VCAM-1/CD106 Extracellular Domain (human, recombinant)

Vascular cell adhesion molecule 1 (VCAM-1), also known as CD106, is a member of the immunoglobulin (Ig) superfamily that is involved in the adhesion and migration of leukocytes and angiogenesis.^1,2,3,4 It is composed of an extracellular domain, which may contain seven or six Ig-like repeats depending on the splice variant, a transmembrane domain, and a C-terminal domain.^5,3 VCAM-1 is constitutively expressed in dendritic cells, monocyte-derived cells, and epithelial cells and in endothelium when induced by cytokines.^1,2,5 It can be cleaved by disintegrin and metalloproteinase domain-containing protein 17 (ADAM17) and other metalloproteinases to release soluble VCAM-1 (sVCAM-1), which is a process known as shedding, and is induced by TNF-α, IL-1β, and other cytokines.³ Increased circulating levels of sVCAM-1 is associated with several diseases, including cancer, diabetes, sepsis, cardiovascular diseases, and preeclampsia, as well as parasitic infections.^6,7,8,3,9,10 Cayman’s VCAM-1/CD106 Extracellular Domain (human, recombinant) protein can be used for cell-based adhesion assays. This protein is a disulfide-linked homodimer. The reduced monomer, composed of VCAM-1 (amino acids 25-697) fused to human IgG1 Fc at its C-terminus, consists of 911 amino acids, has a calculated molecular weight of 100.8 kDa, and a predicted N-terminus of Phe25 after signal peptide cleavage. As a result of glycosylation, the monomer migrates at approximately 116.3 kDa by SDS-PAGE under reducing conditions.

WARNING This product is not for human or veterinary use.

1. Gearing, A.J.H., Hemingway, I., Pigott, R., et al. Soluble forms of vascular adhesion molecules, E-selectin, ICAM-1, and VCAM-1: Pathological significance. Ann. N. Y. Acad. Sci. 667, 324-331 (1992).

2. Gearing, A.J.H., and Newman, W. Circulating adhesion molecules in disease. Immunol. Today 14, 506-512 (1993).

3. Troncoso, M.F., Ortiz-Quintero, J., Garrido-Moreno, V., et al. VCAM-1 as a predictor biomarker in cardiovascular disease. Biochim. Biophys. Acta Mol. Basis Dis. 1867(9), 166170 (2021).

4. Koch, A.E., Halloran, M.M., Haskell, C.J., et al. Angiogenesis mediated by soluble forms of E-selectin and vascular cell adhesion molecule-1. Nature 376(6540), 517-519 (1995).

5. Cybulsky, M.I., Fries, J.W.U., Williams, A.J., et al. Gene structure, chromosomal location, and basis for alternative mRNA splicing of the human VCAM1 gene. Proc. Natl. Acad. Sci. USA 88(17), 7859-7863 (1991).

6. Banks, R.E., Gearing, A.J.H., Hemingway, I.K., et al. Circulating intercellular adhesion molecule-1 (ICAM-1), E-selectin and vascular cell adhesion molecule-1 (VCAM-1) in human malignancies. Br. J. Cancer 68(1), 122-124 (1993).

7. Cominacini, L., Garbin, U., Pasini, A.F., et al. Increased levels of plasma ELAM-1, ICAM-1 and VCAM-1 in NIDDM: Possible role of oxidized LDL. Diabetologia 39(10), 1237-1245 (1996).

8. Cowley, H.C., Heney, D., Gearing, A.J.H., et al. Increased circulating adhesion molecule concentrations in patients with the systemic inflammatory response syndrome: A prospective cohort study. Crit. Care Med. 22(4), 651-657 (1994).

9. Lyall, F., Greer, I.A., Boswell, F., et al. The cell adhesion molecule, VCAM-1, is selectively elevated in serum in pre-eclampsia: Does this indicate the mechanism of leucocyte activation? Br. J. Obstet. Gynaecol. 101(6), 485-487 (1994).

10. Jakobsen, P.H., Morris-Jones, S., Ronn, A., et al. Increased plasma concentrations of sICAM-1, sVCAM-1 and sELAM-1 in patients with Plasmodium falciparum or P. vivax malaria and association with disease severity. Immunology 83(4), 665-669 (1994).