Strep-tag Antibody

For highly sensitive and specific detection of Strep-tagged proteins

Features

  • Excellent results in dot- and western-blotting procedures
  • Highly sensitive and specific detection
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Strep-tag Antibody (100 μg)

Cat. No. / ID: 34850

Mouse monoclonal antibody that recognizes the Strep-tag II epitope; lyophilized, for 1000 ml working solution
€667.00
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The Strep-tag Antibody is intended for molecular biology applications. This product is not intended for the diagnosis, prevention, or treatment of a disease.

Product Details

Monoclonal mouse Strep-tag antibodies are used to detect recombinant proteins carrying the short Strep-tag affinity tag epitope with high specificity and sensitivity. Like all QIAGEN mouse monoclonal antibodies, they are prepared under serum-free conditions — guaranteeing absence of viruses, mycoplasma, and contaminating immunoglobulins.

Performance

The Strep-tag Antibody allows highly sensitive detection of proteins (see figures  Highly sensitive detection of proteins carrying a Strep-tag and  Ultrapure protein in two steps)
See figures

Principle

The Two-Step Affinity Purification System, which is based on the proven 6xHis tag and the short Strep-tag II, enables simple and highly efficient purification of ultrapure proteins in a fast and standardized procedure. Recombinant proteins carrying both tags are purified sequentially on Ni-NTA and Strep-Tactin matrices (see figure  Ultrapure protein in two steps). The two simple affinity purifications provide fully active, full-length, ultrapure protein, suitable for any downstream application.

See figures

Procedure

Recombinant proteins that carry two small affinity tags (the 6xHis tag and Strep-tag II) are efficiently expressed in E. coli, insect, or mammalian cells using pQE-TriSystem His·Strep vectors. After cell lysis and clearing of the lysate, proteins are initially purified using an immobilized-metal affinity chromatography procedure that is based on the proven 6xHis-tag-Ni-NTA interaction. After elution from the Ni-NTA matrix using imidazole, recombinant proteins (which also carry the Strep-tag II epitope) are loaded directly onto a Strep-Tactin matrix. No buffer exchange is required. Protein is eluted from the Strep-Tactin matrix using either biotin or desthiobiotin. This two-step affinity purification delivers ultrapure (>98% pure) protein (see figure  Two-step affinity purification procedure). The order of purifications can be reversed (i.e., Strep-Tactin followed by Ni- NTA purification). Proteins can be detected with high specificity and sensitivity using mouse monoclonal Strep-tag or Anti·His antibodies.

See figures

Applications

The two-step affinity purification system, using the Strep-tag Antibody for detection, is highly suited for applications where high purity is at a premium or is difficult to achieve. The standardized purification procedure also increases throughput by eliminating the need for protein-specific purification protocol development and optimization. The ultrahigh purity and convenience provided by the two-step affinity purification system make it the method of choice for:

  • Structural and functional analyses
  • Expression in eukaryotic systems

Supporting data and figures

Specifications

FeaturesSpecifications
ApplicationsWestern blot, dot blot, ELISA, immunoprecipitation, immunohistochemistry
DetectionSecondary antibody required
Sensitivity in Western blots (chemiluminescent detection)1 ng
Substrate for blot detectionDependent on secondary antibody
Substrates for assay procedureDependent on secondary antibody
TagStrep-tag
Epitope detectedSAWSHPQFEK

Resources

Kit Handbooks (1)

FAQ

What is the basic technology behind the Strep-tag Protein Purification System?

The basic technology behind the Strep-tag System is a Two-Step Affinity Protein Purification using sequential purification of recombinant proteins carrying two affinity tags. Proteins that carry these two small tags (the 6xHis tag and the 8 amino acid containing Strep-tag) are efficiently expressed in E. coli, insect, or mammalian cells using pQE-TriSystem His·Strep vectors. After cell lysis and clearing of the lysate, proteins are initially purified by a procedure based on the proven 6xHis-tag-Ni-NTA interaction. After elution from the Ni-NTA matrix using imidazole, recombinant proteins (which also carry the Strep-tag epitope) are loaded directly onto a Strep-Tactin matrix (Strep-Tactin SuperFlow or Strep-Tactin Magnetic Beads). Protein is eluted from the Strep-Tactin matrix using either biotin or desthiobiotin. This two-step affinity purification delivers ultrapure (>98% pure) protein. The order of purifications can also be reversed (i.e., Strep-Tactin followed by Ni-NTA purification). Since purification is done under native conditions, the Two-Step Affinity Purification System can be beneficial for highly demanding applications (i.e., crystallization studies).

 

FAQ ID -740
What is the concentration of SureENTRY Transduction Reagent?
The concentration of SureENTRY Transduction Reagent is 10 mg/ml.
FAQ ID - 3708