Ambient

Intended Use
GenScript Streptavidin
MagBeads are ideal for fast and convenient purification of biotinylated
proteins, peptides, antibodies and oligonucleotides, and protein interaction
studies.

Principle
Add the sample containing
biotinylated molecules to the Streptavidin MagBeads and allow the molecules
bind to the MagBeads during a short incubation. Then separate the molecule‐bound beads with a magnetic separation rack. With indirect capture, mix
the biotinylated molecule with the sample to capture the molecule‐target complex before adding the MagBeads.

Description of Material
GenScript Streptavidin MagBeads
are super paramagnetic beads of approximately 45-100
μm in diameter, covalently coated with highly
purified streptavidin. These magnetic beads are composed of magnetite core
encapsulated by agarose. The magnetic beads have streptavidin as its surface
protein which is 53kDa. in size having four binding site per molecule. These
beads have pH stability of 2 to 14 (short term); 3 to 13 (long term). The beads
are supplied as 25% slurry in phosphate buffered saline (PBS), pH 7.4,
containing 20% ethanol.

Storage and Stability
This product is stable
until the expiration date stated on the COA, when stored unopened at 2–8°C. Do NOT freeze the product. Keep
the MagBeads in liquid suspension during storage and all handling steps. Drying
will cause loss of binding capacity and result in reduced performance.
Resuspend the beads well before use. Be careful to avoid bacterial/fungal
contamination.

GenScript Streptavidin Resin is an affinity chromatography medium designed for easy,
one-step purification of biotinylated peptides, antibodies, lectins, etc
from samples. The purified recombinant streptavidin is covalently coupling to 4%
highly cross-linked agarose. The
coupling is optimized to give high binding capacity for biotinylated molecules. The total
binding capacity of Streptavidin Resin is more
than 120 nmol of D-Biotin/ml
settled resin. Table 1 lists the characteristics of Streptavidin Resin.

Streptavidin is a biotin-binding protein found in the culture broth of the bacterium Streptomyces
avidinii. Streptavidin binds 4 moles of biotin per mole of protein with an
extremely high affinity. Streptavidin lacks carbohydrate side chains present on
avidin and has an isoelectric point of 6.5 (vs 10 for avidin) close to
where most useful biological interactions occur. As a result,
streptavidin frequently exhibits much lower non-specific binding than avidin
does.