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U6253

Sigma-Aldrich

Ubiquitin from bovine erythrocytes

BioUltra, ≥98% (SDS-PAGE), essentially salt-free, lyophilized powder

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Synonym(s):
ATP-dependent proteolytic factor, Ub
CAS Number:
MDL number:
NACRES:
NA.32

biological source

bovine erythrocytes

Quality Level

product line

BioUltra

assay

≥98% (SDS-PAGE)

form

essentially salt-free, lyophilized powder

storage condition

(Tightly closed. Dry)

technique(s)

western blot: suitable

impurities

salt, essentially free

solubility

water: 1 mg/mL, clear, colorless

UniProt accession no.

storage temp.

2-8°C

Gene Information

bovine ... LOC(101902760)

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This Item
C6905L4765S1135
Ubiquitin from bovine erythrocytes BioUltra, ≥98% (SDS-PAGE), essentially salt-free, lyophilized powder

U6253

Ubiquitin from bovine erythrocytes

β-Casein from bovine milk BioUltra, ≥98% (PAGE)

C6905

β-Casein from bovine milk

Lactoferrin from bovine colostrum ≥85% (SDS-PAGE)

L4765

Lactoferrin from bovine colostrum

Stroma from bovine erythrocytes source of stromal-bound enzymes

S1135

Stroma from bovine erythrocytes

technique(s)

western blot: suitable

technique(s)

activity assay: suitable

technique(s)

electrophoresis: suitable, ion chromatography: suitable

technique(s)

-

biological source

bovine erythrocytes

biological source

bovine milk

biological source

bovine colostrum

biological source

bovine erythrocytes

form

essentially salt-free, lyophilized powder

form

essentially salt-free, lyophilized powder

form

powder

form

solid

storage condition

(Tightly closed. Dry)

storage condition

-

storage condition

-

storage condition

-

Gene Information

bovine ... LOC(101902760)

Gene Information

bovine ... CSN2(281099), CSN3(281728)

Gene Information

cow ... LTF(280846)

Gene Information

-

General description

Research area: Cancer

Ubiquitin is a highly conserved regulatory protein. It is found in all eukaryotic cells and is virtually identical across all forms of life including yeast, humans, and plants. ubiquitin structure contains seven Lys residues and an N-terminus, all of which are target sites for ubiquitination.

Application

Ubiquitin from bovine erythrocytes has been used to study the role of exogenous ubiquitin in chronic β-adrenergic receptor (β-AR)-stimulated myocardial remodeling. It has also been used to test the inhibitor of nuclear factor kappa-B kinase subunit beta (IKKβ) ubiquitylation.

Ubiquitin from bovine erythrocytes can be used for in vitro ubiquitinylation assay. The product can also be used as a marker in western blotting.

Biochem/physiol Actions

Ubiquitination is a post-translational modification process where ubiquitin-protein is attached to a substrate protein. Ubiquitination plays a vital role in the regulation of cellular signaling in various biological processes such as apoptosis, protein processing, immune response, and DNA repair. Ubiquitination mediates protein degradation via the ubiquitin-proteasome pathway. Ubiquitination is implicated in various cellular signaling pathways. Polyubiquitination modulates the signal activation of NF-κ-B inhibitor alpha (IkB-α) in the inflammatory signaling pathway. Elevated levels of ubiquitin have been observed in various diseases such as parasitic and allergic diseases, alcoholic liver disease, type 2 diabetes, β2-microglobulin amyloidosis, and chronic hemodialysis.

Preparation Note

Ubiquitin from bovine erythrocytes can dissolved in water at 1 mg/ml to yield a clear, 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)


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American journal of physiology. Heart and circulatory physiology, 303(12), H1459-H1468 (2012-10-09)
β-Adrenergic receptor (β-AR) stimulation increases extracellular ubiquitin (UB) levels, and extracellular UB inhibits β-AR-stimulated apoptosis in adult cardiac myocytes. This study investigates the role of exogenous UB in chronic β-AR-stimulated myocardial remodeling. l-Isoproterenol (ISO; 400 μg·kg(-1)·h(-1)) was infused in mice
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Field asymmetric waveform ion mobility spectrometry (FAIMS) has emerged as an analytical tool of broad utility, especially in conjunction with mass spectrometry. Of particular promise is the use of FAIMS and 2-D ion mobility methods that combine FAIMS with conventional

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