Cat-Nr.S01-068SSize10 µgPrice90 €SourceE. coliLabelHis-TagFormulationlyophilizedPurity Confirmation> 95% by SDS-PAGELength [aa]211Molecular Weight23.4 kDaN Terminal SequenceMIVLESpecies ReactivityHumanSynonymsEPH-related receptor tyrosine kinase ligand 5; HTK ligand; DescriptionThe large families of Eph receptor tyrosine kinases and their Ephrin ligands transduce signals in a cell-cell contact-dependent fashion. They thereby coordinate the growth, differentiation, and patterning of almost every organ and tissue. Eph/Ephrin interactions can trigger a wide array of cellular responses, including cell adhesion, boundary formation, and repulsion. The exact mechanisms leading to this diversity of responses are unclear but appear to involve differential signaling, proteolytic cleavage of Ephrins, and endocytosis of the ligand-receptor complex. In the developing cardiovascular system, Eph and Ephrin molecules control the angiogenic remodeling of blood vessels and lymphatic vessels and play essential roles in endothelial cells as well as in supporting pericytes and vascular smooth muscle cells. Recent evidence suggests that Ephs and Ephrins may also be involved in pathological angiogenesis, in particular, the neovascularization of tumors. Consequently, the expression, interactions, or signaling of Eph/Ephrin molecules might be targets for future therapeutic approaches. Ephrins are naturally divided into two structural groups. All ligands share a conserved extracellular sequence, which most likely corresponds to the receptor-binding domain. This conserved sequence consists of approximately 125 amino acids and includes four invariant cysteines. The B-class ligands are transmembrane proteins, which can be tyrosine phosphorylated upon receptor ligation. Class B ephrins show 33% amino acid sequence identity in their extracellular segments and 44% amino acid sequence identity in their cytoplasmic regions.Protein SequenceMIVLEPIYWNSSNSKFLPGQGLVLYPQIGDKLDIICPKVDSKTVGQYEYYKVYMVDKDQADRCTIKKENTPLLNCAKPDQDIKFTIKFQEFSPNLWGLEFQKNKDYYIISTSNGSLEGLDNQEGGVCQTRAMKILMKVGQDASSAGSTRNKDPTRRPELEAGTNGRSSTTSPFVKPNPGSSTDGNSAGHSGNNILGSEVALFALEHHHHHHUniprot IDP52799Protein RefSeqNP_004084.1mRNA RefSeqNM_004093.3
Receptor Ligand Technologies GmbH 公司（RELIA Tech ）位于德国不伦瑞克，是一家后基因组生物技术公司，该公司运用独特的技术专注于受体和配体的发现与研究，从而使商业化，产品广泛使用于科学研究，实验诊断和临床应用。瑞莱技术的灵活性和竞争力必将使其在这个快速整合的功能基因组学和蛋白组学的新时代发展壮大.RELIA公司提供的细胞因子，生长因子，重组蛋白产品一致内毒素检测项目，且内毒素水平非常低。
受体配体技术有限公司（RELIATech）是一家后基因组生物技术公司，致力于在配体与受体相互作用领域的新技术和新产品的发现和商业化，用于研究，诊断和临床领域。该公司位于德国不伦瑞克，由以下公司成立于2000年10月：
阿夫纳·亚永教授
以色列魏兹曼科学研究所（WIS）
赫伯特·韦奇博士
德国生物技术德国研究中心（GBF）
Bernhard Barleon博士
德国肿瘤生物学诊所（KTB）
创始人是从事细胞生长因子相互作用，酪氨酸激酶及其信号传导途径（涉及组织重塑，体内平衡和疾病）领域的细胞和分子生物学家，工作时间超过10年。特别是Herbert A. Weich博士和Bernhard Barleon博士从事血管生成，肿瘤血管生成和实体瘤进展领域的基础研究。
诸如“生长因子和细胞因子”之类的信号蛋白，连同其跨膜/“可溶性受体”和相关的激酶，在生理和病理生理条件下都作为关键的调节分子参与了所有高级生物的发育和功能。这些多肽调节细胞分化，组织重塑和体内平衡，并在各种疾病状态下被失调。由人类基因组计划编码新信号蛋白的新生长调节基因的发现，以及对它们功能的阐明，无疑将是未来十年的主要挑战之一。
RELIATech的使命是开发和商品化在“受体和配体相互作用”领域中有用的新产品，用于基础研究，药物开发和临床社区。RELIATech的灵活性和能力必将使其在功能基因组学和蛋白质组学的新时代迅速整合和扩展。
