Date published: 2026-4-24

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Blood Group Lewis x Activators

The chemical class termed Blood Group Lewis x Activators refers to a collection of compounds that are designed to influence or modulate the expression, synthesis, or display of the Lewis x (Le^x) antigen structure on cells and proteins. The Lewis x structure, which is characterized as Galβ1-4(Fucα1-3)GlcNAc, is an essential component of certain glycolipids and glycoproteins found on the surfaces of various cells. The activators pertinent to this class play a pivotal role in the biochemical pathways that regulate this specific glycosylation.

Molecular synthesis, transportation, and presentation of Lewis x structures require a tightly coordinated system of enzymes, substrates, and cofactors. Blood Group Lewis x Activators often function by either directly providing necessary chemical building blocks or by modulating the activity of key enzymes that produce the Le^x structure. For instance, GDP-Fucose and UDP-Galactose are essential substrates for the glycosyltransferases involved in the formation of Le^x structures. Meanwhile, other chemicals in this class might interact with the cellular machinery responsible for glycan processing, either promoting or inhibiting specific steps in the complex assembly of the Lewis x structures. In summary, Blood Group Lewis x Activators constitute a diverse class of compounds that are integral to the molecular landscape governing the biosynthesis and display of the Lewis x antigen on cell surfaces.

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Brefeldin A

20350-15-6sc-200861C
sc-200861
sc-200861A
sc-200861B
1 mg
5 mg
25 mg
100 mg
$31.00
$53.00
$124.00
$374.00
25
(3)

A fungal metabolite that interferes with protein transport from the endoplasmic reticulum to the Golgi apparatus, affecting glycosylation patterns.

N-Acetyl-D-galactosamine

1811-31-0sc-221979
sc-221979A
sc-221979C
sc-221979B
sc-221979D
10 mg
100 mg
1 g
5 g
50 g
$51.00
$77.00
$267.00
$1040.00
$1326.00
(0)

When introduced to cells, can potentially increase the O-GalNAc type glycosylation.