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Recombinant Human CD33 Protein(His tag), Biotinylated (HH0032CL)

Biotinylated recombinant Human CD33 Protein (P20138) (Asp 18 - His 259) with a polyhistidine tag at the C-terminus was expressed in HEK293.

Size Price Qty
25ug $649.00
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PRODUCT INFORMATION

Cat.No.
HH0032CL
Synonyms
CD33; p67; SIGLEC 3; SIGLEC3; gp67; SIGLEC-3;
Accession
Form
Lyophilized from sterile PBS, pH7.4, 10% Trehalose.
Molecular Mass
Biotinylated recombinant Human CD33 Protein carries a polyhistidine tag at the C-terminus, and has a calculated MW of 27.6 kDa. The protein migrates as 40-45 kDa on a SDS-PAGE gel under reducing condition due to glycosylation.
Endotoxin
< 1.0 EU per 1 microgram of protein (determined by LAL method).
Purity
> 95 % by SDS-PAGE.
Storage
In lyophilized state for 1 year (4°C); After reconstitution under sterile conditions for 3 months (-70°C). Avoid repeated freeze/thaw cycles.
Reconstitution
Dissolve with double distilled water.
Warning
For research use only!
Background
Putative adhesion molecule of myelomonocytic-derived cells that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules. Induces apoptosis in acute myeloid leukemia (in vitro).
Tag
His
Species
Human
Source
HEK293

BACKGROUND

Background
Putative adhesion molecule of myelomonocytic-derived cells that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules. Induces apoptosis in acute myeloid leukemia (in vitro).
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