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About This Item
NACRES:
NA.21
UNSPSC Code:
12352200
Product Name
Streptavidin Mutein Matrix, Streptavidin, suitable for purification of biotinylated proteins and other biomolecules.
form
suspension
parameter
4-25 °C optimum reaction temp.
matrix
(immobilised onto crosslinked agarose beads)
shipped in
wet ice
storage temp.
2-8°C
mol wt
60 kDa (approx.)
packaging
pkg of 5 mL
manufacturer/tradename
Roche
Application
- Streptavidin Mutein Matrix: Is highly suitable for purification of biotinylated proteins
- Has been tested for use with in vitro expressed biotinylated proteins, using the RTS AviTag Biotinylation Kits
- Is convenient for purification of chemically biotinylated proteins
- It was also used in single-step affinity chromatography and affinity chromatography.
Features and Benefits
- Mild purification conditions: Low biotin dissociation constant allows elution of biotinylated proteins under gentle conditions.
- Stable: No significant loss of binding capacity upon storage. The low dissociation constant of the streptavidin mutein is obtained by genetic engineering and not by dissociation of avidin- or streptavidin tetramers.
- Economic: High binding capacity and multiple reuse allows economic handling of the matrix.
General description
Contents
Settled resin of 50% suspension Streptavidin Mutein Matrix.
Settled resin of 50% suspension Streptavidin Mutein Matrix.
Streptavidin mutein, immobilized.
The binding of biotin to avidin/streptavidin is the strongest known noncovalent interaction of biological molecules [(Kd 0.6 x 10-15 M (avidin), 4 x 10-14 M (streptavidin)]. Strong binding provides a great advantage for certain applications of the derived biotin-avidin/streptavidin technology, such as surface immobilization, blotting technologies, immunoassays, cross-linking studies, and histochemistry. However, the use of immobilized avidin/streptavidin for the purification of biotinylated proteins is limited. In this instance, the extreme affinity of the binding partners creates a drawback of enabling elution only under very harsh conditions that usually destroy the functionality of the protein of interest.
Recombinant streptavidin technology was used to screen for a mutant streptavidin with reduced binding affinity toward biotin. By substituting three amino acids, a mutein was obtained with a biotin dissociation constant of 1.3 x 10-7 M.
The Streptavidin Mutein Matrix provides this mutein immobilized onto cross-linked agarose beads in a highly stable and regenerable form, which allows purification of biotinylated proteins that results in excellent purity and recovery.
Recombinant streptavidin technology was used to screen for a mutant streptavidin with reduced binding affinity toward biotin. By substituting three amino acids, a mutein was obtained with a biotin dissociation constant of 1.3 x 10-7 M.
The Streptavidin Mutein Matrix provides this mutein immobilized onto cross-linked agarose beads in a highly stable and regenerable form, which allows purification of biotinylated proteins that results in excellent purity and recovery.
Other Notes
For life science research only. Not for use in diagnostic procedures.
Preparation Note
Store at 2 to 8 °C. (Do not freeze!)
Storage Class
12 - Non Combustible Liquids
wgk
WGK 1
flash_point_f
does not flash
flash_point_c
does not flash
Regulatory Information
常规特殊物品
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Nancy G Nossal et al.
The Journal of biological chemistry, 282(2), 1098-1108 (2006-11-16)
Our previous electron microscopy of DNA replicated by the bacteriophage T4 proteins showed a single complex at the fork, thought to contain the leading and lagging strand proteins, as well as the protein-covered single-stranded DNA on the lagging strand folded
Dalia Juzumiene et al.
Nuclear receptor signaling, 3, e001-e001 (2006-04-11)
The full-length human androgen receptor with an N-terminal biotin acceptor peptide tag was overexpressed in Spodoptera frugiperda cells in the presence of 1 microM dihydrotestosterone. Site-specific biotinylation of BAP was achieved in vivo by co-expression of E. coli biotin holoenzyme
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