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CP-fusion proteins

Labeling of CP-fusion Proteins as a Tool to Study Cell Surface Proteins... [Pg.470]

Another general approach for the labeling of fusion proteins, which conceptually resembles the labeling of CP-fusion proteins is the biotinylation of so-called acceptor peptides by biotin ligase [31, 58]. The biotinylation of fusion proteins by itself is a valuable modification, as numerous streptavidin-and avidin-based probes and materials are commercially available. However,... [Pg.475]

NTA - nitrilotriacetic acid CP - carrier protein, b Requires expression as N-terminal fusion with ubiquitin or intein. [Pg.462]

We have recently developed a novel labeling strategy for cell surface proteins, which promises to overcome some of the limitations of these approaches [30], Here, the protein of interest is fused to a carrier protein (CP) and the corresponding fusion protein is then specifically labeled with CoA derivatives through a posttranslational modification catalyzed by a PPT. [Pg.471]

Zucchini yellow mosaic virus Fusion with CP with protease cleavage anti-HIV proteins 37... [Pg.79]

Other biomolecules that are of interest in p.CP are lipids and lipid bilayers. Supported lipid bilayers are very fragile assemblies that are formed by lipids that are organized into two opposing leaflets on hydrophilic surfaces, such as glass or mica substrates. These structures can be also patterned on solid substrates but the p.CP technique differs slightly from the ones that were applied for proteins or DNA. First, the bilayer has to be formed on the oxidized PDMS stamp from the buffer solution by lipid vesicle fusion. Second, printing has to be carried out in water, otherwise the bilayer will lose its structure.99 This method allows efficient and reliable transfer of membrane patches to glass surfaces. [Pg.450]

Cp is a soluble protein, secreted by mammalian cells into the plasma or interstitial space. However, in some cells (neuronal, visual), alternative splicing of the nascent Cp transcript produces an mRNA that is translated into a Cp protein with a carboxyl-terminal extension that is substrate for the addition of a glycosylphosphatidylinositol (GPI) tag. This tag leads to the insertion of this Cp form into the timer surface of the vesicular membrane that encloses this Cp processing pathway. Upon fusion of this vesicle with the plasma membrane, the Cp becomes tethered to the outer... [Pg.1005]

Williams BJ, Smith JS, Fu KM, Hamilton DK, Polly DW, Jr., Ames CP, et al. Does bone morphogenetic protein increase the incidence of perioperative complications in spinal fusion A comparison of 55,862 cases of spinal fusion with and without bone morphogenetic protein. Spine. 2011 36 1685-91. [Pg.77]


See other pages where CP-fusion proteins is mentioned: [Pg.82]    [Pg.472]    [Pg.475]    [Pg.475]    [Pg.476]    [Pg.82]    [Pg.472]    [Pg.475]    [Pg.475]    [Pg.476]    [Pg.165]    [Pg.72]    [Pg.78]    [Pg.90]    [Pg.449]    [Pg.233]    [Pg.576]    [Pg.472]    [Pg.473]    [Pg.473]    [Pg.203]    [Pg.389]    [Pg.282]    [Pg.267]    [Pg.28]    [Pg.1003]    [Pg.1002]    [Pg.185]    [Pg.568]    [Pg.185]   


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