Description
Recombinant Rat ESAM Protein (Fc Tag) | PKSR030296 | Gentaur US, UK & Europe Disrtribition
Synonyms: ESAM
Active Protein: N/A
Activity: A DNA sequence encoding the rat ESAM (Q6AYD4) extracellular domain (Met 1-Ala 251) was fused with the Fc region of human IgG1 at the C-terminus.
Protein Construction: A DNA sequence encoding the rat ESAM (Q6AYD4) extracellular domain (Met 1-Ala 251) was fused with the Fc region of human IgG1 at the C-terminus.
Fusion Tag: C-Fc
Species: Rat
Expressed Host: HEK293 Cells
Shipping: This product is provided as lyophilized powder which is shipped with ice packs.
Purity: > 85 % as determined by reducing SDS-PAGE.
Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method
Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.
Molecular Mass: 51.2 kDa
Formulation: Lyophilized from sterile PBS, pH 7.4
Reconstitution: Please refer to the printed manual for detailed information.
Background: Endothelial cell-selective adhesion molecule (ESAM) is a member of JAM family of immunoglobulin superfamily and consists of one V-type and one C2-type immunoglobulin domain, as well as a hydrophobic signal sequence, a single transmembrane region, and a cytoplasmic domain. It is specifically expressed at endothelial tight junctions and on activated platelets. ESAM at endothelial tight junctions participates in the migration of neutrophils through the vessel wall, possibly by influencing endothelial cell contacts. The adaptor protein membrane-associated guanylate kinase MAGI-1 has been identified as an intracellular binding partner of ESAM. Previous studies have indicated that ESAM regulates angiogenesis in the primary tumor growth and endothelial permeability. It suggest that ESAM has a redundant functional role in physiological angiogenesis but serves a unique and essential role in pathological angiogenic processes such as tumor growth.
Research Area: N/A