Human ESAM

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Cat-Nr.300-057
Size20 µg
Price120 €
SourceE. coli
LabelHis-Tag
Formulationlyophilized
Purity Confirmation> 95% by SDS-PAGE
Molecular Weight27.8 kDa
Biological ActivityData not available.
Species ReactivityHuman
BufferPBS
ReconstitutionHuman ESAM should be reconstituted in sterile water to a concentration of 0.1 mg/ml. This solution can be diluted in water or other buffer solutions or stored at -20°C.
Stability and StorageThe lyophilized human ESAM, though stable at room temperature, is best stored desiccated below 0°C.
SynonymsESAM; W117m
DescriptionEndothelial cell selective adhesion molecule (ESAM) is a 55 kDa type I transmembrane glycoprotein that belongs to the JAM family of immunoglobulin superfamily molecules. Human ESAM is synthesized as a 390 amino acid (aa) protein composed of a 29 aa signal peptide, a 216 aa extracellular region, a putative 26 aa transmembrane segment, and a 119 aa cytoplasmic domain. The extracellular region contains one V-type and one C2-type Ig domain and is involved in hemophilic adhesion. In the cytoplasmic domain, there is a docking site for the multifunctional adaptor protein MAGI1. The extracellular region of human ESAM shows 90%, 74%, 69% and 67% aa identity with monkey, canine, mouse and rat extracellular ESAM, respectively. ESAM is expressed on endothelial cells, activated platelets and megakaryocytes, and can be found associated with cell to cell junctions. Whether ESAM is restricted to a particular junctional type is not clear. ESAM deficient mice have no defect in vascularization but do have reduced angiogenic potential. This may be due to a decreased migratory response to FGF2. Soluble ESAM is fused to a C-terminal His-tag (6x His).
Protein SequenceISLPGPLVTNLLRFLFLGLSALAPPSRAQLQLHLPANRLQAVEGGEVVLPAWYTLHGEVSSSQPWEVPFVMWFFKQKEKEDQVLSYINGVTTSKPGVSLVYSMPSRNLSLRLEGLQEKDSGPYSCSVNVQDKQGKSRGHSIKTLELNVLVPPAPPSCRLQGVPHVGANVTLSCQSPRSKPAVQYQWDRQLPSFQTFFAPALDVIRGSLSLTNLSSSMAGVYVCKAHNEVGTAQCNVTLEVSTGPGARSHHHHHH
Uniprot IDQ96AP7
Protein RefSeqNP_620411.2
mRNA RefSeqNM_138961.2

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