Neu5Gc/Neu5Ac N-Glycan Array
Neu5Gc is a major mammalian sialic acid synthesized from Neu5Ac by an enzyme that is no longer present in humans. Regardless, nonhuman, diet-derived Neu5Gc is metabolically integrated into a variety of human tissues. Human cells can biochemically recognize Neu5Gc and incorporate it into cell-surface glycoconjugates, however the immune system recognizes Neu5Gc-containing glycans as alien and produces anti-Neu5Gc antibodies resulting in inflammation. Diseases relating to chronic inflammation such as cancer, cardiovascular diseases, and thyroiditis are associated with higher levels of anti-Neu5Gc and Neu5Gc, and it is suspected to be involved in other diseases that are exacerbated by a red meat, Neu5Gc-rich diet.
Z Biotech's Neu5Gc microarray represents a broad range of N-glycans found on cell surfaces that have incorporated Neu5Gc. These arrays can be investigated with glycan-binding proteins, antibodies, or cells in order to determine their specific interaction with this Neu5Gc xenoantigen. For comparison, each array includes the precursory, non-xenogenic Neu5Ac sialic acid form of each glycan.
For the Neu5Gc/Neu5Ac N-Glycan Array user manual, click here.
click here for more.
Example 1: A subarray assayed with glycan-binding protein biotinylated SNA lectin, followed by a streptavidin-Cy3 conjugate. Array was scanned with a microarray scanner at 532nm wavelength. There is no non-specific binding for the negative control spots. A positive control and the marker show binding as expected, as well as α-2,6 sialic acid-containing N-glycans. There is generally stronger binding to Neu5Gc sialylated N-glycans.
Innovative Biochemical Analysis Solutions
These glycans are included in our standard Neu5Gc/Neu5Ac array.
Example 2: A subarray assayed with glycan-binding protein biotinylated WGA lectin, followed by streptavidin-Cy3 conjugate. Array was scanned with a microarray scanner at 532nm wavelength. There is no non-specific binding for the negative control spots. A positive control and the marker show binding as expected, as well as most N-glycans. WGA binds more strongly to sialylated N-glycans with terminal Neu5Ac.