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Recombinant Mouse MGL2/CD301b Protein (His Tag)
Recombinant Mouse MGL2/CD301b Protein (His Tag)
Artikelnummer
ELSPKSM041306-10
Verpackungseinheit
10 µg
Hersteller
Elabscience Biotechnology
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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.
Sequence: Ser72-Pro232.
Fusion tag: N-His.
Accession: Q8JZN1.
Purity: > 95 % as determined by reducing SDS-PAGE.
Endotoxin: < 1.0 EU per μg as determined by the LAL method.
Mol Mass: 30.9 kDa.
AP Mol Mass: 30-40 kDa.
Formulation: Lyophilized from a 0.2 μm filtered solution of PBS,pH 7.4.
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.
Sequence: Ser72-Pro232.
Fusion tag: N-His.
Accession: Q8JZN1.
Purity: > 95 % as determined by reducing SDS-PAGE.
Endotoxin: < 1.0 EU per μg as determined by the LAL method.
Mol Mass: 30.9 kDa.
AP Mol Mass: 30-40 kDa.
Formulation: Lyophilized from a 0.2 μm filtered solution of PBS,pH 7.4.
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.
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