biotinylation การใช้

• Luciferase can act as an ATP sensor protein through biotinylation.
• Biotinylation at carboxyl groups occur at pH 4.5 5.5.
• Biotinylation will immobilize luciferase on the cell-surface by binding to a streptavidin-biotin complex.
• One idea is to attach the exonuclease to the nanopore, perhaps through biotinylation to the beta barrel hemolsyin.
• The advent of proximity biotinylation by birA * has facilitated the first proteomics-based studies of the cadherin adhesome.
• Lysine guanidination followed by biotinylation of N-termini uses a chemical to block lysine residues and tag free N-termini.
• Subtiligase biotinylation of N-termini uses enzymatic labeling of N-terminal peptides, but does not use lysine blocking chemicals.
• Biotinylation of DNA and RNA with photoactivatable biotin is easier and less expensive than enzymatic methods since the DNA and RNA does not degrade.
• For Chem-seq to be feasible, the small molecule under study must be amenable to biotinylation without disruption of its natural binding properties.
• Acetylation of amines followed by tryptic digestion and biotinylation of free N-terminal peptides uses chemical ( acetylation ) to label free lysines and N-termini.
• Protein tags may allow specific enzymatic modification ( such as biotinylation by biotin ligase ) or chemical modification ( such as reaction with FlAsH-EDT2 for fluorescence imaging ).
• Photoactivatable biotinylation reagents can also be used to activate biotinylation at specific times in an experiment or during certain reaction conditions, by simply exposing the reaction to UV light at the specific time or condition.
• Photoactivatable biotinylation reagents can also be used to activate biotinylation at specific times in an experiment or during certain reaction conditions, by simply exposing the reaction to UV light at the specific time or condition.
• The attachment of biotin to various chemical sites, biotinylation, is used as an important laboratory technique to study various processes, including protein localization, histone proteins, but little biotin is found naturally attached to chromatin.
• Exploiting these facts, scientists have bioengineered E . coli to produce soluble MHC molecules with a biotinylation protein domain, meaning a part of the MHC can be replaced by covalently bound biotin ( via BirA enzyme activity ).
• DIB involves an initial biotinylation of all erythrocytes in circulation, followed by a second biotinylation a few days after, at a lower density, that labels the biotin-negative erythrocytes that have entered since the first biotinylation.
• DIB involves an initial biotinylation of all erythrocytes in circulation, followed by a second biotinylation a few days after, at a lower density, that labels the biotin-negative erythrocytes that have entered since the first biotinylation.
• DIB involves an initial biotinylation of all erythrocytes in circulation, followed by a second biotinylation a few days after, at a lower density, that labels the biotin-negative erythrocytes that have entered since the first biotinylation.
• Lysine can be modified through acetylation ( acetyllysine ), methylation ( methyllysine ), ubiquitination, sumoylation, neddylation, biotinylation, pupylation, and carboxylation, which tends to modify the function of the protein of which the modified lysine residue ( s ) are a part.
• Post-translational modification of proteins can include : acetylation, acylation ( myristoylation, palmitoylation ), alkylation, arginylation, ADP-Ribosylation, biotinylation, formylation, geranylgeranylation, glutamylation, glycosylation, glycylation, hydroxylation, isoprenylation, lipoylation, methylation, nitroalkylation, phosphopantetheinylation, phosphorylation, prenylation, selenation, S-nitrosylation, succinylation, sulfation, transglutamination and ubiquitination ( sumoylation, neddylation ).