Ubiquitin, a small protein consisting of 76aa, has been found in all eukaryotic cells studied. It is one of the most conserved proteins known. Two classes of ubiquitin genes are recognized. Class I is a polyubiquitin gene encoding a polyprotein of tandemly repeated ubiquitins. The class II genes are fusion products between a single ubiquitin gene and 1 of 2 other possible sequences, either 52 or 76 to 80 predominantly basic amino acids. Ubiquitin is required for ATP-dependent, nonlysosomal intracellular protein degradation, which eliminates most intracellular defective problems as well as normal proteins with a rapid turnover. Degradation involves covalent binding of ubiquitin to the protein to be degraded, through isopeptide bonds from the C-terminal glycine residue to the epsilon-amino groups of lysyl side chains. Presumably, the function of ubiquitin is to label the protein for disposal by intracellular proteases. The most abundant ubiquitin- protein conjugate, however, is ubiquitin-H2A, in which ubiquitin is bound to lys119 in histone H2A; this conjugate is not degraded. Since such ubiquitinated histones are present primarily in actively transcribed chromosomal regions, ubiquitin may play a role in regulation of gene expression.
Source:Recombinant protein corresponding to human Ubiquitin, expressed in E. coli.
Applications:Suitable for use in ELISA, Western Blot and can be used for metal chelate affinity chromatography of ubiquinated molecules. It can also serve as a Positive Control for his-tagged antibodies. Other applications not tested.
Recommended Dilution:ELISA: can be used to coat plates at 1ug/ml and detect with antibodiesWestern Blot: 50-200ng/lane Optimal dilutions to be determined by the researcher.
Storage and Stability:May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
