HAL is a lectin that recognizes the epitopes containing α-D-N-acetylgalactosamine (GalNAc). The biological assembly of HAL is a hexamer formed by three dimers, with monomers of each dimer connected by a single disulfide bridge. The overall fold could be described as a β-sandwich fold. The GalNAc binding sites of HAL are occupied by GalNAc moieties retained by the protein sample throughout the purification process.
Fig.1 The structures of HAL. (Pietrzyk-Brzezinska & Bujacz, 2020)
HAL Production Service at CD BioGlyco
HAL has a unique structure and physiology. Therefore, it is very necessary to study HAL from extraction, purification, and characterization to activity. At CD BioGlyco, we have a professional talent team to provide efficient HAL production for clients.
HAL production services
Sample processing service
We select the healthy Helix aspersa as the raw material. By washing, blood collection, liver and protein glands, and other steps. The samples obtained are immediately stored at -80°C for further extraction. All you need to do is to hand over the samples to us.
HAL extraction service
We offer different extraction methods for lectins originating from different parts of Helix aspersa. The two main ones are tissue source and blood source.
Fig.2 Flowchart of HAL extraction. (CD BioGlyco)
HAL purification service
We offer purification methods such as column mounting with an ultraviolet (UV) detector, high-performance liquid chromatography (HPLC), etc.
Applications of HAL
HAL combined with GalNAc is a valuable tool for cancer diagnosis.
Proteomic analysis: the diabetes diagnostic test is based on HAL binding levels.
A semi-automated high-throughput glycoprotein biomarker discovery platform consisting of HAL and tandem mass spectrometry technologies.
The changes in Immunoglobulin A (IgA) and Immunoglobulin D (IgD) glycosylation patterns are also identified by HAL binding levels.
HAL is more often used in analytics, as they recognize GalNAc-containing glycans with high specificity. Therefore, it is becoming an important component of multi-lectin systems that are employed for the analysis of glycosylation patterns of proteins.
When the drug delivery system is designed, the choice of a particular lectin should depend on the type of cancer cells that are the target of the therapy. In the case of HAL, these proteins are useful mainly in targeting malignant breast and colorectal cancer, as they bind to the cell surface of this cell.
Advantages of Us
With a professional production team, and managers with great industry experience, we offer a comprehensive range of services to meet the unique requirements of our clients.
Each program is controlled in real-time by professional technicians.
For sample sources, we support our clients in delivering raw materials. Meanwhile, we provide raw materials.
Pietrzyk, A.J.; et al. Structural studies of Helix aspersa agglutinin complexed with GalNAc: A lectin that serves as a diagnostic tool. Int J Biol Macromol. 2015, 81: 1059-68.
Pietrzyk-Brzezinska, A.J.; Bujacz A. H-type lectins-structural characteristics and their applications in diagnostics, analytics and drug delivery. Int J Biol Macromol. 2020, 152: 735-747.
This service is for Research Use Only, not intended for any clinical use.
CD BioGlyco is a world-class biotechnology company with offices in many countries. Our products and services provide a viable option to what is otherwise available.
Fig.1 The structures of HAL. (Pietrzyk-Brzezinska & Bujacz, 2020)
Fig.2 Flowchart of HAL extraction. (CD BioGlyco)
