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anti-Chicken IgY sdAb - N0705-DBCO

A monovalent single domain secondary antibody specific for chicken IgY

 

This product was developed by   

NanoTag-Biotechnologies

Camelid single domain antibodies (sdAbs) consist only of one antigen binding site of an Alpaca heavy chain antibody. With only ~15 kDa, these Tags are about 10-times smaller than conventional IgG antibody molecules.

Camelid single domain antibody
Cat. No.: N0705-DBCO
Amount: 250 µg
Price: $770.00
Cat. No. N0705-DBCO 250 µg purified antibody, lyophilized from PBS, fluorescence-labeled with DBCO.

Dibenzocyclooctyne (DBCO, ADIBO) is one of the most reactive cycloalkynes for strain promoted alkyne azide cycloaddition (spAAC), a copper-free click chemistry reaction.

Albumin was added for stabilization. For reconstitution add 250 µl H2O to get a 1mg/ml solution in PBS. Either add 1:1 (v/v) glycerol, then aliquot and store at -20°C until use, or store aliquots at -80°C without additives.
Reconstitute immediately upon receipt! Avoid bright light when working with the antibody to minimize photo bleeching of the fluorescent dye.
Applications
 
ICC: yes
FACS: yes
Label DBCO
Clone 3G2
Reactivity Reacts with: chicken.
No signal: mouse, rabbit, Guinea pig, donkey, rat, goat, pig, horse, cow, human.
Other species not tested yet.
Specificity Chicken IgY, does not cross-react with mouse, rabbit, guinea pig or rat immunglobulins
Cat. No.: N0705-DBCO
Amount: 250 µg
Price: $770.00
Background

Unlabeled variants and several modifications of sdAbs like biotin, fluorophore or DBCO conjugation are available.

 

IgY is the major immunoglobulin found in chicken eggs. FluoTag®-X2 anti-chicken is a species-specific FluoTag®-X2 directed against immunoglobulin IgY from chicken.
In FluoTag®-X2, two fluorophore molecules are coupled site-specifically to one individual FluoTag® molecule. Therefore, the reagent targets four fluorophores to your primary chicken antibody.
Due to the monovalent binding, there are no primary and secondary antibody clusters formed, leading to better epitope accessibility and a more precise localization.