Recombinant Mouse MGL2/CD301b Protein (His Tag) | PKSM041306

Recombinant Mouse MGL2/CD301b Protein (His Tag) | PKSM041306 | Gentaur US, UK & Europe Disrtribition

Synonyms: Mgl2;CD301b;Macrophage galactose N-acetyl-galactosamine-specific lectin 2;Macrophage Galactose-type C-lectin 2

Active Protein: N/A

Activity: Recombinant Mouse MGL2 is produced by our Mammalian expression system and the target gene encoding Ser72-Pro232 is expressed with a 6His tag at the N-terminus.

Protein Construction: Recombinant Mouse MGL2 is produced by our Mammalian expression system and the target gene encoding Ser72-Pro232 is expressed with a 6His tag at the N-terminus.

Fusion Tag: N-His

Species: Mouse

Expressed Host: Human Cells

Shipping: This product is provided as lyophilized powder which is shipped with ice packs.

Purity: > 95 % as determined by reducing SDS-PAGE.

Endotoxin: < 1.0 EU per μg as determined by the LAL method.

Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

Molecular Mass: 30.9 kDa

Formulation: Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.

Reconstitution: Please refer to the printed manual for detailed information.

Background: Macrophage galactose N-acetyl-galactosamine-specific lectin 2(Mgl2), also known as CD301b, is a 38 kDa member that belongs to the C-type lectin family. Two MGL proteins are encoded by separate genes in the mouse, but share 91% amino acid (aa) identity in the extracellular domain (ECD). Only one MGL occurs in human and rat and this MGL is structurally more similar to mouse MGL1 than MGL2. However, human MGL and mouse MGL2 both bind specifically to terminal GalNAc residues, in contrast with mouse MGL1 which binds Lewis X. GalNAc recognition is likely to be important in dendritic cell-mediated tolerance to self-gangliosides as well as recognition of tumor antigens and parasite glycoproteins.

Research Area: N/A