α-linked Galactose-binding Lectin Production Service

α-linked Galactose-binding Lectin Production Service

A Complete Set of Recombinant Lectin Production Services at CD BioGlyco

  • Production service
  • Select strains and vector: According to the characteristics of the α-linked galactose-binding lectin, obtain the corresponding gene sequences or expression vectors.
  • Expression vector construction: The target gene sequences are cloned into the appropriate expression vector to allow for expression in the host cells. These services include the insertion of the target gene, selecting a suitable promoter, and selecting the appropriate tag or reporter.
  • Transformation, culture, and expression: The transformed host cells are cultured and protein expression is performed under appropriate culture conditions. Our technicians optimize the expression parameters including regulating the medium components, temperature, pH, stirring speed, and other parameters to promote efficient protein expression.
  • Collection and extraction: After a certain time, collect host cell cultures and perform such as cell fragmentation or centrifugation to obtain the target protein.
  • Purification and analysis service

We provide various purification services, including but not limited to affinity purification, ion-column purification, hydrophobic packing purification, and molecular sieve purification. Subsequently, we provide identification and quantification for proteins by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), western blot, mass spectrometry, etc. In addition, if clients need to conduct functional and applied studies on the obtained α-linked galactose-binding lectins, such as enzyme activity determination, structural analysis, or interaction study, our professional team's relevant personalized services.

Fig.1 Flow chart of the recombinant lectin production process. (CD BioGlyco)Fig.1 Flow chart of the recombinant lectin production process. (CD BioGlyco)

Publication

Paper Title: Expression of frutalin, an α-D-galactose-binding jacalin-related lectin, in the yeast Pichia pastoris

Expression System: Yeast-Pichia pastoris

Journal: Protein Expression and Purification

Published: 2008

Results: The recombinant protein was directed to be secreted by optimized cloning of the coding mature sequence into the pPICZαA expression vector, which was applied to protein expression in Pichia pastoris. The soluble recombinant protein was successfully detected in the supernatant. Frutalin was found to be expressed as a single chain by SDS-PAGE and Edman degradation analysis. In addition, a terminal repeat sequence was found possibly due to incomplete signal sequence processing. Recombinant frutalin bound specifically to the monosaccharide Me-α-galactose and had similar binding properties to natural lectin. Showed that Pichia pastoris was an excellent host for the expression of recombinant lectins.

Fig.2 Schematic representation of the expression and processing of recombinant lectins in yeast. (Oliveira, et al., 2008)Fig.2 Schematic representation of the expression and processing of recombinant lectins in yeast. (Oliveira, et al., 2008)

Advantages of Us

  • Our professional researchers select the expression system and host according to the target lectin properties to ensure optimal production services.
  • According to client needs, we provide small-scale and mass-production services.

CD BioGlyco is a professional company that provides Lectin Production services. Based on Galactose-binding Lectin, we offer different specificity lectin production and analysis services. Moreover, we offer Mannan-binding Lectin and Sialic Acid-binding Lectin production services. Please feel free to contact us if you are interested in our lectin service.

References

  1. Kirkeby, S.; Moe, D. Lectin interactions with alpha-galactosylated xenoantigens. Xenotransplantation. 2002, 9(4): 260-7.
  2. Oliveira, C.; et al. Expression of frutalin, an alpha-D-galactose-binding jacalin-related lectin, in the yeast Pichia pastoris. Protein Expr Purif. 2008, 60(2): 188-93.
This service is for Research Use Only, not intended for any clinical use.

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