Ubiquitin (from bovine erythrocytes)
Ubiquitin (from bovine erythrocytes) structure
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Common Name | Ubiquitin (from bovine erythrocytes) | ||
|---|---|---|---|---|
| CAS Number | 79586-22-4 | Molecular Weight | N/A | |
| Density | N/A | Boiling Point | N/A | |
| Molecular Formula | N/A | Melting Point | N/A | |
| MSDS | USA | Flash Point | N/A | |
Use of Ubiquitin (from bovine erythrocytes)Ubiquitin is a small regulatory protein present in eukaryote tissues. |
| Name | UBIQUITIN |
|---|
| Appearance of Characters | essentially salt-free, vacuum-dried powder |
|---|---|
| Storage condition | 2-8°C |
| Water Solubility | Soluble in water at 1mg/ml |
| Personal Protective Equipment | Eyeshields;Gloves;type N95 (US);type P1 (EN143) respirator filter |
|---|---|
| RIDADR | NONH for all modes of transport |
| WGK Germany | 3 |
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Export-deficient monoubiquitinated PEX5 triggers peroxisome removal in SV40 large T antigen-transformed mouse embryonic fibroblasts.
Autophagy 11 , 1326-40, (2015) Peroxisomes are ubiquitous cell organelles essential for human health. To maintain a healthy cellular environment, dysfunctional and superfluous peroxisomes need to be selectively removed. Although em... |
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Insights into Ubiquitination from the Unique Clamp-like Binding of the RING E3 AO7 to the E2 UbcH5B.
J. Biol. Chem. 290 , 30225-39, (2015) RING proteins constitute the largest class of E3 ubiquitin ligases. Unlike most RINGs, AO7 (RNF25) binds the E2 ubiquitin-conjugating enzyme, UbcH5B (UBE2D2), with strikingly high affinity. We have de... |
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Stimulation of ATP-dependent proteolysis requires ubiquitin with the COOH-terminal sequence Arg-Gly-Gly.
J. Biol. Chem. 256 , 9235-9241, (1981) It was previously shown that ubiquitin is very similar to the polypeptide cofactor of the ATP-dependent protein degradation system from rabbit reticulocytes (Wilkinson, K. D., Urban, M. K., and Haas, ... |