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Human Ephrin-B1 / EFNB1 Protein (His & Fc Tag)

CFND,CFNS,EFB1,EFL3,Elk-L,EPLG2,LERK2

Catalog Number P10894-H03H
Organism Species Human
Host Human Cells
Synonyms CFND,CFNS,EFB1,EFL3,Elk-L,EPLG2,LERK2
Molecular Weight The recombinant human EFNB1/Fc chimera is a disulfide-linked homodimeric protein. The reduced monomer consists of 458 amino acids and predicts a molecular mass of 51.2 KDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of the protein is approximately 64 and 36 KDa due to glycosylation.
predicted N Leu 28
SDS-PAGE
Purity > (79.7+18.0) % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the human EFNB1 (NP_004420.1) extracellular domain (Met 1-Gly 232) was was fused with the C-terminal polyhistidine-tagged Fc region of human IgG1 at the C-terminus.
Bio-activity Measured by its binding ability in a functional ELISA . Immobilized mouse EphB3 at 2 μg/ml (100 μl/well) can bind human EFNB1 Fc chimera with a linear ranger of 1.56-25 ng/ml.
Research Area Neuroscience |Cell Type Marker in Neurodevelopment |Neuronal Cell Markers |Growth Cone
Formulation Lyophilized from sterile PBS, pH 7.4
1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background Ephrin-B1 also known as EFNB1, is a member of the ephrin family. The transmembrane- associated ephrin ligands and their Eph family of receptor tyrosine kinases are expressed by cells of the SVZ. Eph/ephrin interactions are implicated in axon guidance, neural crest cell migration, establishment of segmental boundaries, and formation of angiogenic capillary plexi. Eph receptors and ephrins are divided into two subclasses, A and B, based on binding specificities. Ephrin subclasses are further distinguished by their mode of attachment to the plasma membrane: ephrin-A ligands bind EphA receptors and are anchored to the plasma membrane via a glycosylphosphatidylinositol (GPI) linkage, whereas ephrin-B ligands bind EphB receptors and are anchored via a transmembrane domain. An exception is the EphA4 receptor, which binds both subclasses of ephrins. EphrinB1 and B class Eph receptors provide positional cues required for the normal morphogenesis of skeletal elements. Another malformation, preaxial polydactyly, was exclusively seen in heterozygous females in which expression of the X-linked ephrinB1 gene was mosaic, so that ectopic EphB-ephrinB1 interactions led to restricted cell movements and the bifurcation of digital rays.
Reference
  • Davy A, et al. (2004) Ephrin-B1 forward and reverse signaling are required during mouse development. Genes Dev. 18(5): 572-83.
  • Compagni A, et al. (2003) Control of skeletal patterning by ephrinB1-EphB interactions. Dev Cell. 5(2): 217-30.
  • Wieland I, et al. (2004) Mutations of the ephrin-B1 gene cause craniofrontonasal syndrome. Am J Hum Genet. 74(6): 1209-15.