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Mouse Ephrin-B2 Recombinant Protein C-Fc-6 His Tag Lyophilized
Mouse Ephrin-B2 Recombinant Protein C-Fc-6 His Tag Lyophilized
SKU:IMSEPHB2RCFC6HISLY50UG
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Key facts
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Mouse Ephrin-B2 Recombinant Protein C-Fc-6 His Tag Lyophilized from Innovative Research has been recombinantly produced in Human Cells. This is a Lyophilized protein buffered in Lyophilized from a 0.2 um filtered solution of PBS,pH7.4. It is not recommended to reconstitute to a concentration less than 100UG/ml. Dissolve the lyophilized protein in ddH2O. with a purity of Greater than 95% as determined by reducing SDS-PAGE.Endotoxin level less than 0.1 ng/ug (1 IEU/ug) as determined by LAL test..More Details: Species: Mouse Target: Efnb2 Purity: Greater than 95% as determined by reducing SDS-PAGE.Endotoxin level less than 0.1 ng/ug (1 IEU/ug) as determined by LAL test. Source: Human Cells Storage Conditions: Lyophilized protein should be stored at -20░C, though stable at room temperature for 3 weeks.Reconstituted protein solution can be stored at 4-7░C for 2-7 days.Aliquots of reconstituted samples are stable at -20░C for 3 months.
Additional Information:
Ephrin-B2 is a single-pass type I membrane protein and it contains 1 ephrin RBD (ephrin receptor-binding) domain. Ephrin-B2 belongs to the ephrin (EPH) family and it is 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. The ephrins and EPH-related receptors contain the largest subfamily of receptor protein-tyrosine kinases and have been associated with mediating developmental events, particularly in the nervous system and in erythropoiesis. Based upon their structures and sequence relationships, ephrins are allocated into the ephrin-A (EFNA) class, which are anchored to the membrane by a glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB) class, which are transmembrane proteins. It also binds to receptor tyrosine kinase including EPHA4, EPHA3 and EPHB4 and together with EPHB4 plays a central role in heart morphogenesis and angiogenesis through regulation of cell adhesion and cell migration.This recombinant protein can be used for biological assays. For research use only. . At Innovative Research we provide reliable, consistent products that deliver reliable, consistent results.In-depth information
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Additional Information:
Ephrin-B2 is a single-pass type I membrane protein and it contains 1 ephrin RBD (ephrin receptor-binding) domain. Ephrin-B2 belongs to the ephrin (EPH) family and it is 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. The ephrins and EPH-related receptors contain the largest subfamily of receptor protein-tyrosine kinases and have been associated with mediating developmental events, particularly in the nervous system and in erythropoiesis. Based upon their structures and sequence relationships, ephrins are allocated into the ephrin-A (EFNA) class, which are anchored to the membrane by a glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB) class, which are transmembrane proteins. It also binds to receptor tyrosine kinase including EPHA4, EPHA3 and EPHB4 and together with EPHB4 plays a central role in heart morphogenesis and angiogenesis through regulation of cell adhesion and cell migration.This recombinant protein can be used for biological assays. For research use only. . At Innovative Research we provide reliable, consistent products that deliver reliable, consistent results.This material is sold for in-vitro use only for manufacturing and research. This material is not suitable for human or animal use. While we make every effort to ensure the safety of our products, we recommend handling any biological materials with standard precautions as if capable of spreading infectious disease. The statements herin are offered for informational purposes only to be used solely for your consideration, investigation, and verification.
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