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Manufactured by BioVendor

VCAM-1 Human HEK293 cells

  • Regulatory status:RUO
  • Type:Recombinant protein
  • Source:HEK293 cells
  • Other names:Vascular cell adhesion protein 1, CD106 antigen
  • Species:Human
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Cat. No. Size Price

RBG10340010 10 µg
RBG10340050 50 µg
RBG10340100 100 μg
PubMed Product Details
Technical Data


Recombinant protein


VCAM is a 110 kDa, cell surface integral membrane glycoprotein that belongs to the Ig-related superfamily of adhesion molecules. The primary function of VCAM-1 is the mediation of leukocyte-endothelial cell adhesion and signal transduction. VCAM-1 may play a vital role in the development of several diseases, including atherosclerosis and rheumatoid arthritis. The human VCAM-1 gene codes for a 715 amino acid transmembrane glycoprotein containing a 19 amino acid cytoplasmic domain, a 22 amino acid transmembrane domain, and a 674 amino acid extracellular domain. Recombinant Human VCAM-1 is a 74.1 kDa glycoprotein comprising the extracellular domain (674 amino acid residues) of VCAM-1. Monomeric glycosylated VCAM-1 migrates at an apparent molecular weight of approximately 90.0 kDa by SDS-PAGE analysis under reducing conditions.

Amino Acid Sequence



HEK293 cells



Biological Activity

Determined by its ability to support the adhesion of human U937 cells. The expected ED50 for this effect is 0.8–1.0 μg/ml.


Endotoxin level is <0.1 ng/μg of protein (<1EU/μg).


Centrifuge the vial prior to opening. Reconstitute in water to a concentration of 0.1–1.0 mg/ml. Do not vortex. For extended storage, it is recommended to further dilute in a buffer containing a carrier protein (example 0.1% BSA) and store in working aliquots at –20°C to –80°C.




Research topic

Cell adhesion proteins


The vascular cell adhesion molecule-1 (VCAM-1) or CD106 is a member of the immunoglobulin gene superfamily. The initial molecular cloning of VCAM-1 reported six extracellular Ig-like domains (6D VCAM-1). This 6D VCAM-1 arises due to alternative splicing from a seven-domain VCAM-1 (7D VCAM-1). 7D VCAM-1 is the dominant form expressed by cultured human endothelial cells. Domains 1 through 3 are highly homologous to domains 4 through 6, suggesting that they arose by gene duplication. The cDNA of 7D VCAM-1 predicts a core protein of approximately 81 kDa with seven potential N-linked glycosylation sites. Upon complete glycosylation the mature protein has a molecular weight of approximately 102 kDa. This observation is in general agreement with immunoprecipitation studies that show a protein of approximately 110 kDa on cytokineactivated endothelium. Murine and rat VCAM-1 have been cloned. In contrast to ICAM-1, VCAM-1 appears to have been highly conserved through evolution. Both rat and mouse VCAM-1 are highly homologous at the protein level to the human VCAM-1 (77% and 76%, respectively). VCAM-1 supports the adhesion of lymphocytes, monocytes, natural killer cells, eosinophils, and basophils through its interaction with leukocyte very late antigen-4 (VLA-4). VCAM-1/VLA- 4 interaction mediates firm adherence of circulating non-neutrophilic leukocytes to endothelium. VCAM-1 also participates in leukocyte adhesion outside of the vasculature, mediating precursor lymphocyte adhesion to bone marrow stromal cells and B cell binding to lymph node follicular dendritic cells. VCAM-1 is not constitutively expressed on endothelium, but can be up-regulated in vitro in response to LPS, TNF-a, and IL-1, as well as to interferon-g and IL-4. VCAM-1 is also present on tissue macrophages, dendritic cells, bone marrow fibroblasts, myoblasts and myotubes. A soluble form of VCAM-1 (sVCAM-1) has been described. Soluble VCAM-1 levels have been found in the serum of healthy individuals and increased levels of sVCAM-1 can be detected in several diseases.

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