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H-LL^EAAR-OH
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H-LL^EAAR-OH

Ref. 3D-PP41871

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Estimated delivery in United States, on Tuesday 10 Dec 2024

Product Information

Name:
H-LL^EAAR-OH
Description:

Peptide H-LL^EAAR-OH is a Research Peptide with significant interest within the field academic and medical research. This peptide is available for purchase at Cymit Quimica in multiple sizes and with a specification of your choice. Recent citations using H-LL^EAAR-OH include the following: Tankyrase-1 ankyrin repeats form an adaptable binding platform for targets of ADP-ribose modification T Eisemann, M McCauley , MF Langelier, K Gupta - Structure, 2016 - cell.comhttps://www.cell.com/structure/pdf/S0969-2126(16)30225-8.pdf Poly (ADP-ribose) polymerase enzymes and the maintenance of genome integrity T Eisemann, JM Pascal - Cellular and Molecular Life Sciences, 2020 - Springerhttps://link.springer.com/article/10.1007/s00018-019-03366-0 Structural Analysis of Tankyrase-1 Regulation and Binding Partner Interaction T Eisemann - 2017 - search.proquest.comhttps://search.proquest.com/openview/e32928d536eaa944cb1a0884d58eac17/1?pq-origsite=gscholar&cbl=18750 Vertebrate tankyrase domain structure and sterile alpha motif (SAM)-mediated multimerization M De Rycker , RN Venkatesan, C Wei - Biochemical , 2003 - portlandpress.comhttps://portlandpress.com/biochemj/article-abstract/372/1/87/43616 Characterization of tankyrase structure and function: Evidence for a role as a master scaffolding protein M De Rycker - 2005 - search.proquest.comhttps://search.proquest.com/openview/c5026196ce62a2dd9cd5024452c50eb9/1?pq-origsite=gscholar&cbl=18750&diss=y Tankyrase-2 oligomerizes with tankyrase-1 and binds to both TRF1 (telomere-repeat-binding factor 1) and IRAP (insulin-responsive aminopeptidase) JI Sbodio, HF Lodish, NW Chi - Biochemical Journal, 2002 - portlandpress.comhttps://portlandpress.com/biochemj/article-abstract/361/3/451/39822 Development of chemical tool compounds targeting the non-catalytic functions of tankyrase I Black - 2023 - repository.icr.ac.ukhttps://repository.icr.ac.uk/handle/internal/5848

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