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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:
60267-61-0
Numero MDL:
MFCD02100852
Codice UNSPSC:
41106500
NACRES:
NA.32
Prezzi e disponibilità al momento non sono disponibili

Origine biologica

human

Livello qualitativo

200

Ricombinante

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

Saggio

≥95% (GE)

Stato

lyophilized powder

PM

10.7 kDa

tecniche

ligand binding assay: suitable

Solubilità

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

Compatibilità

suitable for molecular biology

N° accesso UniProt

P0CG47
P0CG48

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Questo articolo
U5382U9382SRP8047
Ubiquitin human recombinant, expressed in E. coli (N-terminal histidine tagged)

U5507

Ubiquitin human

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

U5382

Ubiquitin human

Ubiquitin-Carrier Protein H10 human ≥95% (SDS-PAGE), recombinant, expressed in E. coli (histidine-tagged), buffered aqueous glycerol solution

U9382

Ubiquitin-Carrier Protein H10 human

Omentin human recombinant, expressed in CHO cells, FLAG® tagged, >95% (SDS-PAGE)

SRP8047

Omentin human

biological source

human

biological source

human

biological source

human

biological source

human

technique(s)

ligand binding assay: suitable

technique(s)

mass spectrometry (MS): suitable

technique(s)

ligand binding assay: suitable

technique(s)

ligand binding assay: suitable

recombinant

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

recombinant

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

recombinant

expressed in E. coli (histidine-tagged)

recombinant

expressed in CHO cells

assay

≥95% (GE)

assay

≥95% (SDS-PAGE)

assay

≥95% (SDS-PAGE)

assay

>95% (SDS-PAGE)

suitability

suitable for molecular biology

suitability

-

suitability

-

suitability

-

mol wt

10.7 kDa

mol wt

10 kDa

mol wt

~20 kDa

mol wt

~38 kDa

Descrizione generale

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.[1]
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.[2]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.

Applicazioni

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.[3]
Ubiquitin human has been used:
  • as a substrate in in vitro ubiquitination assays[4]
  • as substrate in ADP-ribosylation and ubiquitylation assays[5]
  • 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[6]

Azioni biochim/fisiol

Ubiquitin is a small regulatory protein present in eukaryote tissues. Exogenous ubiquitin can stimulate apoptosis in numerous cell lines.[7] E7 protein of human papilloma virus-16 stimulates Retinoblastoma Protein degradation via Ubiquitin-Proteasome Pathway.[8]
Ubiquitin plays a key role in normal eukaryotic cell function. It participates in the development and function of the immune system.[9] This immunophilin is also known to participate in immune homeostasis. The ubiquitin peptide fragment (U50-59) is capable of blocking cellular and humoral immunity.[6]
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.[10]

Nota sulla preparazione

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.

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Dispositivi di protezione individuale

Eyeshields, Gloves, type N95 (US)

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    Certificati d'analisi (COA)

    Lot/Batch Number
    079M4104V
    11190121
    108M4174V
    11180609
    048M4030V

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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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