|Target/Specificity||The synthetic peptide sequence is selected from aa 1~16 of OXYTR UEV|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
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Provided below are standard protocols that you may find useful for product applications.
Ubiquitin is a 76 amino acid highly conserved eukaryotic polypeptide that selectively marks cellular proteins for proteolytic degradation by the 26S proteasome. The process of target selection, covalent attachment and shuttle to the 26S proteasome is a vital means of regulating the concentrations of key regulatory proteins in the cell by limiting their lifespans. Polyubiquitination is a common feature of this modification. Serial steps for modification include the activation of ubiquitin, an ATP-dependent formation of a thioester bond between ubiquitin and the enzyme E1, transfer by transacylation of ubiquitin from E1 to the ubiquitin conjugating enzyme E2, and covalent linkage to the target protein directly by E2 or via E3 ligase enzyme. Deubiquitination enzymes also exist to reverse the marking of protein substrates. Posttranslational tagging by Ub is involved in a multitude of cellular processes, including the cell cycle, cell growth and differentiation, embryogenesis, apoptosis, signal transduction, DNA repair, regulation of transcription and DNA replication, transmembrane transport, stress responses, the immune response, and nervous system functions.
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