![]() ![]() C07K14/00- Peptides having more than 20 amino acids Gastrins Somatostatins Melanotropins Derivatives thereof.C12N15/85- Vectors or expression systems specially adapted for eukaryotic hosts for animal cells.C12N15/79- Vectors or expression systems specially adapted for eukaryotic hosts.C12N15/63- Introduction of foreign genetic material using vectors Vectors Use of hosts therefor Regulation of expression.plasmids, or their isolation, preparation or purification Use of hosts therefor C12N15/00- Mutation or genetic engineering DNA or RNA concerning genetic engineering, vectors, e.g.C12N- MICROORGANISMS OR ENZYMES COMPOSITIONS THEREOF PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS MUTATION OR GENETIC ENGINEERING CULTURE MEDIA.C12- BIOCHEMISTRY BEER SPIRITS WINE VINEGAR MICROBIOLOGY ENZYMOLOGY MUTATION OR GENETIC ENGINEERING.Assignors: WEISSMAN, DREW, KARIKO, KATALIN Status Abandoned legal-status Critical Current Links Assignors: UNIVERSITY OF PENNSYLVANIA Assigned to THE TRUSTEES OF THE UNIVERSITY OF PENNSYLVANIA reassignment THE TRUSTEES OF THE UNIVERSITY OF PENNSYLVANIA ASSIGNMENT OF ASSIGNORS INTEREST (SEE DOCUMENT FOR DETAILS). GOVERNMENT CONFIRMATORY LICENSE (SEE DOCUMENT FOR DETAILS). OF HEALTH AND HUMAN SERVICES (DHHS), U.S. GOVERNMENT reassignment NATIONAL INSTITUTES OF HEALTH (NIH), U.S. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.) Filing date Publication date Application filed by University of Pennsylvania Penn filed Critical University of Pennsylvania Penn Priority to US14/776,525 priority Critical patent/US20160032316A1/en Publication of US20160032316A1 publication Critical patent/US20160032316A1/en Assigned to NATIONAL INSTITUTES OF HEALTH (NIH), U.S. ![]() Original Assignee University of Pennsylvania Penn Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.) Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.) Abandoned Application number US14/776,525 Inventor Drew Weissman Katalin Kariko Current Assignee (The listed assignees may be inaccurate. Google Patents Purification and Purity Assessment of RNA Molecules Synthesized with Modified Nucleosidesĭownload PDF Info Publication number US20160032316A1 US20160032316A1 US14/776,525 US201414776525A US2016032316A1 US 20160032316 A1 US20160032316 A1 US 20160032316A1 US 201414776525 A US201414776525 A US 201414776525A US 2016032316 A1 US2016032316 A1 US 2016032316A1 Authority US United States Prior art keywords another embodiment rna purified preparation cell messenger rna Prior art date Legal status (The legal status is an assumption and is not a legal conclusion. Google Patents US20160032316A1 - Purification and Purity Assessment of RNA Molecules Synthesized with Modified Nucleosides Due to glycosylation, the protein migrates to 54-58 kDa based on Tris-Bis PAGE result.US20160032316A1 - Purification and Purity Assessment of RNA Molecules Synthesized with Modified Nucleosides Mature human ROR2 contains a 369 amino acid (aa) extracellular domain (ECD) and a 518 aa cytoplasmic tail containing an tyrosine kinase domain.Ĥ4.2 kDa. (Receptor Tyrosine Kinase-Like Orphan Receptor 2 (ROR2))īDB Protein, BDB1 Protein, NTRKR2 Protein, Ntrkr2 Protein, mRor2 Protein, ROR2 Protein, bdb Protein, bdb1 Protein, Xror2 Protein, ntrkr2 Protein, MGC97773 Protein, LOC100219935 Protein, ror2 Protein, xror2 Protein, receptor tyrosine kinase like orphan receptor 2 Protein, receptor tyrosine kinase-like orphan receptor 2 Protein, receptor tyrosine kinase like orphan receptor 2 L homeolog Protein, ROR2 Protein, Ror2 Protein, ror2 Protein, ror2.L ProteinīDB, BDB1, NTRKR2, ROR2,ROR2 (Receptor Tyrosine Kinase-like Orphan Receptor 2) is a member of the ROR family of receptor tyrosine kinases and is important for skeletal development, including bone and cartilage formation, as well as for the development of the central nervous system. Use a manual defrost freezer and avoid repeated freeze-thaw cycles. Reconstituted protein stable at -80☌ for 12 months, 4☌ for 1 week. Normally 5 % trehalose is added as protectant before lyophilization. Lyophilized from 0.22μm filtered solution in PBS ( pH 7.4). Dissolve the lyophilized protein in distilled water. Reconstituting to a concentration more than 100 μg/mL is recommended (usually we use 1 mg/mL solution for lyophilization). Custom Recombinant Antibody (rAbs) ServicesĬentrifuge tubes before opening.Annexin V-FITC Apoptosis Detection Kits.
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