Description
Recombinant Human Ephrin-A1/EFNA1 Protein (Fc Tag)(Active) | PKSH032389 | Gentaur US, UK & Europe Disrtribition
Synonyms: Ephrin-A1; EPH-Related Receptor Tyrosine Kinase Ligand 1; LERK-1; Immediate Early Response Protein B61; Tumor Necrosis Factor Alpha-Induced Protein 4; TNF Alpha-Induced Protein 4; EFNA1; EPLG1; LERK1; TNFAIP4
Active Protein: Active protein
Activity: Recombinant Human Ephrin-A1 is produced by our Mammalian expression system and the target gene encoding Asp19-Ser182 is expressed with a Fc tag at the C-terminus.
Protein Construction: Recombinant Human Ephrin-A1 is produced by our Mammalian expression system and the target gene encoding Asp19-Ser182 is expressed with a Fc tag at the C-terminus.
Fusion Tag: C-Fc
Species: Human
Expressed Host: Human Cells
Shipping: This product is provided as lyophilized powder which is shipped with ice packs.
Purity: > 95 % as determined by reducing SDS-PAGE.
Endotoxin: < 1.0 EU per µg 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: 46.5 kDa
Formulation: Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.
Reconstitution: Please refer to the printed manual for detailed information.
Background: Ephrin-A1 is a member of the A-type ephrin family of cell surface proteins that function as ligands for the A-type Eph receptor tyrosine kinase family. Ephrin-A1 can be induced by TNF and IL1B. Its expression levels can be down-regulated in primary glioma tissues compared to the normal tissues. The soluble monomeric form is expressed in the glioblastoma multiforme (GBM) and breast cancer cells. Soluble Ephrin-A1 is necessary for the transformation of HeLa and SK-BR3 cells and participates in the relocalization of EPHA2 away from sites of cell-cell contact during transformation. Ephrin-A1 plays an important role in angiogenesis and tumor neovascularization.
Research Area: Signal Transduction, Cardiovascular, Neuroscience,