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Frequently
Asked Questions
How many COOH groups are on each
ProteoColor Trilite Nanocluster?
The exact number is not known,
but it is of the order of tens of thousands.
How many biotin binding sites are on each avidin-conjugated
Trilite Nanocluster?
The exact number is not known, but it is probably 4.
What is the size of each Trilite Nanocluster?
The average diameter is 25 nm, with a size distribution of
+/- 15 nm.
What is the Full width at half maximum (FWHM) of the emission
spectra?
28 – 32 nm for each color.
How are the molecular weight (MW) and net charge (pI) of a
protein altered by conjugation to Trilite Nanoclusters?
We do not know the exact effect of conjugating Trilite
Nanoclusters to proteins. The coupling takes place via amino
groups on proteins by formation of an amide bond with the
carboxyl groups on the surface of Trilite Nanoclusters. The
exact number of Trilite Nanoclusters conjugating to each protein
and the number of unused carboxyl groups on the Trilite
Nanoclusters would determine the change in molecular weight and
pI of the protein.
Is there a spacer arm between the surface of the Trilite
Nanoclusters and the carboxyl groups?
No.
What is the quantum efficiency of each Trilite Nanocluster?
Approximately 50%.
How many nanocrystals does each Trilite Nanocluster contain?
Approximately 200.
Does the fluorescence signal self-quench if too many Trilite
Nanoclusters conjugate to a protein/antibody?
No.
Is it possible to separate unconjugated protein from protein
molecules conjugated to Trilite Nanoclusters by centrifugation?
It should be possible. Alternatively, filtration can be
used. We use 25 nm mixed cellulose ester membrane filters to
separate the bulk of the unconjugated avidin from
avidin-conjugated Trilite Nanoclusters.
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