Well-Coated™ Neutravidin™ (4 Citations)
Well-Coated™ Neutravidin™ plates are designed to specifically bind biotinylated molecules, including biotin tagged antibodies, with minimal non-specific binding. This is particular advantageous for antibodies known to denature upon direct binding to polystyrene plates.
Biotin exhibits an extraordinary binding affinity for avidin (Ka=1015M-1) and Neutravidin™ (Ka=1015 M-1). Biotin and avidin interaction is rapid and once the bond is established it can survive up to 3M guanidine-hydrochloride and extremes of pH. Biotin-avidin bonds can only be reversed by denaturing the avidin protein molecule with 8M guanidine-hydrochloride at pH1.5 or by autoclaving. Neutravidin™ is in many respects is similar to avidin except that it has no carbohydrate side chains to eliminate lectin binding; is of near neutral pI (6.3) to reduce non-specific adsorption; lacks the RYD sequence eliminating interaction with RGD domain of adhesion receptors. The binding of Neutravidin™ is similar to that of avidin and streptavidin with less non-specific binding.
Well-Coated™ Neutravidin™ plates are suitable for direct, indirect, competitive and sandwich assays. The wells are coated to a 100µl depth and are supplied pre-blocked in our proprietary Superior™ Blocking Buffer. The clear, white and black plates are offered for colorimetric, chemiluminescence and fluorescent detection systems, respectively.
Features
- High binding capacity for biotin
- Low non-specific binding
- Ideal for peptides, antibodies and small hydrophilic molecules
- Reduced non-specific binding as plates are pre-blocked with Superior™ Blocking Buffer
Protocol | |
786-743 | |
786-766 | |
786-767 |
Material Safety Data Sheet | |
786-743 | |
786-766 | |
786-767 |
Technical Literature | |
Assay Development | A handbook for selection of products for assay development, including coated plates, blocking agents, antibodies, enzymes and antibody labeling tools. |
Bioassays Handbook |
- Ouellette, S. et al (2016) A Cell-Based Assay for Measuring Endogenous BcrAbl Kinase Activity and Inhibitor Resistance. PLOS doi.org/10.1371/journal.pone.0161748
- Kim, T et al (2015) Anal Biochem. 480:21
- Negmeldin, A.T. and Pflum, M.H J Biomol Screen. doi: 10.1177/1087057115598118
- Lamont, E.A. et al (2011) Analyst. 136:3884