Helix Pomatia Lectin Production Service

Helix Pomatia Lectin Production Service

The Specific Binding of Helix pomatia Lectin (HPL)

HPL recognizes a range of O-linked glycans bearing the terminal monosaccharide GalNAc, including blood group A substance, Forssman antigens, Tn epitope, and, to a lesser extent, terminal GlcNAc. HPL also binds to Thomsen Friedenreich (TF) antigen and ganglioside GD2, a tumor-associated carbohydrate antigen. Crystallographic studies of HPL revealed a new β-sandwich lectin fold. Three disulfide-linked dimers form the HPL hexamer. Six GalNAc binding sites are characterized in the HPL-GalNAc crystal structure.

Fig.1 Glycan array analysis of HPL as measured by fluorescence intensity. (Sanchez, et al., 2016)Fig.1 Glycan array analysis of HPL as measured by fluorescence intensity. (Sanchez, et al., 2016)

HPL Production Service at CD BioGlyco

HPL attracts much attention due to its specificity and multimeric molecular architecture, so it is essential to produce, isolate, and identify HPL as comprehensively as possible. At CD BioGlyco, we develop a complete set of HPL production and profiling services.

  • HPL production service
  • We select the healthy Helix pomatia as the raw material. Then, we extract lectins from HP's mucus, lymph, and protein glands. It's worth mentioning that we offer different isolation and extraction methods for different tissue sites. Especially, the lectins in protein glands are extremely temperature dependent and are not suitable for extraction at room temperature.
  • Based on knowledge of cDNA sequence and structural features, we support the production of a large number of recombinant HPL services with constant quality.
  • HPL immunohistochemistry service

HPL glycoproteins are isolated from fresh specimens by affinity chromatography, and analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and western blotting. We assess alteration in cellular glycosylation, detected by HPL binding. Moreover, we provide an analysis of qualitative and quantitative differences in HPL-binding glycoproteins.

We provide professional HPL microarray determination services. After labeling HPL with the markers, the labeled sample is purified on a polyacrylamide desalting column. The labeled HPL is used to probe the printed glycan arrays.

Fig.2 Schematic diagram of HPL production and analysis. (CD BioGlyco)Fig.2 Schematic diagram of HPL production and analysis. (CD BioGlyco)

Applications of HPL

  • Testing of HPL to distinguish tumor cells from healthy cells also reflects subtle alterations in glycosylation profiles.
  • HPL is a major group of glycan-binding proteins characterized and defined by the presence of carbohydrate-recognizing domains.
  • HPL has been demonstrated to be a useful tool in histopathology. Identification of O-linked glycoproteins binding to the HPL as markers of metastatic colorectal cancer. The use of the HPL as a prognostic indicator and as a tool in cancer research.
  • HPL agglutinates blood cells, thus facilitating hematology research. It is used in cytology, hematology research, and biotechnology research.
  • HPL-containing fluorophores are applied in the testing industry.

Advantages of Us

  • Our professional talent team customizes the service process according to client needs. In addition, we provide analysis for HPL-binding glycoproteins on cells.
  • We customize cell culture programs or mouse growth cycle services throughout the process. All data will be sent to the client’s email address as soon as possible.

At CD BioGlyco, our professional team includes experienced technicians and knowledgeable scientists to provide clients with fast, reliable Animal Lectin Production Services. Clients in various countries have recognized our positive and serious attitude and high level of service. Please feel free to contact us anytime if you have any needs.

References

  1. Parameswaran, R.; et al. Helix pomatia agglutinin binding glycoproteins in thyroid tumors. World J Surg. 2011, 35(10): 2219-2227.
  2. Parameswaran, R.; et al. Binding of aberrant glycoproteins recognizable by Helix pomatia agglutinin in adrenal cancers. BJS Open. 2018, 2(5): 353-359.
  3. Simplicien, M.; et al. The T/Tn-specific Helix pomatia lectin induces cell death in lymphoma cells negative for T/Tn antigens. Cancers (Basel). 2021, 13(17): 4356.
  4. Sanchez, J.F.; et al. Biochemical and structural analysis of Helix pomatia agglutinin. A hexameric lectin with a novel fold. Journal of Biological Chemistry. 2006, 281(29): 20171-20180.
This service is for Research Use Only, not intended for any clinical use.

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