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03708152001

Roche

Streptavidin Mutein Matrix

suspension, pkg of 5 mL

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.21

form

suspension

packaging

pkg of 5 mL

manufacturer/tradename

Roche

parameter

4-25 °C optimum reaction temp.

shipped in

wet ice

General description

Contents
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.

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.

Storage and Stability

Store at 2 to 8 °C. (Do not freeze!)

Other Notes

For life science research only. Not for use in diagnostic procedures.

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point(F)

does not flash

Flash Point(C)

does not flash


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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
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

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