Recombinant Human CD162 protein with C-terminal 6×His tag
Figure 1. Human CD162 Protein, His Tag on SDS-PAGE under reducing condition.
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Amount : | 50 µg |
Purification : | The purity of the protein is greater than 95% as determined by SDS-PAGE and Coomassie blue staining. |
Content : | Lyophilized from sterile PBS, pH 7.4. Normally 5 % - 8 % trehalose is added as protectants before lyophilization. |
Storage condition : | Store at -80°C for 12 months (Avoid repeated freezing and thawing) |
Alternative Name : | PSGL1,CD162,SELPLG,Selectin P ligand |
Expression Host : HEK293
The protein has a predicted molecular mass of 31.4 kDa after removal of the signal peptide.The apparent molecular mass of CD162-His is approximately 70-100 kDa due to glycosylation.
This gene encodes a glycoprotein that functions as a high affinity counter-receptor for the cell adhesion molecules P-, E- and L- selectin expressed on myeloid cells and stimulated T lymphocytes. As such, this protein plays a critical role in leukocyte trafficking during inflammation by tethering of leukocytes to activated platelets or endothelia expressing selectins. This protein requires two post-translational modifications, tyrosine sulfation and the addition of the sialyl Lewis x tetrasaccharide (sLex) to its O-linked glycans, for its high-affinity binding activity. Aberrant expression of this gene and polymorphisms in this gene are associated with defects in the innate and adaptive immune response. Alternate splicing results in multiple transcript variants.
The protein has a predicted molecular mass of 31.4 kDa after removal of the signal peptide.The apparent molecular mass of CD162-His is approximately 70-100 kDa due to glycosylation.
This gene encodes a glycoprotein that functions as a high affinity counter-receptor for the cell adhesion molecules P-, E- and L- selectin expressed on myeloid cells and stimulated T lymphocytes. As such, this protein plays a critical role in leukocyte trafficking during inflammation by tethering of leukocytes to activated platelets or endothelia expressing selectins. This protein requires two post-translational modifications, tyrosine sulfation and the addition of the sialyl Lewis x tetrasaccharide (sLex) to its O-linked glycans, for its high-affinity binding activity. Aberrant expression of this gene and polymorphisms in this gene are associated with defects in the innate and adaptive immune response. Alternate splicing results in multiple transcript variants.
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