Myc-Trap Affinity Reagents

Capture Myc-tagged Proteins

Purify Myc-tagged proteins without contaminating peptides

The Myc-Trap is a single chain polypeptide antibody coupled to agarose beads or magnetc agaorse beads for immunoprecipitation of Myc-tagged proteins. All Nano-Traps use a recombinant antibody fragment lacking a heavy chain. For this reason the Myc-Trap cannot dissociate from the agarose bead carrier, and therefore, offers the cleanest pulldown results. The Myc-Trap recognizes the Myc-tag sequence EQKLISEEDL at the N-terminus, C-terminus, or internal site of any fusion protein. We guarantee you’ll see the fastest and most efficient performance! Typical results yield much lower background than other commercial or home-made affinity reagents. This make Myc-Trap perfect for labs who need crystal clean results for applications like mass spectrometry or other persnickety analyses



LITERATURE
Protocols
FAQs
 
RELATED PRODUCTS
Other Nano-Trap Reagents
Antibodies
Live Cell Imaging  Microscopes

 

 

Better than traditional monoclonal antibodiesComparison of Myc-tag pulldown

To the right is a pull-down experiment comparing the Myc-Trap technology versus a conventional monoclonal Myc antibody. Most researchers today use the immobilized anti-Myc antibody 9E10 for immunoprecipitation of Myc fusion-proteins. During immunoprecipitation with 9E10, heavy and light antibody chains can dissociate from the immobilized 9E10 and contaminate the eluate of the Myc-tagged protein of interest with these antibody molecules. As you can see from the data, the single polypeptide chain used in the Myc-Trap does not suffer from this issue and provides clean results without contaminating peptides.

 

 

 

 

 

 

 

Nano-Traps

 

 

 

 

 

 

 

 

 

Camelidae Antibody

Camelidae single-domain antibodies are like IgGs on steroids

The family of animals known as Camelidae (camels, dromedaries, llamas and alpacas) produce functional antibodies devoid of light chains, so called "heavy chain" antibodies. These heavy chain antibodies recognize and bind their antigens via a single variable domain. When cleaved from their carboxy tail, these barrel-shaped structures (2x3 nm) are extraordinarily small, naturally-occurring, and intact antigen binding fragments (MW  of 13 kDa). These fragments, called Nanobodies, are characterized by high specificity and affinities in the low nanomolar range, and dissociation constants in the sub-nanomolar range (typically 10- to 100-fold better than mouse IgGs). The compact size of Nanobodies makes them extremely stable at temperatures up to 70°C, and functional even in 2M NaCl or 0.5% SDS. These small and powerful antibody fragments can be used in a variety of unique applications. They will open up your research possibilities.

 

 

 

 

SPECIFICATIONS

Configuration:

Specific Camelidae antibody linked to agarose bead

Particle Size:

~90 µm when coupled to an agarose beads

 

~40 µm when coupled to magnetic agarose

Storage Buffer: 20% EtOH

Part Numbers

YTA010, YTA020, YTA100, YTA200,YTA400, YTAK020, YTMA010, YTMA020, YGTMA100, YTMA200, YTA400, YTMAK020, YT250

Storage and Stability:

store at 4°C; stable for one year. Do not freeze.


Myc Traps Coupled to Agarose Beads

ORDERING - MycTraps Coupled to Agarose

 

 

Myc Traps Coupled to Magnetic Agarose Beads

ORDERING - Myc-Traps Coupled to Magnetic Agarose Beads

 

 

Myc Traps Non-Coupled

ORDERING - Myc-Traps Non-Coupled

 

Binding Controls
Spin Columns for agarose beads