H-DDDDK-OH

Ref. 3D-PP43889

Información del producto

• Nombre: H-DDDDK-OH
• Sinónimos: NH2-Asp-Asp-Asp-Asp-Lys-OH

Descripción

Peptide H-DDDDK-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-DDDDK-OH include the following: Fusion expression and purification of four disulfide-rich peptides reveals enterokinase secondary cleavage sites in animal toxins Z Chen, S Han, Z Cao, Y Wu, R Zhuo, W Li - Peptides, 2013 - Elsevierhttps://www.sciencedirect.com/science/article/pii/S0196978112004780 Substrate specificities of porcine and bovine enteropeptidases toward the peptide Val-(Asp) 4-Lys-Ile-Val-Gly and its analogs YT Kim, W Nishii, M Matsushima, H Inoue - Bioscience , 2008 - jstage.jst.go.jphttps://www.jstage.jst.go.jp/article/bbb/72/3/72_70732/_article/-char/ja/ Recombinant active peptides and their therapeutic functions YS Ajingi , N Rukying, A Aroonsri - Current Pharmaceutical , 2022 - ingentaconnect.comhttps://www.ingentaconnect.com/content/ben/cpb/2022/00000023/00000005/art00005 Engineering SpyCatcher Variants with Proteolytic Sites for Less-Trace Ligation XJ Zhang, XL Wu , D Liu, XD Da - Chinese Journal of , 2019 - Wiley Online Libraryhttps://onlinelibrary.wiley.com/doi/abs/10.1002/cjoc.201800475 New Substrates for Enteropeptidase: I. Biologically Active Hepta-, Octa-, and Nonapeptides VV Likhareva, BV Vas' kovskii, NE Shepel' - Russian Journal of , 2003 - Springerhttps://link.springer.com/article/10.1023/A:1023200230022 Synthetic model and bioactive peptides as potential substrates for enteropeptidase VV Likhareva, AG Mikhailova, BV Vaskovsky - Letters in Peptide , 2002 - Springerhttps://link.springer.com/article/10.1023/A:1024146528313 Dissecting structural basis of the unique substrate selectivity of human enteropeptidase catalytic subunit VG Ostapchenko , ME Gasparian - Journal of , 2012 - Taylor & Francishttps://www.tandfonline.com/doi/abs/10.1080/07391102.2012.674249 Enhanced protease cleavage efficiency on the glucagon-fused interleukin-2 by the addition of synthetic oligopeptides SW Kim, JB Kim, WS Lee, WH Jung, JM Ryu - Protein expression and , 2007 - Elsevierhttps://www.sciencedirect.com/science/article/pii/S1046592807000976 Enzymatic Release of a Surface-Adsorbed RGD Therapeutic from a Cleavable Peptide Anchor SR Meyers , DJ Kenan, MW Grinstaff - : Chemistry Enabling Drug , 2008 - academia.eduhttps://www.academia.edu/download/28028790/grinstaff_-_chemmedchem_(2008).pdf Enhancing the specificity of the enterokinase cleavage reaction to promote efficient cleavage of a fusion tag SH Shahravan , X Qu , IS Chan, JA Shin - Protein expression and purification, 2008 - Elsevierhttps://www.sciencedirect.com/science/article/pii/S1046592808000600 Development of peptides targeting receptor binding site of the envelope glycoprotein to contain the West Nile virus infection P Mertinkova, E Mochnačova, K Bhide, A Kulkarni - Scientific Reports, 2021 - nature.comhttps://www.nature.com/articles/s41598-021-99696-w An SRLLR motif downstream of the scissile bond enhances enterokinase cleavage efficiency OW Liew, PCJ Chong, YZ Lim, CX Ang, YCA Lau - Biochimie, 2007 - Elsevierhttps://www.sciencedirect.com/science/article/pii/S0300908406002392 Preparation of recombinant thioredoxin fused N-terminal proCNP: analysis of enterokinase cleavage products reveals new enterokinase cleavage sites OW Liew, JPC Chong, TG Yandle - Protein expression and , 2005 - Elsevierhttps://www.sciencedirect.com/science/article/pii/S1046592805000847 PSA-selective activation of cytotoxic human serine proteases within the tumor microenvironment as a therapeutic strategy to target prostate cancer OC Rogers, L Anthony, DM Rosen, WN Brennen - Oncotarget, 2018 - ncbi.nlm.nih.govhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5976476/ Substrates of the prostate-specific serine protease prostase/KLK4 defined by positional-scanning peptide libraries M Matsumura, AS Bhatt , D Andress, N Clegg - The , 2005 - Wiley Online Libraryhttps://onlinelibrary.wiley.com/doi/abs/10.1002/pros.20101 Negatively Charged Peptide-Assistant Gold Nanoparticles for Mitochondria Targeting and High-Fidelity Intracellular Bioimaging Enterokinase Levels L Huang, B Zhou, C YU, Q Shen, Z Huang - Available at SSRN - papers.ssrn.comhttps://papers.ssrn.com/sol3/papers.cfm?abstract_id=4161821 Protease specificity determination by using cellular libraries of peptide substrates (CLiPS) KT Boulware, PS Daugherty - Proceedings of the National , 2006 - National Acad Scienceshttps://www.pnas.org/doi/abs/10.1073/pnas.0511108103 Cellular libraries of peptide substrates (CLiPS): a high-throughput method for proteolytic enzyme characterization KT Boulware - 2007 - search.proquest.comhttps://search.proquest.com/openview/b0f304ef3b5a12c97ffeddff5d8d8cfb/1?pq-origsite=gscholar&cbl=18750 New strategy for specific activation of recombinant microbial pro-transglutaminase by introducing an enterokinase cleavage site K Wang, B Wang, HL Yang , L Pan - Biotechnology letters, 2013 - Springerhttps://link.springer.com/article/10.1007/s10529-012-1090-5 Identification of new tag sequences with differential and selective recognition properties for the anti-FLAG monoclonal antibodies M1, M2 and M5 JW Slootstra, D Kuperus, A Pluckthun , RH Meloen - Molecular diversity, 1997 - Springerhttps://link.springer.com/article/10.1007/BF01682203 Investigating Peptide Conjugation for the Selective Activation of Metal Complexes in Tumours J Norman - 2013 - ses.library.usyd.edu.auhttps://ses.library.usyd.edu.au/handle/2123/9506 Enzymatic cleavage of branched peptides for targeting mitochondria H He , J Wang, H Wang , N Zhou , D Yang - Journal of the , 2018 - ACS Publicationshttps://pubs.acs.org/doi/abs/10.1021/jacs.7b11582 Branched peptides for enzymatic supramolecular hydrogelation H He , H Wang , N Zhou , D Yang, B Xu - Chemical communications, 2018 - pubs.rsc.orghttps://pubs.rsc.org/en/content/articlehtml/2018/cc/c7cc08421h Three-Dimensional Structure of the Antimicrobial Peptide Cecropin P1 in Dodecylphosphocholine Micelles and the Role of the C-Terminal Residues H Gu, T Kato, H Kumeta, Y Kumaki, T Tsukamoto - ACS , 2022 - ACS Publicationshttps://pubs.acs.org/doi/abs/10.1021/acsomega.2c02778 AdDLP, a bacterial defensin-like peptide, exhibits anti-Plasmodium activity B Gao, M del Carmen Rodriguez - Biochemical and , 2009 - Elsevierhttps://www.sciencedirect.com/science/article/pii/S0006291X09013862 Study of secondary specificity of enteropeptidase in comparison with trypsin AG Mikhailova, VV Likhareva, BV Vaskovsky - Biochemistry , 2004 - Springerhttps://link.springer.com/article/10.1023/B:BIRY.0000040224.47278.3b

• Marca: Biosynth