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Ubiquitin

Ubiquitin is a small (8.5 kDa) regulatory protein that has been found in almost all tissues (ubiquitously) of eukaryotic organisms. It was discovered in 1975 by Goldstein and further characterized throughout the 1970s and 1980s. There are four genes in the human genome that produce ubiquitin: UBB, UBC, UBA52 and RPS27A. Ubiquitination is a post-translational modification (an addition to a protein after it has been made) where ubiquitin is attached to a substrate protein. The addition of ubiquitin can affect proteins in many ways: It can signal for their degradation via the proteasome, alter their cellular location, affect their activity, and promote or prevent protein interactions. Ubiquitination is carried out in three main steps: activation, conjugation, and ligation, performed by ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s), and ubiquitin ligases (E3s), respectively. The result of this sequential cascade binds ubiquitin to lysine residues on the protein substrate via an isopeptide bond or to the amino group of the protein's N-terminus via a peptide bond. The protein modifications can be either a single ubiquitin protein (monoubiquitination) or a chain of ubiquitin (polyubiquitination). The ubiquitination bonds are always formed with one of the seven lysine residues from the ubiquitin molecule. These 'linking' lysines are represented by a "K" (which is the one-letter amino acid notation of lysine) and a number, referring to its position in the ubiquitin molecule. First, a ubiquitin molecule is bonded by its C-terminus to a specific lysine residue (e.g. K48, K29, K63,…) on the target protein. Poly-ubiquitination occurs when the C-terminus of another ubiquitin, will be linked again to a lysine residue (for example again K48 or K29) on the previously added ubiquitin molecule, forming a chain. This process repeats several times, leading to the addition of several ubiquitins. Only poly-ubiquitination on defined lysines, mostly on K48 and K29, is related to degradation with the proteasome (referred to as the "molecular kiss of death"), while other polyubiquitinations (e.g. on K63, K11, K6) and monoubiquitinations may regulate processes such as endocytic trafficking, inflammation, translation and DNA repair.

Ubiquitin Target Details

Target Name: Ubiquitin

Publications (9)

1
Identification of metabolic enzymes in renal cell carcinoma utilizing PROTEOMEX analyses. Lichtenfels R, Kellner R, Atkins D, Bukur J, Ackermann A, Beck J, Brenner W, Melchior S, Seliger B. Biochimica et biophysica acta. 2003 1646:21-31. [PubMed:12637008]
2
Alzheimer disease-specific conformation of hyperphosphorylated paired helical filament-Tau is polyubiquitinated through Lys-48, Lys-11, and Lys-6 ubiquitin conjugation. Cripps D, Thomas SN, Jeng Y, Yang F, Davies P, Yang AJ. The Journal of biological chemistry. 2006 281:10825-38. [PubMed:16443603]
3
A drosophila model for amyotrophic lateral sclerosis reveals motor neuron damage by human SOD1. Watson MR, Lagow RD, Xu K, Zhang B, Bonini NM. The Journal of biological chemistry. 2008 283:24972-81. [PubMed:18596033] [PMC:PMC2529125]
4
RanBP2 and SENP3 function in a mitotic SUMO2/3 conjugation-deconjugation cycle on Borealin. Klein UR, Haindl M, Nigg EA, Muller S. Molecular biology of the cell. 2009 20:410-8. (WB) [PubMed:18946085] [PMC:PMC2613119]
5
Suppression of the deubiquitinating enzyme USP5 causes the accumulation of unanchored polyubiquitin and the activation of p53. Dayal S, Sparks A, Jacob J, Allende-Vega N, Lane DP, Saville MK. The Journal of biological chemistry. 2009 284:5030-41. [PubMed:19098288] [PMC:PMC2696100]
6
COP9 signalosome- and 26S proteasome-dependent regulation of SCFTIR1 accumulation in Arabidopsis. Stuttmann J, Lechner E, Gurois R, Parker JE, Nussaume L, Genschik P, Nol LD. The Journal of biological chemistry. 2009 284:7920-30. (WB; Plant) [PubMed:19147500] [PMC:PMC2658085]
7
Analysis of macroautophagy by immunohistochemistry. Rosenfeldt MT, Nixon C, Liu E, Mah LY, Ryan KM. Autophagy. 2012 8:963-9. (IHC; Mouse) [PubMed:22562096] [PMC:PMC3427261]
8
Requirement of PML SUMO interacting motif for RNF4- or arsenic trioxide-induced degradation of nuclear PML isoforms. Maroui MA, Kheddache-Atmane S, El Asmi F, Dianoux L, Aubry M, Chelbi-Alix MK. PloS one. 2012 7:e44949. (WB; Human) [PubMed:23028697] [PMC:PMC3445614]
9
Acute ethanol exposure reduces serotonin receptor 1A internalization by increasing ubiquitination and degradation of ß-arrestin2. Deborah J Luessen, Haiguo Sun, Molly M McGinnis, Michael Hagstrom, Glen Marrs, Brian A McCool, Rong Chen. The Journal of biological chemistry. 2019 September;294:14068-14080. [Full Text Article] [PubMed:31366729] [PMC:PMC6755807] Related Antibodies: LS-C76671.
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31.25 - 2000 pg/ml
Colorimetric - 450nm (TMB)
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1 Plate/$651
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62.5 - 4000 pg/ml
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25 - 500 ng/ml
Colorimetric - 450nm (TMB)
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1 Plate/$913
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62.5 - 4000 pg/ml
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1 Plate/$728
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3.125 - 200 pg/ml
Colorimetric - 450nm (TMB)
1 Plate/$728
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96-Well Strip Plate
Rabbit
2.5 - 160 pg/ml
Colorimetric - 450nm (TMB)
1 Plate/$728
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96-Well Strip Plate
Porcine
62.5 - 4000 pg/ml
Colorimetric - 450nm (TMB)
1 Plate/$728
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Mouse
12.5 - 800 ng/ml
Colorimetric - 450nm (TMB)
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500 Wells/$1,178; 1000 Wells/$1,739
Ubiquitin ELISA Kit
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Development Kit
Antibody Pair and Standard
Human
12.5 - 800 ng/ml
Colorimetric - 450nm (TMB)
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500 Wells/$1,178; 1000 Wells/$1,739
Ubiquitin ELISA Kit
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Development Kit
Antibody Pair and Standard
Rat
12.5 - 800 ng/ml
Colorimetric - 450nm (TMB)
Plasma, Serum
500 Wells/$1,178; 1000 Wells/$1,739
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12 x 8-Well Microstrips
Mouse
12.5 - 800 pg/ml
Chemiluminescent
Plasma, Serum
1 Plate/$728
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12 x 8-Well Microstrips
Human
15.625 - 1000 pg/ml
Chemiluminescent
Plasma, Serum
1 Plate/$728
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96-Well Strip Plate
Mouse
1 - 25 ng/ml
Colorimetric - 450nm (TMB)
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1 Plate/$913
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Rat
250 - 5000 pg/ml
Colorimetric - 450nm (TMB)
Plasma, Serum
1 Plate/$913
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The data on this page has been compiled from LifeSpan internal sources, the National Center for Biotechnology Information (NCBI), and The Universal Protein Resource (UniProt).