Ubiquitin human
SIGMA/U5507 - recombinant, expressed in E. coli (N-terminal histidine tagged)
CAS Number: 60267-61-0
MDL Number: MFCD02100852
Product Type: Chemical
SDS-PAGE Ubiquitin human (Cat. No. U5507) was assessed on SDS-PAGE.
The ubiquitin-proteasome system. Ubiquitin is first activated by the ubiquitin-activating enzyme, E1, to a high energy thiol ester intermediate. It is then transferred, still as a high energy intermediate, to a member of the ubiquitin-carrier proteins family of enzymes, E2 (also known as a ubiquitin-conjugating enzyme - UBC). From E2 it can be transferred directly to the substrate, S, that is bound specifically to a member of the ubiquitin ligase family of proteins, E3. This occurs when the E3 belongs to the RING finger family of ligases (A). In the case of an HECT (Homologous tothe E6-AP C-Terminal domain) domain-containing E3 ligase (B), the activated ubiquitin moiety is transferred first to the E3, to generate yet another high-energy thiol ester intermediate, before it is transferred to the E3-bound target substrate. Additional ubiquitin moieties are added successively to
the previously conjugated one in a similar mechanism to generate a poly-ubiquitin chain. The poly-ubiquitinated substrate is bound specifically to the
26S proteasome complex. The substrate is degraded to short peptides, and free and reusable ubiquitin is released via the activity of de-ubiquitinating
enzymes (DUBS)
the previously conjugated one in a similar mechanism to generate a poly-ubiquitin chain. The poly-ubiquitinated substrate is bound specifically to the
26S proteasome complex. The substrate is degraded to short peptides, and free and reusable ubiquitin is released via the activity of de-ubiquitinating
enzymes (DUBS)
| assay | ≥95% (GE) |
| biological source | human |
| form | lyophilized powder |
| mol wt | 10.7 kDa |
| Quality Level | 200  |
| recombinant | expressed in E. coli (N-terminal histidine tagged) |
| storage temp. | −20°C |
| technique(s) | ligand binding assay: suitable |
| UniProt accession no. | P0CG47  |
| P0CG48 |
| Application: | N-Terminal histidine-tagged ubiquitin can replace native ubiquitin in formation of poly-ubiquitin—protein conjugates. The histidine tag enables separation and enrichment of protein conjugates on a Ni(II) column and 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. |
| Application: | 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. |
| Biochem/physiol Actions: | 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. |
| General description: | 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. |
| Packaging: | 1 mg in glass bottle |
| 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. |
| RIDADR | NONH for all modes of transport |
| WGK Germany | WGK 3 |
| Flash Point(F) | Not applicable |
| Flash Point(C) | Not applicable |
| Purity | ≥95% (GE) |
| Storage Temp. | −20°C |
| UNSPSC | 12352200 |