CD162/PSGL-1 Protein, Human (HEK293, mFc)

CD162/PSGL-1 Protein is a sialomucin expressed on leukocytes, which through high affinity, calcium-dependent interactions with E- and P-selectins, mediates rapid rolling of leukocytes over vascular surfaces during the initial steps in inflammation^[1]. CD162/PSGL-1 Protein, Human (HEK293, mFc) is the recombinant human-derived CD162/PSGL-1 protein, expressed by HEK293 , with C-mFc labeled tag.

In humans, P-selectin glycoprotein ligand-1 (PSGL-1) (or cluster differentiation (CD) 162) is coded by selectin P ligand (SELPLG). This cellular transmembrane receptor is expressed on most hematopoietic cells, including T-cells, B-cells, neutrophils, monocytes, and platelets. PSGL-1 is a critical proinflammatory protein that is essential for the recruitment of immune cells into sites of inflammation. As such, PSGL-1 significantly contributes to the relocation of immune cells from the circulating blood to inflamed tissue. A major question concerning selectin ligands is whether they mediate physiologically relevant cell-cell interaction. PSGL-1 on other classes of leukocytes such as monocytes, T lymphocytes, and mast cells as well as on hematopoietic stem cells is likely to be a predominant ligand for P-selectin. PSGL-1 is an HIV restriction factor and HIV, in turn, utilizes several mechanisms to counter PSGL-1 activity^[1].

Human

HEK293

C-mFc

AAC50061.1(L18-V295)

6404  [NCBI]

Approximately 55.4 kDa.

Greater than 95% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.