VCAM1 ELISA Kit

Catalog No. ABIN4987154

Product Details VCAM1 ELISA Kit

Target: VCAM1 (Vascular Cell Adhesion Molecule 1 (VCAM1))

Reactivity: Human

Detection Method: Colorimetric

Method Type: Sandwich ELISA

Detection Range: 62.5-4000 pg/mL

Minimum Detection Limit: 62.5 pg/mL

Application: ELISA

Sample Type: Cell Culture Supernatant, Serum, Plasma (heparin), Plasma (citrate), Plasma (EDTA)

Analytical Method: Quantitative

Specificity: Natural and recombinant Human VCAM-1 Ligand

Sensitivity: 31 pg/mL

Material not included:

• Microplate reader.
• Pipettes and pipette tips.
• EP tube Deionized or distilled water.

Application Details

Application Notes: Detection Wavelength: 450 nm

Sample Volume: 20 μL

Assay Time: 3 h

Plate: Pre-coated

Restrictions: For Research Use only

Handling

Storage: 4 °C

Target Details for VCAM1

Target: VCAM1 (Vascular Cell Adhesion Molecule 1 (VCAM1))

Alternative Name: VCAM-1 (VCAM1 Products)

Synonyms: CD106 ELISA Kit, INCAM-100 ELISA Kit, Vcam-1 ELISA Kit, VCAM1B ELISA Kit, fi76d06 ELISA Kit, wu:fi76d06 ELISA Kit, zgc:158875 ELISA Kit, VCAM1 ELISA Kit, vascular cell adhesion molecule 1 ELISA Kit, vascular cell adhesion molecule 1b ELISA Kit, VCAM1 ELISA Kit, Vcam1 ELISA Kit, vcam1b ELISA Kit, VCAM-1 ELISA Kit

Background: Human Vascular Cell Adhesion Molecule-1 (VCAM-1) is a 100 - 110 kDa, 715 amino acid (aa) type I transmembrane glycoprotein typically characterized by the presence of seven C2-type immunoglobulin (Ig) domains (1 - 3). Its extracellular region is 674 aa in length, followed by a 22 aa transmembrane segment and a 19 aa cytoplasmic tail (1, 2). In the extracellular region, there are multiple N-linked glycosylation sites (the predicted molecular weight is 80 kDa), and each C2 domain is closed by a disulfide bridge. There is considerable interspecies VCAM-1 homology, with mouse and rat VCAM-1 showing approximately 75 % aa identity to human VCAM-1 (2 - 4). Notably, the short 19 aa cytoplasmic tail is absolutely conserved, mouse to human to rat (4). Cells expressing mouse VCAM-1 bind both mouse and human leukocytes, and this reflects their high degree of aa identity (4). A number of variants of VCAM-1 are known to occur, all of which are likely the result of alternate gene splicing. In particular, a human six Ig domain molecule is known (1), and in rabbits, an eight Ig domain form has been identified (2). There is also a three-C2 domain, 43 kDa GPI-linked form of VCAM-1 (5, 6). Although it binds known VCAM-1 ligands (or co-receptors), its function is unclear. Cells known to express VCAM-1 include neurons (7), endothelial cells (8), smooth muscle cells (9), fibroblasts (10) and macrophages (11). Soluble VCAM-1 has been identified in culture supernates (12), blood (13 - 15), and cerebrospinal fluid (15, 16). In vitro, basal levels of VCAM-1 shedding by unstimulated NIH3T3 cells appear to partially require metalloproteinase activity, while PMA-induced shedding is dependent upon the proteolytic activity of TACE/ADAM17 (12).Functionally, VCAM-1 binds to both a4b1 (VLA-4) and a4b7 (LPAM-1) integrins (17, 18). These integrins (or VCAM-1 ligands) are expressed on a variety of cells, with VLA-4 found on all leukocytes with the exception of neutrophils (17, 19, 20). Because of this, VCAM-1/VCAM-1 ligand interactions are undoubtedly key events in the rate and timing of leukocyte extravasation(3). Other roles proposed for VCAM-1 include the regulation of osteoclastogenesis via a cell-to-cell contact mechanism (22) and the induction of sickle cell adherence to vascular endothelial cells during hypoxemia (23).

Pathways: Carbohydrate Homeostasis