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U5382

Sigma-Aldrich

Ubiquitin human

≥95% (SDS-PAGE), recombinant, expressed in E. coli (N-terminal FLAG® tagged), essentially salt-free, lyophilized powder

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CAS Number:
MDL number:
NACRES:
NA.32

biological source

human

Quality Level

recombinant

expressed in E. coli (N-terminal FLAG® tagged)

assay

≥95% (SDS-PAGE)

form

essentially salt-free, lyophilized powder

mol wt

10 kDa

technique(s)

mass spectrometry (MS): suitable

solubility

0.05 M Tris pH 7.5: ≥10 mg/mL

UniProt accession no.

storage temp.

−20°C

Gene Information

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This Item
U6253U5507U5379
vibrant-m

U5382

Ubiquitin human

vibrant-m

U6253

Ubiquitin from bovine erythrocytes

vibrant-m

U5507

Ubiquitin human

biological source

human

biological source

bovine erythrocytes

biological source

human

biological source

rabbit

technique(s)

mass spectrometry (MS): suitable

technique(s)

western blot: suitable

technique(s)

ligand binding assay: suitable

technique(s)

immunohistochemistry (frozen sections): suitable, western blot: 1:100 using ubiquitin purified from bovine red blood cells

recombinant

expressed in E. coli (N-terminal FLAG® tagged)

recombinant

-

recombinant

expressed in E. coli (N-terminal histidine tagged)

recombinant

-

mol wt

10 kDa

mol wt

-

mol wt

10.7 kDa

mol wt

antigen 8.6 kDa

form

essentially salt-free, lyophilized powder

form

essentially salt-free, lyophilized powder

form

lyophilized powder

form

lyophilized powder

General description

Ubiquitin is a highly conserved globular protein and has lysine in the surface. The C-terminal end comprises the Leu-Arg-Gly-Gly structural motif.

Application

Ubiquitin human can be used as a standard for mass spectrometry.
Ubiquitin human has been used in mono-ubiquitination of yeast proliferating cell nuclear antigen (PCNA) and in in vitro ubiquitination assay of defective in mitotic arrest 1 (Dma1)
Ubiquitin, N-terminal FLAG-tagged can replace the ubiquitin in formation of poly-ubiquitin—protein conjugates. The FLAG tag enables separation and enrichment of the protein conjugates on anti-FLAG affinity columns and detection of conjugates in western blot by anti-FLAG antibodies.

Biochem/physiol Actions

Ubiquitin interacts with the lysine residue of proteins through its ε-amino group of the C-terminal glycine residue. Proteins interacting with ubiquitin either undergo mono-ubiquitination or multi-mono-ubiquitination via a three-step process. Ubiquitination regulates intracellular trafficking and protein degradation and an imbalance in the pathway is implicated in disorders.
Ubiquitin is a small regulatory protein present in eukaryote tissues. Exogenous ubiquitin can stimulate apoptosis in numerous cell lines. E7 protein of human papilloma virus-16 stimulates Retinoblastoma Protein degradation via Ubiquitin-Proteasome Pathway.

Packaging

Package size based on protein content

Preparation Note

Ubiquitin human can be dissolved in 0.05 M Tris-HCl at a concentration of 10.00 - 11.00 mg/ml to yield a clear to slightly hazy, colorless solution.

Legal Information

FLAG is a registered trademark of Merck KGaA, Darmstadt, Germany

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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Customers Also Viewed

David Komander
Biochemical Society transactions, 37(Pt 5), 937-953 (2009-09-17)
Protein ubiquitination and protein phosphorylation are two fundamental regulatory post-translational modifications controlling intracellular signalling events. However, the ubiquitin system is vastly more complex compared with phosphorylation. This is due to the ability of ubiquitin to form polymers, i.e. ubiquitin chains
Ana Camara-Artigas et al.
Acta crystallographica. Section F, Structural biology communications, 72(Pt 1), 29-35 (2016-01-12)
Ubiquitin is a small globular protein that has a considerable number of lysine residues on its surface. This results in a high surface entropy that precludes the formation of crystal-packing interactions. To date, only a few structures of the native
Boris Macek et al.
Molecular & cellular proteomics : MCP, 5(5), 949-958 (2006-02-16)
Top-down proteomics, the analysis of intact proteins (instead of first digesting them to peptides), has the potential to become a powerful tool for mass spectrometric protein characterization. Requirements for extremely high mass resolution, accuracy, and ability to efficiently fragment large
Sara Hernández-Ortega et al.
The Journal of biological chemistry, 288(7), 4704-4714 (2012-12-25)
Progression through the G(1) phase of the cell cycle is controlled by diverse cyclin-dependent kinases (CDKs) that might be associated to numerous cyclin isoforms. Given such complexity, regulation of cyclin degradation should be crucial for coordinating progression through the cell
B L Brizzard et al.
BioTechniques, 16(4), 730-735 (1994-04-01)
The FLAG epitope is an eight amino acid peptide (AspTyrLysAspAspAspAspLys) that is useful for immunoaffinity purification of fusion proteins. A monoclonal antibody (anti-FLAG M1) that binds the FLAG epitope in a calcium-dependent manner and requires an N-terminal FLAG sequence has

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