Epha1 blocking peptide

Epha1 Blocking Peptide (Center)

• Gene Names: Epha1; Eph; Esk; AL033318; 5730453L17Rik
• Synonyms: Epha1; Epha1 Blocking Peptide (Center); Ephrin type-A receptor 1; mEpha1; Embryonic stem cell kinase; Tyrosine-protein kinase receptor ESK; Esk; Epha1 blocking peptide

• Specificity: The synthetic peptide sequence is selected from aa 453-467 of HUMAN Epha1
• Form/Format: Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.
• Sequence Length: 977

• Cellular Location: Cell membrane; Single-pass type I membrane protein
• Tissue Location: Preferentially expressed in epithelial cells including skin, kidney, liver and thymus
• Preparation and Storage: Maintain refrigerated at 2-8 degree C for up to 6 months. For long term storage store at -20 degree C.

Related Product Information for Epha1 blocking peptide

Receptor 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. Binds with a low affinity EFNA3 and EFNA4 and with a high affinity to EFNA1 which most probably constitutes its cognate/functional ligand. Upon activation by EFNA1 induces cell attachment to the extracellular matrix inhibiting cell spreading and motility through regulation of ILK and downstream RHOA and RAC. Plays also a role in angiogenesis and regulates cell proliferation. May play a role in apoptosis.

NCBI and Uniprot Product Information

• NCBI GI #: 47117897
• NCBI GeneID: 13835
• UniProt Accession #: Q60750; Q8CED9; Q9ESJ2
• Molecular Weight: 108,578 Da
• NCBI Official Full Name: Ephrin type-A receptor 1
• NCBI Official Synonym Full Names: Eph receptor A1
• NCBI Official Symbol: Epha1
• NCBI Official Synonym Symbols: Eph; Esk; AL033318; 5730453L17Rik
• NCBI Protein Information: ephrin type-A receptor 1
• UniProt Protein Name: Ephrin type-A receptor 1
• Protein Family: Ephrin type-A receptor
• UniProt Gene Name: Epha1
• UniProt Synonym Gene Names: Esk; mEpha1
• UniProt Entry Name: EPHA1_MOUSE

Uniprot Description

EphA1: a receptor tyrosine kinase. Receptor for members of the ephrin-A family. Binds with a low affinity to ephrin-A1. The Eph receptor tyrosine kinase family, the largest in the tyrosine kinase group, has fourteen members. They bind membrane-anchored ligands, ephrins, at sites of cell-cell contact, regulating the repulsion and adhesion of cells that underlie the establishment, maintenance, and remodeling of patterns of cellular organization. Eph signals are particularly important in regulating cell adhesion and cell migration during development, axon guidance, homeostasis and disease. EphA receptors bind to GPI-anchored ephrin-A ligands, while EphB receptors bind to ephrin-B proteins that have a transmembrane and cytoplasmic domain. Interactions between EphB receptor kinases and ephrin-B proteins transduce signals bidirectionally, signaling to both interacting cell types. Eph receptors and ephrins also regulate the adhesion of endothelial cells and are required for the remodeling of blood vessels. Misexpressed in several cancers, including upregulation in head and neck cancer, and downregulation in invasive breast cancer cell lines and glioblastoma

Protein type: Membrane protein, integral; EC 2.7.10.1; Kinase, protein; Protein kinase, tyrosine (receptor); Protein kinase, TK; TK group; Eph family

Cellular Component: integral to plasma membrane

Molecular Function: protein kinase activity; protein kinase binding; transmembrane-ephrin receptor activity

Biological Process: cell surface receptor linked signal transduction; negative regulation of cell migration; negative regulation of protein kinase activity; peptidyl-tyrosine phosphorylation; positive regulation of angiogenesis; positive regulation of cell migration; positive regulation of cell proliferation; positive regulation of cell-matrix adhesion; positive regulation of stress fiber formation; protein amino acid autophosphorylation; regulation of GTPase activity