin-protein ligase SCFSKP2 and E2F-1 underlies the regulation of E2F-1 degradation. Nat Cell Biol. 1:14-9 (1999).

Additional Info

Recognizes other ubiquitinated inclusion bodies such as the Lewy bodies of Parkinson's disease and the Pick bodies in Pick's disease in formalin fixed tissues. Will recognize human, bovine, chicken, Drosophila, and C. elegans in ELISA. Excellent for the detection of ubiquitinated inclusions seen in human neurodegenerative diseases such as the neurofibrillary tangles of Alzheimer's disease.