Wisteria floribunda Lectin Production Service

Wisteria floribunda Lectin Production Service

Wisteria floribunda Lectin (WFL) Production Services at CD BioGlyco

Lectins have been used in a variety of fields due to their ability to agglutinate cells. CD BioGlyco offers a wide range of Lectin Production Services based on our advanced glycobiology technology. For Plant Lectin Production, we have extensive experience. Moreover, we have prepared several related Lectin Products for clients to choose from. Among them, we provide WFL production services including but not limited to the following.

  • Extraction isolation and purification

First, we use saline to soakWisteria floribunda seeds. Then it is crushed. Secondly, we collect the precipitated portion through operations such as centrifugation and salting out to obtain the crude WFL.

In the second step, we purify the crude product by separation with Affinity Chromatography residence and collect the elution peaks. Then it is dialyzed and freeze-dried to obtain WFL.

Procedure for the isolation and purification of WFL. (CD BioGlyco) Fig.1 Procedure for the isolation and purification of WFL. (CD BioGlyco)

  • Properties analysis
    • Hemagglutination viability
      We test the hemagglutination viability of lectin extracts using aldehyde-formalized animal erythrocytes. For the aldolization of fresh animal erythrocytes glutaraldehyde method is used.
    • Protein content
      We use animal serum proteins as a control to make a standard curve. The protein content is tested using an ultraviolet and visible spectrophotometer (UV).
    • Molecular weight
      We use the polyacrylamide gel electrophoresis (PAGE) method to determine the molecular weight of lectins.
    • Protein subunit composition
      Using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) to determine the subunit composition as well as the molecular weight size of WFL.
    • Isoelectric point
      Using disk continuous isoelectric focusing electrophoresis, to test the isoelectric point of WFL.
    • Amino acid composition
      Amino acid composition in lectins is determined using an amino acid analyzer by hydrolyzing the sample in redistilled hydrochloric acid. In this case, cysteine is determined by hydrolyzing the sample and then performing acid oxidation. Tryptophan is determined by spectrophotometry.
    • Sugar-binding property
      We mix different sugar solutions with the lectin solution, leave it to stand, add animal erythrocyte suspension to it, and observe the agglutination activity of the lectin. Different results are compared to get the sugar-binding property of lectin and the magnitude of sugar inhibition of hemagglutination. This method is also known as the semi-antigenic inhibition test.

Property testing services. (CD BioGlyco) Fig.2 Property testing services. (CD BioGlyco)

Applications

  • WFL has sugar-binding specificity and it is used in research on cytogenetics and clinical immunity.
  • WFL is used for the detection and analysis of cell surface glycans.
  • WFL is used to help plants acquire appropriate pest resistance or nitrogen fixation in a non-transgenic state.

Advantages of Us

  • We take the confidentiality of our client's projects very seriously and always make it a core principle of our work.
  • We provide custom lectin production services to our clients according to their scientific needs.
  • We use advanced technical equipment and high-quality raw materials to ensure that we provide products with high purity, good stability, and reliable quality.

CD BioGlyco has an experienced R&D team with advanced technology to provide lectin production services to clients worldwide. Our programs are tailored to the needs of our clients to ensure that we help them solve the challenges they encounter in their research. Please feel free to contact us if you are interested in our services and have any questions.

Reference:

  1. grawal, S.B.; et al. Anticancer activity of lectins from Bauhinia purpurea and Wisteria floribunda on breast cancer MCF-7 cell lines. Protein & Peptide Letters. 2020, 27(9): 870-877.
This service is for Research Use Only, not intended for any clinical use.

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