EphA2 recombinant protein

Recombinant Mouse EphA2 Protein (His tag)

Cat. Num. AAA2546896

• Gene Names: Epha2; Eck; Myk2; Sek2; Sek-2; AW545284
• Purity: > 98 % as determined by SDS-PAGE
• Synonyms: EphA2; Recombinant Mouse EphA2 Protein (His tag); RP23-308N2.1; AW545284; Eck; Myk2; Sek-2; Sek2; EphA2 recombinant protein

• Host: Human Cells
• Purity/Purification: > 98 % as determined by SDS-PAGE
• Form/Format: Lyophilized from sterile 20mM Tris, 150mM NaCl, pH 7.5
• Sequence Length: 977

• Application Notes: The secreted recombinant mouse EPHA2 consists of 523 amino acids and has a predicted molecular mass of 58 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rmEPHA2 is approximately 65 kDa due to glycosylation.
• Predicted N Terminal: Gln 24
• Endotoxin: < 1.0 EU per mug of the protein as determined by the LAL method
• Preparation and Storage: Samples are stable for up to twelve months from date of receipt at -70 degree C

Related Product Information for EphA2 recombinant protein

Background: Eph receptor A2 (Ephrin type -A receptor 2 or EphA2) is a member of the ephrin receptor subfamily of the protein-tyrosine kinase family. The Eph receptors' corresponding family of ligands are the ephrins anchored to cell surfaces. The ephrins and Eph receptors are implicated as positional labels that may guide the development of neural topographic maps. They have also been found implicated in embryonic patterning, neuronal targeting, vascular development and adult neovascularization. The large family of ligands and receptors may make a major contribution to the accurate spatial patterning of connections and cell position in the nervous system. Furthermore, elevated expression of Eph receptors and ephrin ligands is associated with tumors and associated tumor vasculature, suggesting the Eph receptors and ephrin ligands also play critical roles in tumor angiogenesis and tumor growth. Unlike most Eph kinases, which are primarily expressed during development, EphA2 is primarily found in adult human epithelial cells. The cellular functions of EphA2 may be regulating cell growth, survival, migration, and angiogenesis.Unlike other receptor tyrosine kinases, ligand binding is not necessary for EphA2. Rather, the ligand appears to regulate EphA2 subcellular localization and its interactions with downstream adapter and signaling proteins. Eph receptor A2 (EphA2) has been demonstrated to critically regulate tumor cell growth, migration and invasiveness. Eph receptor A2 (EphA2) is frequently overexpressed and functionally altered in aggressive tumor cells, and that these changes promote metastatic character.

Description: A DNA sequence encoding the mouse EPHA2 (NP_034269.2) extracellular domain (Met 1-Asn 535) was expressed, fused with a polyhistidine tag at the C-terminus.

NCBI and Uniprot Product Information

• NCBI GI #: 32484983
• NCBI GeneID: 13836
• NCBI Accession #: NP_034269.2
• NCBI GenBank Nucleotide #: NM_010139.3
• UniProt Accession #: Q03145; Q3UNI2; Q60633; Q62212
• Molecular Weight: 108,852 Da
• NCBI Official Full Name: ephrin type-A receptor 2
• NCBI Official Synonym Full Names: Eph receptor A2
• NCBI Official Symbol: Epha2
• NCBI Official Synonym Symbols: Eck; Myk2; Sek2; Sek-2; AW545284
• NCBI Protein Information: ephrin type-A receptor 2
• UniProt Protein Name: Ephrin type-A receptor 2
• Protein Family: Ephrin type-A receptor
• UniProt Gene Name: Epha2
• UniProt Synonym Gene Names: Eck; Myk2; Sek2

Uniprot Description

EphA2: a receptor tyrosine kinase. Receptor for members of the ephrin-A family. Binds to ephrin-A1, -A3, -A4 AND -A5. 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. Overexpressed in many cancers including aggressive ovarian, cervical and breast carcinomas, and lung cancer. Expression correlates with degree of angiogenesis, metastasis and xenograft tumor growth. Soluble receptor inhibits tumor growth and angiogenesis in mice.

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

Chromosomal Location of Human Ortholog: 4 D3|4 73.67 cM

Cellular Component: cell surface; cell-cell adherens junction; focal adhesion; integral to plasma membrane; lamellipodium; plasma membrane

Molecular Function: protein binding; transmembrane receptor protein tyrosine kinase activity

Biological Process: axial mesoderm formation; blood vessel development; blood vessel endothelial cell proliferation during sprouting angiogenesis; blood vessel morphogenesis; bone remodeling; cAMP metabolic process; cell migration; cell motility involved in cell locomotion; defense response to Gram-positive bacterium; DNA damage response, signal transduction resulting in induction of apoptosis; ephrin receptor signaling pathway; inflammatory response; keratinocyte differentiation; mammary gland epithelial cell proliferation; negative regulation of angiogenesis; negative regulation of chemokine production; negative regulation of cytokine production; negative regulation of protein kinase B signaling cascade; neural tube development; neuron differentiation; notochord cell development; notochord formation; notochord morphogenesis; osteoblast differentiation; osteoclast differentiation; protein kinase B signaling cascade; regulation of angiogenesis; regulation of blood vessel endothelial cell migration; regulation of cell adhesion mediated by integrin; skeletal development; vasculogenesis