Site-Specific Antibody Conjugation with Alexa Fluor 647

Site-Specific Antibody Conjugation with Alexa Fluor 647

CD BioGlyco has developed a highly specialized Glycoengineering Platform and provides various systematic Site-Specific Antibody Conjugation Service. The efficient services and accurate results have gained a good reputation worldwide for our company.

Alexa Fluor 647 Dye

Alexa Fluor 647 dye is a bright, far-red–fluorescent dye with excitation ideally suited for the 594 nm or 633 nm laser lines. Alexa Fluor 647 conjugated antibodies are the best choice of far-red emitting dyes for multiple labeling detection with a confocal microscope, and are also widely used in immunolabeling, fluorescence microscopy, and flow cytometry.

Chemical structure of Alexa Fluor 647. (PubChem)Fig.1 Chemical structure of Alexa Fluor 647. (PubChem)

Labeled Antibodies

Labeled antibodies are the cornerstone of biological research and diagnostic testing, with applications in immunodetection, immunoassays, immunohistochemistry, cell imaging, and many others. Antibodies can be conjugated to a variety of small molecules, including biotin, fluorescent dyes, proteins, nanoparticles, and radioactive molecules. More recently, labeled antibodies have also found therapeutic applications, in which drug molecules are attached to the antibody, thereby improving disease treatment.

Cell internalization of AlexaFluor 647 conjugate of Trastuzumab made using amine chemistry.Fig.2 Cell internalization of AlexaFluor 647 conjugate of Trastuzumab made using amine chemistry. (Nath, et al., 2015)

Site-Specific Antibody Conjugation with Alexa Fluor 647 at CD BioGlyco

Antibody-drug conjugates are a new class of anticancer therapy. It can combine the efficacy of small molecule therapy with the targeting ability of antibodies. Conventional conjugates are typically produced by conjugating drugs to antibodies through side chains of surface-exposed lysines or free cysteines that reduce the generation of interchain disulfide bonds. Since antibodies contain many lysine and cysteine residues, conventional nonspecific conjugation often results in heterogeneous mixtures. This hinders analytical characterization and manufacturing.

These problems can be attributed to the coupling strategy employed. To achieve superior efficacy and safety, antibody-drug conjugates must have homogeneous dye-to-antibody ratios and attachment sites. Given a large number of reactive residues in IgG, improvement strategies for antibody-drug conjugates are challenging. Site-selective protein modification is one of a new generation of strategies capable of exploiting homogeneity requirements. Site-selective modifications can be defined as chemical and regioselective protein modifications

CD BioGlyco offers a method for the specific conjugation of antibodies labeled with Alexa Fluor 647. This technology specifically conjugates Alexa Fluor 647 to conserved N-linked glycosylation sites on the CH2 domain of each heavy chain of the Fc region.

Applications

  • Immunoassays
  • Cell imaging
  • Immunocytochemical techniques
  • Enzyme-linked immunosorbent assay

Advantages of Us

  • Site-specific conjugation
  • A highly specialized glycoengineering platform
  • Performed under physiological conditions
  • Reliable and detailed service

CD BioGlyco has an advanced glycoengineering platform and a large number of experts in glycoscience. In addition, our professional research teams allow us to provide you with high-quality services for site-specific antibody conjugation with Alexa Fluor 647. If you are interested in our services, please contact us for more details without any hesitation.

Reference:

  1. Nath, N.; et al. On-bead antibody-small molecule conjugation using high-capacity magnetic beads. Journal of Immunological Methods. 2015, 426: 95-103.
This service is for Research Use Only, not intended for any clinical use.

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About Us

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.

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