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
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
€551.00
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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
sensitivityinwesternblotschemiluminescentdetection1 ng
substrateforblotdetectionDependent on secondary antibody
substratesforassayprocedureDependent on secondary antibody
tagStrep-tag
epitopedetectedSAWSHPQFEK

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