Human Ephrin-B1/EFNB1 protein (Recombinant) (C-hFc&His) (STJP001018)
SPECIFICATIONS
HostHEK293 cells
ConjugationUnconjugated
ImmunogenRecombinant Human Ephrin-B1/EFNB1 Protein is produced by HEK293 expression system. The target protein is expressed with sequence (Leu 28-Gly 232 ) of human Ephrin-B1 (Accession #NP_004420.1) fused with an Fc, 6×His tag at the C-terminus.
General Information
| Short Description | Recombinant-Human Ephrin-B1/EFNB1-C-hFc&His protein was developed in hek293 cells using the region Leu 28-Gly 232. For use in research applications. |
| Host | HEK293 cells |
| Note | STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS. |
Product Properties
| Conjugation | Unconjugated |
| Formulation | Lyophilised from a 0.22 Mu m filtered solution of PBS, pH 7.4. |
| Storage Instruction | Store at-20°C for up to 1 year from the date of receipt, and avoid repeat freeze-thaw cycles. |
| Immunoreactivity | Measured by its binding ability in a functional ELISA. Immobilized Mouse EphB2 at 2 Mu g/mL (100 Mu L/well) can bind Human EFNB1 with a linear range of 0.01-0.54 ng/mL. |
| Determination Method | < 0.01 EU/Mu g of the protein by LAL method. |
Target Information
| Gene Symbol | EFNB1 |
| Gene ID | 1947 |
| Uniprot ID | EFNB1_HUMAN |
| Immunogen | Recombinant Human Ephrin-B1/EFNB1 Protein is produced by HEK293 expression system. The target protein is expressed with sequence (Leu 28-Gly 232 ) of human Ephrin-B1 (Accession #NP_004420.1) fused with an Fc, 6×His tag at the C-terminus. |
| Immunogen Region | Leu 28-Gly 232 |
| Immunogen Sequence | LAKNLEPVSWSSLNPKFLSG KGLVIYPKIGDKLDIICPRA EAGRPYEYYKLYLVRPEQAA ACSTVLDPNVLVTCNRPEQE IRFTIKFQEFSPNYMGLEFK KHHDYYITSTSNGSLEGLEN REGGVCRTRTMKIIMKVGQD PNAVTPEQLTTSRPSKEADN TVKMATQAPGSRGSLGDSDG KHETVNQEEKSGPGASGGSS GDPDG |
Additional Info
| Tissue Specificity | Widely expressed. Detected in both neuronal and non-neuronal tissues. Seems to have particularly strong expression in retina, sciatic nerve, heart and spinal cord. |
| Post Translational Modifications | Inducible phosphorylation of tyrosine residues in the cytoplasmic domain. Proteolytically processed. The ectodomain is cleaved, probably by a metalloprotease, to produce a membrane-tethered C-terminal fragment. This fragment is then further processed by the gamma-secretase complex to yield a soluble intracellular domain peptide which can translocate to the nucleus. The intracellular domain peptide is highly labile suggesting that it is targeted for degradation by the proteasome. |
| Function | Cell surface transmembrane ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binding to Eph receptors residing on adjacent cells leads to contact-dependent bidirectional signaling into neighboring cells. Shows high affinity for the receptor tyrosine kinase EPHB1/ELK. Can also bind EPHB2 and EPHB3. Binds to, and induces collapse of, commissural axons/growth cones in vitro. May play a role in constraining the orientation of longitudinally projecting axons. |
| Protein Name | Ephrin-B1Efl-3Elk LigandElk-LEph-Related Receptor Tyrosine Kinase Ligand 2Lerk-2 Cleaved Into - Ephrin-B1 C-Terminal FragmentEphrin-B1 Ctf - Ephrin-B1 Intracellular DomainEphrin-B1 Icd |
| Database Links | Reactome: R-HSA-2682334Reactome: R-HSA-3928662Reactome: R-HSA-3928664Reactome: R-HSA-3928665 |
| Cellular Localisation | Cell MembraneSingle-Pass Type I Membrane ProteinMembrane RaftMay Recruit Grip1 And Grip2 To Membrane Raft DomainsEphrin-B1 C-Terminal Fragment: Cell MembraneEphrin-B1 Intracellular Domain: NucleusColocalizes With Zhx2 In The Nucleus |
| Alternative Protein Names | Ephrin-B1 proteinEfl-3 proteinElk Ligand proteinElk-L proteinEph-Related Receptor Tyrosine Kinase Ligand 2 proteinLerk-2 Cleaved Into - Ephrin-B1 C-Terminal Fragment proteinEphrin-B1 Ctf - Ephrin-B1 Intracellular Domain proteinEphrin-B1 Icd proteinEFNB1 proteinEFL3 proteinEPLG2 proteinLERK2 protein |
Information sourced from Uniprot.org