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  • Regulatory status:RUO
  • Type:Sandwich ELISA, Biotin-labelled antibody
  • Other names:Vascular cell adhesion protein 1, CD106 antigen
  • Species:Human
Cat. No. Size Price

RAF118R 96 wells (1 kit) $721,83
PubMed Product Details
Technical Data


Sandwich ELISA, Biotin-labelled antibody


The human sVCAM-1 ELISA is an enzyme-linked immunosorbent assay for the quantitative detection of human sVCAM-1. The human sVCAM-1 ELISA is for research use only. Not for diagnostic or therapeutic procedures.


Serum, Plasma-EDTA, Plasma-Heparin, Plasma-Citrate, Amniotic fluid, Cell culture supernatant

Sample Requirements

100 µl (1:50 prediluted)


On blue ice packs. Upon receipt, store the product at the temperature recommended below.


Store the kit at 2–8°C. The lyophilized controls at -20°C. Under these conditions, the kit is stable until the expiration date (see label on the box).

Calibration Curve

Calibration Range

3.1–100 ng/ml

Limit of Detection

0.6 ng/ml

Intra-assay (Within-Run)

CV = 3.1%

Inter-assay (Run-to-Run)

CV = 5.2%

Spiking Recovery


Dilution Linearity




  • RUO
  • calibration range 3.1-100 ng/ml
  • limit of detection 0.6 ng/ml
  • lyophilized controls
  • intra-assay CV = 3.1%
  • inter-assay CV = 5.2%

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 cytokine-activated 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-, and IL-1, as well as to interferon- and IL-4. VCAM-1 is also present on tissue macrophages, dendritic cells, bone marrow fibroblasts, myoblasts and myotubes.

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