Invitrogen™ Ubiquitin Monoclonal Antibody (eBioP4D1 (P4D1)), Biotin, eBioscience™, Invitrogen™

Description

Description: The monoclonal antibody eBioP4D1 (p4D1) recognizes ubiquitin, a small 8Ka protein. Ubiquitin units are linked to proteins via a ubiquitination process, thereby signaling the protein for degradation by the 26S proteosome. The process of ubiquitination plays a role in differentiation, cell cycle progression, apoptosis and disease progression. For example, neuronal inclusions called Lewis bodies from Parkinson patients are rich in ubiquitin. Applications Reported: This eBioP4D1 (P4D1) antibody has been reported for use in immunoblotting (WB). Applications Tested: This eBioP4D1 (P4D1) antibody has been tested by immunoblotting of treated cell lines. This can be used at less than or equal to 0.5 μg/mL. It is recommended that the antibody be carefully titrated for optimal performance in the assay of interest. Filtration: 0.2 μm post-manufacturing filtered.

Ubiquitin, a highly conserved protein that has a major role in targeting cellular proteins for degradation by the 26S proteosome, is synthesized as a precursor protein consisting of either polyubiquitin chains or a single ubiquitin fused to an unrelated protein. This gene encodes a fusion protein consisting of ubiquitin at the N terminus and ribosomal protein S27a at the C terminus. When expressed in yeast, the protein is post-translationally processed, generating free ubiquitin monomer and ribosomal protein S27a. Ribosomal protein S27a is a component of the 40S subunit of the ribosome and belongs to the S27AE family of ribosomal proteins. It contains C4-type zinc finger domains and is located in the cytoplasm. Pseudogenes derived from this gene are present in the genome. As with ribosomal protein S27a, ribosomal protein L40 is also synthesized as a fusion protein with ubiquitin; similarly, ribosomal protein S30 is synthesized as a fusion protein with the ubiquitin-like protein fubi. Multiple alternatively spliced transcript variants that encode the same proteins have been identified.