Custom Single Domain Antibody Production for Phosphorylation Research
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INQUIRYCreative BioMart is confident to provide our customers with unparalleled single domain antibodies for their kinase/phosphatase biology research and pharmaceutical development projects. As a leading sdAb service provider, we offer a full range of customized services from antigen preparation to antibody engineering to ensure that our customers receive requested deliverables as soon as possible.
Background
Single domain antibodies (sdAbs) are antibody fragments consisting of a single monomeric variable antibody domain yet possess fully functional and selective antigen-binding capability. sdAbs with a molecular weight of only 12-15 kDa are much smaller than common antibodies, and even smaller than Fab fragments and single-chain variable fragments. The first sdAbs were engineered from heavy-chain antibodies found in camelids. sdAbs have demonstrated high value in basic research, the development of antibody drugs or diagnostic tools, and other therapeutic applications.
Kinases and phosphatases, as highly dynamic enzymes, are key regulators of signaling pathways. Understanding their functions requires knowledge of their structural plasticity. The use of high-affinity sdAbs in crystallization complexes has been reported to help determine the conformation-specific structures of kinases. The introduction of sdAbs has also been shown to overcome some drawbacks of intact antibody-based cancer therapeutics and diagnostics.
Figure 1. Nb_GAK1 and Nb_GAK4 capture different activation states of GAK. (Chaikuad A, et al., 2014)
Advantages of sdAbs
- Small size, hydrophily, and highly stable.
- Ability to bind inaccessible or novel epitopes in challenging targets.
- Easier to transform into bacterial cells for bulk production.
- Easier to engineer bi-specific and tri-specific antibody.
- Great potential for humanization.
- Better tissue penetration.
- Improved bioavailability for pharmaceutical applications.
Capabilities
Creative BioMart offers extensive experience in the production of single domain antibodies and advanced technology to maximize the chance to produce highly specific, sensitive and reproducible antibodies within a short period of time.
Service Options
Creative BioMart offers a comprehensive set of custom single domain antibody production services. We will do our best to optimize the custom project to accommodate your needs. We also have the capacity to manufacture antibodies in large quantities.
| Applications | ||
| Biotechnological applications | Therapeutic applications | Diagnostics applications |
| Expression Systems | ||
| Bacteria | Yeast | Mammalian Cells |
| Bacillus subtilis | Pichia pastoris | CHO cells |
| Bifidobacterium longum | Saccharomyces cerevisia | HEK293 cells |
| Brevibacillus choshinensis | Fungi | NS0 myeloma cells |
| Escherichia coli | Aspergillus awamori | Plants |
| Lactobacillu jensenii | Aspergillus oryzae | Arabidopsis thaliana |
| Lactobacillus paracasei | Insects | Nicotiana benthamiana |
| Lactococcus lactis | Trichoplusia ni | Potato plants |
| Pseudoalteromonas haloplanktis | Spodoptera frugiperda | Rice |
| Additional Services | ||
| Single domain antibody library | Antibody humanization | Antibody stability improvement |
| Antibody engineering | Antibody characterization | Large-scale antibody manufacturing |
If you can't find what you are looking for in the options above, please fill out the online inquiry form and let us know more details.
Standard Service Process
Highlights
Creative BioMart provides comprehensive and flexible custom single domain antibody production services to meet the individual needs of our customers. Our advanced technology platform coupled with a large product portfolio has enabled us to successfully complete numerous challenging projects, helping our customers save time and effort. If you are interested in our services or products, please do not hesitate to contact us.
References
- Chaikuad A, et al. Structure of cyclin G-associated kinase (GAK) trapped in different conformations using nanobodies. Biochemical Journal, 2014, 459(1): 59-69.
- Eyer L & Hruska K. Single-domain antibody fragments derived from heavy-chain antibodies: a review. Vet Med, 2012, 57(9): 439-513.