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963results about "Fusion with spectroscopic/fluorescent detection" patented technology

Small molecule-dependent inteins and uses thereof

ActiveUS20140065711A1Low splicing efficiencySlow splicingHydrolasesFusion with post-translational modification motifInteinNatural state
Elucidating the function of proteins in mammalian cells is particularly challenging due to the inherent complexity of these systems. Methods to study protein function in living cells ideally perturb the activity of only the protein of interest but otherwise maintain the natural state of the host cell or organism. Ligand-dependent inteins offer single-protein specificity and other desirable features as an approach to control protein function in cells post-translationally. Some aspects of this invention provide second-generation ligand-dependent inteins that splice to substantially higher yields and with faster kinetics in the presence of the cell-permeable small molecule 4-HT, especially at 37° C., while exhibiting comparable or improved low levels of background splicing in the absence of 4-HT, as compared to the parental inteins. These improvements were observed in four protein contexts tested in mammalian cells at 37° C., as well as in yeast cells assayed at 30° C. or 37° C. The newly evolved inteins described herein are therefore promising tools as conditional modulators of protein structure and function in yeast and mammalian cells.
Owner:PRESIDENT & FELLOWS OF HARVARD COLLEGE

Emission ratiometric indicators of phosphorylation by C-kinase

InactiveUS20050026234A1Facilitate its translocationPeptide/protein ingredientsAntibody mimetics/scaffoldsNucleotideFluorophore
A chimeric phosphorylation indicator (CPI) as provided herein can contain a donor molecule, a phosphorylatable domain, a phosphoaminoacid binding domain (PAABD), and an acceptor molecule. Where the phosphorylatable domain is phosphorylatable by protein kinase C (PKC), the CPI is a c-kinase activity reporter (CKAR). Donor and acceptor molecules may be, independently, fluorescent proteins such as non-oligomerizing fluorescent proteins. A CPI can contain a phosphorylatable polypeptide and a fluorescent protein; the phosphorylatable polypeptide may be contained within the sequence of the fluorescent protein, or the fluorescent protein may be contained within the sequence of the phosphorylatable polypeptide. The spatiotemporal properties of the PKC signal pathway may be tested with CKAR, calcium-sensing fluorophores and FRET-based translocation assays. Polynucleotides encoding such CPIs, and kits containing the indicators and / or the polynucleotides, are provided. A method of using the chimeric phosphorylation indicators to detect a kinase or phosphatase in a sample is provided.
Owner:RGT UNIV OF CALIFORNIA +1

Cell Penetrating Peptide, Conjugate Comprising Same, and Composition Comprising Conjugate

The present invention relates to a conjugate of cell penetrating peptide and an active ingredient; and its use. Specifically, a conjugate including a cell penetrating peptide which is a peptide comprising any one amino acid sequence of SEQ ID NO: 1 to SEQ ID NO: 6, a fragment of any one sequence of SEQ ID NO: 1 to SEQ ID NO: 6, or a peptide having above 80% homology with the above-mentioned sequence; and a composition comprising the same are disclosed.
Owner:GEMVAX & KAEL

Genetically encoded fluorescent reporters of kinase, methyltransferase, and acetyl-transferase activities

The invention provides fusion protein reporter molecules that can be used to monitor protein modifications (e.g., histone modifications) in living cells, and methods of using the fusion reporter molecules for diagnosing protein-modification-associated disorders (e.g. histone-modification-associated disorders). The invention also provides methods of using the fusion protein reporters to identify candidate pharmaceutical agents that effect protein modification in cells and tissues, thus permitting identification of candidate pharmaceutical agents for treatment of protein-modification-associated disorders.
Owner:MASSACHUSETTS INST OF TECH
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