|Other Names||E3 ubiquitin-protein ligase ARIH1, 632-, H7-AP2, HHARI, Monocyte protein 6, MOP-6, Protein ariadne-1 homolog, ARI-1, UbcH7-binding protein, UbcM4-interacting protein, Ubiquitin-conjugating enzyme E2-binding protein 1, ARIH1, ARI, MOP6, UBCH7BP|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP2100b was selected from the C-term region of human UbcH7-BP . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized 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.|
|Synonyms||ARI, MOP6, UBCH7BP|
|Function||E3 ubiquitin-protein ligase, which catalyzes polyubiquitination of target proteins together with ubiquitin- conjugating enzyme E2 UBE2L3. May play a role in protein translation by mediating polyubiquitination of EIF4E2, leading to its subsequent degradation. Acts as the ligase involved in ISGylation of EIF4E2.|
|Cellular Location||Cytoplasm. Note=Mainly cytoplasmic|
|Tissue Location||Widely expressed.|
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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.
Strausberg, R.L., et al., Proc. Natl. Acad. Sci. U.S.A. 99(26):16899-16903 (2002).Stanchi, F., et al., Yeast 18(1):69-80 (2001).Ardley, H.C., et al., J. Biol. Chem. 276(22):19640-19647 (2001).Aguilera, M., et al., Genetics 155(3):1231-1244 (2000).Moynihan, T.P., et al., J. Biol. Chem. 274(43):30963-30968 (1999).
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