SpyTag and SpyCatcher Products
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Custom Recombinant Monoclonal Antibody Generation
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Custom Recombinant Monoclonal Antibody Generation
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Reagents Supporting Antibodies and Proteins Incorporating SpyTag
The innovative SpyTag and SpyCatcher technology has been employed by the scientific community in many ways to address the challenges of detecting and controlling proteins.
We have added SpyTag to our recombinant Fab antibodies and produced a set of SpyCatchers to couple to the Fab, to make TrailBlazer Antibodies.
The SpyTag-SpyCatcher technology enables site-directed conjugation of antibodies to labels such as HRP and biotin, and the formation of bivalent Fabs and Ig-like constructs with human, mouse, and rabbit isotypes.
All SpyCatchers and their derivatives (Table 1) are compatible with our recombinant antibodies that incorporate a SpyTag2 at the C-terminus of the heavy chain (format Fab-F-Spy2-H). SpyCatchers can be coupled to recombinant Fab antibodies as part of our TrailBlazer Antibody Custom Service. SpyCatchers can also be purchased from our catalog for coupling by the user to an antibody or protein with a reactive SpyTag.
Product |
Description |
Availability |
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|---|---|---|---|
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Monovalent Format |
Custom Service |
Catalog Number |
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SpyCatcher2 |
SpyCatcher2 protein |
Yes |
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SpyCatcher2-CYS |
SpyCatcher2 with an engineered cysteine residue; use for site-specific chemical conjugation to a label of choice |
Yes |
|
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SpyCatcher2:Biotin |
SpyCatcher2 conjugated to biotin |
Yes |
Inquire |
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SpyCatcher2:HRP |
SpyCatcher2 conjugated to HRP |
Yes |
Inquire |
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SpyCatcher2:PE |
Spycatcher2 conjugated to RPE |
Inquire |
Inquire |
|
SpyCatcher3 |
SpyCatcher3 protein |
Yes |
|
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SpyCatcher3-CYS |
SpyCatcher3 with an engineered cysteine residue; use for site-specific conjugation to a label of choice |
Yes |
|
|
Bivalent Format |
Custom Service |
Catalog Number |
|
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BiSpyCatcher2 |
BiSpyCatcher2 protein |
Yes |
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BiSpyCatcher2-CYS |
BiSpyCatcher2 with one engineered cysteine residue; use for site-specific conjugation to a label of choice |
Yes |
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BiSpyCatcher2-CYS3 |
BiSpyCatcher2 with three engineered cysteine residues; use for site-specific conjugation to a label of choice |
Yes |
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BiSpyCatcher2:Biotin |
BiSpyCatcher2 conjugated to biotin |
Yes |
Inquire |
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BiSpyCatcher2:HRP |
BiSpyCatcher2 conjugated to HRP |
Yes |
Coming soon |
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BiSpyCatcher2:PE |
BiSpyCatcher2 conjugated to RPE |
Inquire |
Inquire |
|
Ig-like Format |
Custom Service |
Catalog Number |
|
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hIgG1-FcSpyCatcher3 |
SpyCatcher3 fused to the hinge region, CH2, and CH3 of human IgG1 |
Yes |
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hIgG1-FcSpyCatcher3:Biotin |
hIgG1-FcSpyCatcher3 conjugated to biotin |
Yes |
Inquire |
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hIgG1-FcSpyCatcher3:HRP |
hIgG1-FcSpyCatcher3 conjugated to HRP |
Yes |
Inquire |
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hIgG2-FcSpyCatcher3 |
SpyCatcher3 fused to the hinge region, CH2, and CH3 of human IgG2 |
Yes |
Coming soon |
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hIgG3-FcSpyCatcher3 |
SpyCatcher3 fused to the hinge region, CH2, and CH3 of human IgG3 |
Yes |
Coming soon |
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hIgG4-FcSpyCatcher3 |
SpyCatcher3 fused to the hinge region, CH2, and CH3 of human IgG4 |
Yes |
Coming soon |
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hIgG4-Pro-FcSpyCatcher3 |
SpyCatcher3 fused to the hinge region, CH2, and CH3 of human IgG4-Pro (S228P) |
Yes |
Coming soon |
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hIgA-FcSpyCatcher3 |
SpyCatcher3 fused to the hinge region, CH2, and CH3 of human IgA |
Yes |
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mIgG2a-FcSpyCatcher3 |
SpyCatcher3 fused to the hinge region, CH2, and CH3 of mouse IgG2a |
Yes |
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rIgG-FcSpyCatcher3 |
SpyCatcher3 fused to the hinge region, CH2, and CH3 of rabbit IgG |
Yes |
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Protocols to Get You Started
TrailBlazer Antibody Custom Services
Get more details about SpyTag technology, how it works with our custom antibody generation service, and see data for different experimental applications.
References
- Hentrich C et al. (2021). Periplasmic expression of SpyTagged antibody fragments enables rapid modular antibody assembly. Cell Chemical Biology 28, 1-12. bioRxiv preprint
- Keeble A and Howarth M (2020). Power to the protein: Enhancing and combining activities using the Spy toolbox. Chem. Sci., 11, 7,281-7,291.
- Zakeri B et al. (2012). Peptide Tag forming a rapid covalent bond to a protein, through engineering a bacterial adhesin. PNAS 109(12), 690-697.