Recombinant Human ICAM-4 Fc Chimera Protein, CF

Recombinant Human ICAM-4 Fc Chimera Protein, CF Summary

Product Specifications

Product Datasheets

Carrier Free

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

Background: ICAM-4

ICAM-4 (intercellular adhesion molecule-4), also known as CD242, is a transmembrane cell adhesion glycoprotein and a member of the immunoglobulin protein superfamily. The ICAM sub-family consists of five members, ICAM-1 through ICAM-5, and they vary in their tissue expression and number of Ig-like domains in the extracellular domain (ECD) (1). Full-length human ICAM-4 contains 2 Ig-like domains in the ECD, a single transmembrane domain and short intracellular domain. Alternative splicing of ICAM-4 results in at least one soluble form (2). The ECD of mature human ICAM-4 shares 68% and 67% amino acid sequence identity with mouse and rat ICAM-4, respectively. ICAM-4 expression is limited to erythroid and possibly placental tissue but its biological role remains poorly defined (3). ICAM-4 has been shown to bind alpha 4 beta 1 and alpha V family integrins as well as displaying broad ligand binding specificity for some beta 1, beta 2, beta 3 and beta 5 integrins (4, 5). ICAM-4 binding to endothelial alpha v beta 3 has been indicated as a factor in vaso-occlusion, particularly in sickle cell disease (6). ICAM-4 is expressed on red blood cells (RBC), erythroid precursor cells, and possibly placental tissue (3, 7). ICAM-4 has shown to bind alpha 4 beta 1 on hemopoietic cells, alpha V family integrins (avb1, avb3, and avb5) on non-hemopoietic cells as well as displaying broad ligand binding specificity for some beta 1, beta 2, beta 3 and beta 5 integrins (4, 5, 7). Studies have shown aLb2 integrin interacts through the first Ig-like domain of ICAM-4, whereas aMb2 and aXb2 integrins interact through both Ig-like domains of ICAM-4 (7). In addition, initiation of vaso-occlusion in sickle cell disease is implicated by ICAM-4 binding to endothelial alpha v beta 3 integrin (6). The ability of ICAM-4 to interact selectively with different integrins suggests its importance in RBC physiology and pathology as well as its therapeutic value.

Related Research Areas

• Adhesion Molecules in Angiogenesis
• Immunoglobulin Superfamily CAMs