|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||Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed.|
|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.|
|Function||E3 ubiquitin-protein ligase, which catalyzes ubiquitination of target proteins together with ubiquitin-conjugating enzyme E2 UBE2L3 (PubMed:15236971, PubMed:21532592, PubMed:24076655, PubMed:27565346, PubMed:23707686). Acts as an atypical E3 ubiquitin-protein ligase by working together with cullin-RING ubiquitin ligase (CRL) complexes and initiating ubiquitination of CRL substrates: associates with CRL complexes and specifically mediates addition of the first ubiquitin on CRLs targets (PubMed:27565346). The initial ubiquitin is then elongated by CDC34/UBE2R1 and UBE2R2 (PubMed:27565346). E3 ubiquitin-protein ligase activity is activated upon binding to neddylated cullin-RING ubiquitin ligase complexes (PubMed:24076655, PubMed:27565346). Plays a role in protein translation in response to DNA damage by mediating ubiquitination of EIF4E2, the consequences of EIF4E2 ubiquitination are however unclear (PubMed:25624349). According to a report, EIF4E2 ubiquitination leads to promote EIF4E2 cap-binding and protein translation arrest (PubMed:25624349). According to another report EIF4E2 ubiquitination leads to its subsequent degradation (PubMed:14623119). Acts as the ligase involved in ISGylation of EIF4E2 (PubMed:17289916). In vitro, controls the degradation of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex member SUN2 and may therefore have a role in the formation and localization of the LINC complex, and as a consequence, nuclear subcellular localization and nuclear morphology (PubMed:29689197).|
|Cellular Location||Cytoplasm. Nucleus. Nucleus, Cajal body. Note=Mainly cytoplasmic (PubMed:11278816). Present in Lewy body (PubMed:21590270)|
|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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