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U5507

Sigma-Aldrich

Ubiquitin human

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

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About This Item

CAS Number:
MDL number:
UNSPSC Code:
41106500
NACRES:
NA.32

biological source

human

Quality Level

recombinant

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

assay

≥95% (GE)

form

lyophilized powder

mol wt

10.7 kDa

technique(s)

ligand binding assay: suitable

solubility

Tris-HCl, pH 7.5: 1.0—1.10 mg/mL, clear to slightly hazy, colorless

suitability

suitable for molecular biology

UniProt accession no.

storage temp.

−20°C

Gene Information

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General description

Research Area: CANCER
Ubiquitin is a highly conserved protein composed of 76 amino acids, and it is expressed universally in all eukaryotes, ranging from yeast to humans.
Ubiquitin, a globular protein is made of 76 amino acids and has lysine residues on its surface. It has a molecular weight of 8565 Da.N-Terminal histidine-tagged ubiquitin can replace native ubiquitin in the formation of poly-ubiquitin—protein conjugates. The histidine tag enables the separation and enrichment of protein conjugates on a Ni(II) column and the detection of conjugates in western blot by anti-histidine-tag antibodies.

Application

Ubiquitin human can be used as a test compound for studying the isolation and characterization of rice E3-ubiquitin ligase and the role of OsHOS1 gene in the modulation of the cold stress response.
Ubiquitin human has been used:
  • as a substrate in in vitro ubiquitination assays
  • as substrate in ADP-ribosylation and ubiquitylation assays
  • to supplement the 64 ng of endogenous ubiquitin in fresh blood for experiment grouping in order to study its potential clinical impact on cancer prognosis

Biochem/physiol Actions

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.
Ubiquitin plays a key role in normal eukaryotic cell function. It participates in the development and function of the immune system. This immunophilin is also known to participate in immune homeostasis. The ubiquitin peptide fragment (U50-59) is capable of blocking cellular and humoral immunity.
Ubiquitin-mediated proteolysis plays an important role in several basic cellular processes including regulation of cell cycle and division, differentiation and development, modulation of cell-surface receptors, the secretory pathway (protein transport), morphogenesis of neuronal networks, transcriptional regulation and signal transduction, transcriptional silencing, DNA repair, long-term memory, and circadian rhythms.

Preparation Note

Ubiquitin human can dissolved in 0.02 M Tris-HCl at a concentration of 1.00 - 1.10 mg/ml to yield a clear to slightly hazy, colorless solution.

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)


Certificates of Analysis (COA)

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New crystal form of human ubiquitin in the presence of magnesium
Camara-Artigas A, et al.
Acta Crystallographica. Section F, Structural Biology Communications, 72(1), 29-35 (2016)
Extracellular Ubiquitin is the Causal Link between Stored Blood Transfusion Therapy and Tumor Progression in a Melanoma Mouse Model
Zhang J, et al.
Journal of Cancer, 10(12), 2822-2835 (2019)
Jingjun Zhang et al.
Journal of Cancer, 10(12), 2822-2835 (2019-07-02)
Background: The transfusion of blood that has been stored for some time was found to be associated with transfusion-related immune modulation (TRIM) responses in cancer patients, which could result in poor clinical outcomes, such as tumor recurrence, metastasis and reduced
Proteomics strategy to identify substrates of LNX, a PDZ domain-containing E3 ubiquitin ligase
Guo Z, et al.
Journal of Proteome Research, 11(10), 4847-4862 (2012)
Antigenic mimicry of ubiquitin by the gut bacterium Bacteroides fragilis: a potential link with autoimmune disease
Stewart L, et al.
Clinical and Experimental Immunology, 194(2), 153-165 (2018)

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