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ALFA Selector CE affinity resin - N1512

The ALFA tag is a novel peptide tag

This product was developed by   

 

The ALFA-tag is a novel, rationally designed epitope tag (SRLEEELRRRLTE) that forms a small and stable α-helix that is functional irrespective of its position on the target protein in prokaryotic and eukaryotic hosts. Different ALFA-tag based products are available.

 

Selector resins are based on a high-affinity single-domain antibody (sdAb) that is covalently immobilized on 4 % cross-linked agarose beads.

Single Domain
Cat. No.: N1512
Amount: 2000 µl
Price: $325.00
Cat. No. N1512

2000 µL slurry

Storage Store at 4 °C, do not freeze
Applications IP: yes (see remarks) gallery  
Immunogen synthetic peptide SRLEEELRRRLTE
Formulation 50 % slurry in PBS containing 20 % Ethanol
Shelf life Stable for 12 months
Remarks

Every unit of ALFA Selector PE comes with 10 mg of lyophilized elution peptide. If you need more elution buffer the peptide is also available as a separate product.
IP: Suitable for cold elution

Documents data sheet
MSDS
Cat. No.: N1512
Quantity: 2000 µl
Price: $325.00
Background

NanoTag® selector resins are based on a high-affinity single-domain antibody (sdAb) that is covalently immobilized on 4 % cross-linked agarose beads. The innovative, oriented and selective attachment via a flexible linker guarantees a high accessibility of the sdAbs and largely eliminates batch-to-batch variations. Due to the single-chain nature of sdAbs and their stable and covalent attachment, no leakage of light and heavy chains is observed during elution with SDS sample buffer. Selector resins thus features high affinity and superior capacity, while showing negligible unspecific background. Selector resins are compatible not only with physiological buffers but also with high stringency buffers. Selector resins thus provide great freedom to adjust the binding and washing conditions to the experimental needs.


The ALFA-tag is a novel, rationally designed epitope tag (SRLEEELRRRLTE) that forms a small and stable α-helix that is functional irrespective of its position on the target protein in prokaryotic and eukaryotic hosts.

For a poster with detailed information on the ALFA System and its applications click here


The flanking proline residues are not part of the recognition sequence, but may aid in spacial separation of the tag from the protein of interest.


For immunoprecipitations we offer two types of ALFA Selector resins. Both ALFA Selectors are based on covalently coupled nanobodies that specifically recognize ALFA-tagged targets. ALFA Selector ST (for Super-Tight) offers the highest possible affinity for ALFA-tagged targets, which can be eluted under acidic or denaturing conditions. ALFA Selector PE (for Peptide Elution) displays an engineered nanobody with lower affinity (Kd ~11 nM), which is optimized for peptide elution under physiological conditions. ALFA Selector CE (link) (for cold elutable) carries an engineered nanobody with lower affinity (Kd 100 nM), which is optimized for peptide elution under physiological conditions at low temperature (4°C). All Selector resins feature low non-specific protein adsorption and therefore allowing clean and meaningful immunoprecipitations. Due to the covalent and oriented immobilization, the immobilized nanobodies will stay on the resin even when using harsh denaturing and/or reducing conditions for elution. In contrast to conventional immunoprecipitations, eluates from both ALFA Selectors will therefore be free from large amounts of antibody fragments.