Cynomolgus EPHA2 Protein 2978

Additional Information:
accession Q1KL86|express systemHEK293|product tagC-His-Avi|purity> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC|backgroundEphrin type-A receptor 2 (EPHA2) is a receptor tyrosine kinase (RTK), whose over-expression has been observed in a variety of cancers, including breast cancer. EPHA2 expression may be causally related to tumorigenesis; therefore, it is important to understand how EPHA2 gene (EPHA2) expression is regulated.|molecular weightThe protein has a predicted MW of 59.2 kDa. Due to glycosylation, the protein migrates to 60-70 kDa based on Tris-Bis PAGE result.|available size100 g, 500 g|endotoxinLess than 1EU per g by the LAL method.|Cynomolgus EPHA2 Protein 2978proteinSize and concentration100, 500g and lyophilizedFormLyophilizedStorage InstructionsValid for 12 months from date of receipt when stored at -80C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.Storage bufferShipped at ambient temperature.Purity> 95% as determined by Tris-Bis PAGEtarget relevanceEphrin type-A receptor 2 (EPHA2) is a receptor tyrosine kinase (RTK), whose over-expression has been observed in a variety of cancers, including breast cancer. EPHA2 expression may be causally related to tumorigenesis; therefore, it is important to understand how EPHA2 gene (EPHA2) expression is regulated.Protein namesEphrin type-A receptor 2 (EC 2.7.10.1)Gene namesEPHA2,EPHA2Protein familyProtein kinase superfamily, Tyr protein kinase family, Ephrin receptor subfamilyMass9541DaFunctionReceptor tyrosine kinase which binds promiscuously membrane-bound ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Activated by the ligand ephrin-A1/EFNA1 regulates migration, integrin-mediated adhesion, proliferation and differentiation of cells. Regulates cell adhesion and differentiation through DSG1/desmoglein-1 and inhibition of the ERK1/ERK2 signaling pathway. May also participate in UV radiation-induced apoptosis and have a ligand-independent stimulatory effect on chemotactic cell migration. During development, may function in distinctive aspects of pattern formation and subsequently in development of several fetal tissues. Involved for instance in angiogenesis, in early hindbrain development and epithelial proliferation and branching morphogenesis during mammary gland development. Engaged by the ligand ephrin-A5/EFNA5 may regulate lens fiber cells shape and interactions and be important for lens transparency development and maintenance. With ephrin-A2/EFNA2 may play a role in bone remodeling through regulation of osteoclastogenesis and osteoblastogenesis (By similarity).Catalytic activityBINDING 619..627; /ligand=”ATP”; /ligand_id=”ChEBI:CHEBI:30616″; /evidence=”ECO:0000255|PROSITE-ProRule:PRU00159″; BINDING 646; /ligand=”ATP”; /ligand_id=”ChEBI:CHEBI:30616″; /evidence=”ECO:0000255|PROSITE-ProRule:PRU00159″Subellular locationCell membrane ; Single-pass type I membrane protein. Cell projection, ruffle membrane ; Single-pass type I membrane protein. Cell projection, lamellipodium membrane ; Single-pass type I membrane protein. Cell junction, focal adhesion. Note=Present at regions of cell-cell contacts but also at the leading edge of migrating cells. Relocates from the plasma membrane to the cytoplasmic and perinuclear regions in cancer cells.StructureHomodimer. Interacts with SLA. Interacts (phosphorylated form) with VAV2, VAV3 and PI3-kinase p85 subunit (PIK3R1, PIK3R2 or PIK3R3); critical for the EFNA1-induced activation of RAC1 which stimulates cell migration. Interacts with INPPL1; regulates activated EPHA2 endocytosis and degradation. Interacts (inactivated form) with PTK2/FAK1 and interacts (EFNA1 ligand-activated form) with PTPN11; regulates integrin-mediated adhesion. Interacts with ARHGEF16, DOCK4 and ELMO2; mediates ligand-independent activation of RAC1 which stimulates cell migration. Interacts with CLDN4; phosphorylates CLDN4 and may regulate tight junctions. Interacts with ACP1. Interacts with ANKS1A. Interacts with CEMIP. Interacts with NCK1; may regulate EPHA2 activity in cell migration and adhesion.Interacts with TIMD4 (By similarity).Post-translational modificationAutophosphorylates. Phosphorylated on tyrosine upon binding and activation by EFNA1. Phosphorylated residues Tyr-588 and Tyr-594 are required for binding VAV2 and VAV3 while phosphorylated residues Tyr-735 and Tyr-930 are required for binding PI3-kinase p85 subunit (PIK3R1, PIK3R2 or PIK3R3). These phosphorylated residues are critical for recruitment of VAV2 and VAV3 and PI3-kinase p85 subunit which transduce downstream signaling to activate RAC1 GTPase and cell migration. Dephosphorylation of Tyr-930 by PTPRF prevents the interaction of EPHA2 with NCK1. Phosphorylated at Ser-897 by PKB; serum-induced phosphorylation which targets EPHA2 to the cell leading edge and stimulates cell migration. Phosphorylation by PKB is inhibited by EFNA1-activated EPHA2 which regulates PKB activity via a reciprocal regulatory loop. Phosphorylated at Ser-897 in response to TNF by RPS6KA1 and RPS6KA3; RPS6KA-EPHA2 signaling pathway controls cell migration. Phosphorylated at Ser-897 by PKA; blocks cell retraction induced by EPHA2 kinase activity. Dephosphorylated by ACP1.; Ubiquitinated by CHIP/STUB1. Ubiquitination is regulated by the HSP90 chaperone and regulates the receptor stability and activity through proteasomal degradation. ANKS1A prevents ubiquitination and degradation (By similarity).Target Relevance information above includes information from UniProt accession: Q1KL86The UniProt Consortium|