Recombinant Human ICAM-1/CD54 Fc Chimera Avi-tag Protein, CF Summary
Accession # P05362
Gln28 inferred from enzymatic pyroglutamate treatment revealing Thr29
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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.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.|
|Reconstitution||Reconstitute at 500 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
When Human ICAM-1/CD54 (Clone 14C11) Antibody (Catalog # MAB720) is immobilized at 0.5 µg/mL (100 µL/well), Biotinylated Recombinant Human ICAM-1/CD54 Fc Chimera Avi-tag (Catalog # AVI720) binds with an ED50 of 3-18 ng/mL.
2 μg/lane of Biotinylated Recombinant Human ICAM-1/CD54 Fc Chimera Avi-tag (Catalog # AVI720) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 95-125 kDa and 195-215 kDa, respectively.
ICAM-1 (Intercellular Adhesion Molecule-1), also known as CD54, is a transmembrane cell adhesion glycoprotein and a member of the immunoglobulin supergene family. 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). Full-length ICAM-1 contains five Ig-like domains in the ECD, a single transmembrane domain and short intracellular domain. Alternative splicing of ICAM-1 results in at least six membrane-bound forms and one soluble form (1). The ECD of mature, full-length human ICAM-1 shares 78% and 54% amino acid sequence identity with rat and mouse ICAM-1, respectively. ICAM-1 plays an important role in both innate and adaptive immune responses and is upregulated in endothelial and epithelial cells at sites of inflammation (2, 3). ICAM-1 mediates vascular adhesion and paracellular migration of leukocytes expressing activated LFA-1 (CD11a/CD18) and Mac-1 (CD11b/CD18) 2, 3). It also binds several non-integrin ligands including CD43/Sialophorin, Fibrinogen, Hyaluronan, rhinoviruses, and Plasmodium falciparum-infected erythrocytes (4-8). Soluble ICAM-1 promotes angiogenesis and serves as an indicator of vascular endothelial cell activation or damage (9). Elevated levels of soluble ICAM-1 are associated with cardiovascular disease, type 2 diabetes, organ transplant dysfunction, oxidant stress, increased abdominal fat mass, hypertension, liver disease, certain malignancies, and cerebral malaria (10-18). More recently, ICAM-1 was shown to be a novel regulator of group 2 innate lymphoid cells (ILC2s) which play a key role in allergic airway inflammation (19).
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