抗Ubiquitin抗体 | Anti-Ubiquitin Antibody

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	Western Blot: Ubiquitin Antibody [NB300-129] - Analysis of Hek 293 cell lysates using Rabbit pAb to ubiquitin (1:5000 dilution, green) and Mouse mAb to B-Tubulin (1:10000 dilution, red) used as a loading control. Cells were maintained in normal medium (Control-Ct) or treated with proteasome inhibitor lactacystin (Lc) at 10 um for 16 h. Lysed cells were electrophoresed on 4-20% SDS-PAGE, and blotted to PVDF membrane. Note the smeary-patterned reactivities detected above the 200kDa standard that presumably represent accumulation of ubiquitinated proteins in proteasome inhibitor-Lc treated cells. Prominent band at 8kDa corresponds to monoubiquitin
	Immunocytochemistry/Immunofluorescence: Ubiquitin Antibody [NB300-129] - Analysis of HeLa cells stained with rabbit pAb to ubiquitin, NB300-129, dilution 1:1,000 in red, and costained with chicken pAb to vimentin, dilution 1:10,000, in green. The blue is DAPI staining of nuclear DNA. [A] Control HeLa cells maintained in normal medium, [B] HeLa cells treated with 10uM of the proteasome inhibitor lactacystin (Lc) for 24 hours. Proteasomal inhibition leads to formation of strongly ubiquitin positive cytoplasmic inclusions. Note the diffuse cytoplasmic ubiquitin staining in control cells and well defined ubiquitin positive inclusions in the Lc treated cells.
	Immunohistochemistry-Paraffin: Ubiquitin Antibody [NB300-129] - IHC staining of Ubiquitin in human rectal cancer using DAB with hematoxylin counterstain.
	Immunocytochemistry/Immunofluorescence: Ubiquitin Antibody [NB300-129] - Immunofluorescent staining of aggresomes of mouse L-cells treated with lactacysteine, using NB300-129.

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Background

Ubiquitin is a highly conserved protein with nuclear/cytoplasmic localization and is an essential player in the ubiquitin-proteasome pathway, wherein it plays ATP dependent role in targeting of proteins for proteolytic degradation. In ubiquitination process, ubiquitin is first activated by forming a thiolester complex with the activation component E1, which is then transferred to ubiquitin-carrier protein E2, followed by to ubiquitin ligase E3 for final delivery to epsilon-NH2 of the target protein lysine residue. IkB, p53, cdc25A, Bcl-2 etc. have been shown as targets of ubiquitin-proteasome process as part of regulation of cell cycle progression, differentiation, cell stress response, and apoptosis. Moreover, ubiquitin have been reported to bind covalently with pathological inclusions which are resistant to degradation e.g. neurofibrillary tangles/paired helical filaments in Alzheimer's disease, Lewy bodies seen in Parkinson's disease, and Pick bodies found in Pick's disease etc.

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