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Single Domain Antibody(sdAb)

Recombinant antibodies, such as single domain antibodies (sdAb), represent the new generation of engineered antibody fragments. The presence of a single monomeric variable antibody domain reduces the size, raises stability, and increases solubility in comparison to conventional antibodies. Additionally, sdAbs offer not only enhanced permeability and reduced immunogenicity, but also straightforward and cost-effective production processes.
By leveraging Synbio Technologies’ extensive expertise and advanced sdAb discovery technology, we provide our customers with a comprehensive one-stop solution for antigen production and the specific expression of recombinant sdAbs.

Highlights

Expert Antibody Production Team
Proprietary Universal Antigen Immunization Technology
Robust Phage-Display Technology Platform
Advanced Yeast-Display Technology Platform (large library capacity: ~ 10⁹)
Cost-Effective

Service Details

Service Specifications	Turnaround Time
Camel immunization (eg. dromedaries, camels, llamas, and alpacas)	10-11 Months
PBMC isolation and immune library construction
Screening of phage-displayed library
Functional assay for sdAb
Large scale yeast sdAb expression (followed by properties identification)

QUOTE

Workflow

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Deliverables

A glycerol stock of sdAb expressing bacteria (TG1)

Phage-displayed sdAb library

Top 5 identified sdAb strains and corresponding sequences

Full reports (PDF)

FAQs

What are some common applications of sdABs?

Some common applications of sbABs include:

- Diagnostic tools and assays

- Therapeutic agents, particularly in oncology and infectious diseases

- Imaging agents for medical diagnostics

- Research tools for studying protein-protein interactions and cellular processes

How are sdABs produced?

sdABs are typically produced using recombinant DNA technology in microbial systems such as E. coli, yeast, or mammalian cell cultures. This allows for high yield and consistent quality.

Can sdAbs be humanized?

Yes, sdAbs can be humanized to reduce their immunogenicity and improve compatibility with the human immune system, making them suitable for therapeutic applications in humans.

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