Description
Biotin hydrazide is a biotinyl derivative used to label surface functional groups, antibodies, lectins, sugars, nucleic acids, or molecules with free carboxylic or keto groups. Biotin hydrazide is used as a probe for determining protein carbonylation, an irreversible posttranslational modification resulting from the actions of reactive oxygen species or lipid oxidation products. The reaction of this probe is direct and does not require catalysts or reducing agents.
Uses
Biotin Hydrazide is a carbohydrate reactive biotinylation reagent used predominately for labeling monoclonal antibodies, unpaired cytosine residues in nucleic acids and glycoproteins.
Uses
aldehyde reactive biotinylation reagent
Uses
(+)-Biotin hydrazide has been used:
- the modification of alginate
- for the labelling of mitochondrial proteins from non-muscle tissues
- as a component of glycoprotein staining solution
- in periodic acid-biotin-hydrazide (PABH) assay for mucins
- for labeling surface functional groups, biologically active molecules such as antibodies, lectins, sugars, nucleic acids or molecules with free carboxylic or keto groups.
- for coupling to glycoproteins through the carbohydrate by hydrazone formation
General Description
Biotin hydrazide is a biotinylation reagent used to biotinylate glycoproteins with their sugar moieties. Biotin hydrazide can be used to prepare biotin-conjugated alginate. It can also be used for covalent attachment to PAAc via carbodi-imide cross linking.
Purification Methods
Wash the hydrazide with H2O, dry it, wash it with MeOH then Et2O, and dry. Recrystallise it from hot H2O (clusters of prisms) [Hofmann et al. J Biol Chem 144 513 1942]. [Beilstein 27 III/IV 7980.]
References
[1] E. DIAMANDIS T K C. The biotin-(strept)avidin system: principles and applications in biotechnology.[J]. Clinical chemistry, 1991, 37 5 1: 625-636. DOI:
10.1093/clinchem/37.5.625[2] ASHRAF G. MADIAN Fred E R. Proteomic Identification of Carbonylated Proteins and Their Oxidation Sites[J]. Journal of Proteome Research, 2010, 9 8: 3766-3780. DOI:
10.1021/pr1002609
