Creative Biolabs-Immuno-oncology

B Cell based Small-Angle Scattering Assay Service

Creative Biolabs provides specific deliverables that empower you to make data-driven decisions at the earliest stages of biotherapeutic development. You can expect to receive comprehensive structural insights that predict an antibody's stability and function, allowing you to de-risk your pipeline and focus on the most promising candidates. Our service delivers low-resolution 3D models of your antibodies in their native solution state and critical data on their conformational flexibility and aggregation behavior. By identifying potential issues early, we help you avoid costly failures in later development phases.

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Brief Summary of Small-angle Scattering Assay

Small-angle X-ray scattering (SAXS) is a valuable structure analysis technique applied to acquire data on the shape, structure changes, and size of macromolecules in solution. SAXS is typically used to study the interactions between macromolecules and the functional mechanisms of molecules in cells. This method can offer low-resolution structural graphs of bound proteins, such as an antigen-antibody complex, on the shape, conformation, and binding state.

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Fig.1 The principle of biological SAXS experiment. (OA Literature)Fig.1 Schematic representation of a SAXS experiment. 1

What We Can Offer

Function Software Description
Experimental data processing PRIMUS, GNOM, CHROMIXS Primary data processing
Ab initio modeling MONSA, GASBOR, DAMMMIN, DAMMIF Determine shape using dummy atom model
Rigid body modeling CORAL, SASREF, BUNCH, GLOBSYMM Model the multiple motif ensembled complexes
Structure refines SREFLEX Refine high-resolution protein models
Model evaluation and manipulation CRYSOL, SRYSON, CIFSUP, DAMAVER, SASpy Computationally model the scattering pattern
Primary Data p(r) Modeling
Provide primary SAXS data and size determination of single antibody and antigen, as well as the formed complex. Pair distance distribution function p(r) of single antigen, antibody, and antibody-antigen complex. Ab initio shape determination of the antibody-antigen complex.
Rigid body modeling of antibody in complex with antigen.

Key Features of the small-angle scattering assay process. (Creative Biolabs Original)

Workflow of Cell-based Small-angle Scattering Assay Service

The powerful X-ray scattering techniques provided us an insight into the complex interaction between the specific antibody and peptides. A SAS model of the antibody and peptides complex could indicate the shape information on the spatial arrangement of antibodies on an antigen, antibody binding sites, and conformation.

Core steps of the small-angle scattering assay process. (Creative Biolabs Original)

Highlights

Highlights of the small-angle scattering assay process. (Creative Biolabs Original)

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Customer Reviews

FAQs

What is the main advantage of using a B cell-based SAS assay over other structural methods like crystallography?

Our assay provides crucial structural information from samples in their native solution state, without the need for crystallization. This allows us to analyze flexible or unstable molecules that are not suitable for crystallography and to gain insights into their behavior in a more biologically relevant environment.

Can this assay be used for my specific type of antibody or protein?

Absolutely. Our platform is designed to be highly versatile. As long as you can provide the required sample material, our assay can be adapted to characterize a wide range of antibody types, as well as protein-protein and antigen-antibody complexes.

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How to Contact Us

Creative Biolabs provides the cutting-edge insights you need to get ahead in biotherapeutic development. Our B cell-based small-angle scattering assay is a strategic asset for a more efficient and de-risked pipeline. Please contact us for more detailed information.

Reference

  1. Da Vela, Stefano, and Dmitri I Svergun. "Methods, development and applications of small-angle X-ray scattering to characterize biological macromolecules in solution." Current research in structural biology vol. 2 164-170. 27 Aug. 2020. Distributed under an Open Access license CC BY 4.0, without modification. https://doi.org/10.1016/j.crstbi.2020.08.004

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