{"product_id":"new-product-577705","title":"COP1(Phospho Ser387) Polyclonal Antibody","description":"\u003cp\u003eThe RING finger domain, in addition to its role in ubiquitination, functions as a structural scaffold to bring two clusters of positive-charged residues within spatial proximity to mimic a bipartite nuclear localization signal (NLS).,E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Involved in JUN ubiquitination and degradation. Directly involved in p53 (TP53) ubiquitination and degradation, thereby abolishing p53-dependent transcription and apoptosis. Ubiquitinates p53 independently of MDM2 or RCHY1. Probably mediates E3 ubiquitin ligase activity by functioning as the essential RING domain subunit of larger E3 complexes. In contrast, it does not constitute the catalytic RING subunit in the DCX DET1-COP1 complex that negatively regulates JUN, the ubiquitin ligase activity being mediated by RBX1.,induction:By p53\/TP53.,pathway:Protein modification; protein ubiquitination.,Belongs to the COP1 family.,Contains 1 RING-type zinc finger.,Contains 7 WD repeats.,subcellular location:In the nucleus, it forms nuclear speckles.,subunit:Homodimer. Homodimerization is mediated by the coiled coil domain. Component of the DCX DET1-COP1 ubiquitin ligase complex at least composed of RBX1, DET1, DDB1, CUL4A and COP1. Isoform 2 does not interact with CUL4A but still binds to RBX1, suggesting that the interaction may be mediated by another culllin protein. Isoform 1 and isoform 2 interact with CUL5 but not with CUL1, CUL2 not CUL3. Interacts with bZIP transcription factors JUN, JUNB and JUND but not with FOS, ATF2 nor XBP1. Interacts with p53 (TP53).,tissue specificity:Ubiquitously expressed at low level. Expressed at higher level in testis, placenta, skeletal muscle and heart.,\u003c\/p\u003e\n\u003cp\u003eThe COP1(PHOSPHO SER387) Polyclonal Antibody is a highly specific and reliable tool for the detection and analysis of COP1 protein phosphorylated at serine 387. This antibody has been meticulously developed and validated to ensure optimal performance in various applications, including Western blotting, immunoprecipitation, and immunofluorescence.\u003cbr\u003e\u003cbr\u003eWith its exceptional sensitivity and specificity, this polyclonal antibody enables accurate and precise quantification of COP1(PHOSPHO SER387) protein levels in various biological samples. It exhibits minimal cross-reactivity with non-phosphorylated COP1 protein, ensuring reliable and accurate results.\u003cbr\u003e\u003cbr\u003eThe COP1(PHOSPHO SER387) Polyclonal Antibody is produced using state-of-the-art techniques and undergoes rigorous quality control measures to ensure batch-to-batch consistency and reproducibility. It is supplied as a ready-to-use solution, eliminating the need for time-consuming and error-prone antibody preparation.\u003cbr\u003e\u003cbr\u003eThis antibody is suitable for use in both research and clinical settings, providing valuable insights into the role of COP1(PHOSPHO SER387) in cellular processes and disease mechanisms. Its versatility and reliability make it an indispensable tool for scientists and researchers working in the fields of molecular biology, biochemistry, and cell biology.\u003cbr\u003e\u003cbr\u003eOrder the COP1(PHOSPHO SER387) Polyclonal Antibody today and unlock the potential of your research by gaining a deeper understanding of COP1 protein phosphorylation at serine 387.\u003c\/p\u003e","brand":"BT Lab","offers":[{"title":"100ul \/ Rabbit \/ Primary antibody","offer_id":47545795150104,"sku":"BT-AP07999","price":275.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0590\/5652\/1400\/products\/BT_Lab_08bcf16d-b406-4706-b87d-5dd1ddae33b5.png?v=1705675466","url":"https:\/\/danabiosci.com\/products\/new-product-577705","provider":"Dana Bioscience","version":"1.0","type":"link"}