EPHB4 Human
Sf9, Baculovirus cells.
Tyrosine-Protein Kinase TYRO11, Hepatoma Transmembrane Kinase, TYRO11, MYK1, HTK, Ephrin Type-B Receptor, Tyrosine-Protein Kinase Receptor HTK.
Greater than 90.0% as determined by SDS-PAGE.
Description
EPHB4 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (16-539a.a.) and fused to an 8 aa His Tag at C-terminus containing a total of 532 amino acids and having a molecular mass of 58.1 kDa. EPHB4 shows multiple bands between 50-70kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.
Product Specs
Ephrin type-B receptor 4, also known as EPHB4, is a protein encoded by the EPHB4 gene in humans. This receptor and its corresponding ligands, ephrins, are involved in various developmental processes, particularly in the nervous system. Being the largest subgroup of receptor tyrosine kinases (RTKs), EPHB4 and other Ephrin receptors play a crucial role in cell signaling. Specifically, EPHB4 binds to ephrin B2 and is essential for the proper development of the vascular system.
Produced in Sf9 insect cells using a baculovirus expression system, the recombinant EPHB4 protein consists of amino acids 16-539 of the human EPHB4 protein sequence (accession number: a.a.). It is a single, glycosylated polypeptide chain with an 8 amino acid Histidine tag fused at the C-terminus, resulting in a total of 532 amino acids and a molecular weight of 58.1 kDa. Under reducing conditions on SDS-PAGE, EPHB4 appears as multiple bands between 50-70 kDa due to glycosylation. The protein has been purified using proprietary chromatographic techniques.
The EPHB4 protein is supplied as a solution at a concentration of 0.25 mg/ml in a buffer consisting of Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
The purity of the EPHB4 protein is greater than 90.0% as determined by SDS-PAGE analysis.
Tyrosine-Protein Kinase TYRO11, Hepatoma Transmembrane Kinase, TYRO11, MYK1, HTK, Ephrin Type-B Receptor, Tyrosine-Protein Kinase Receptor HTK.
Sf9, Baculovirus cells.
LEETLLNTKL ETADLKWVTF PQVDGQWEEL SGLDEEQHSV RTYEVCDVQR APGQAHWLRT GWVPRRGAVH VYATLRFTML ECLSLPRAGRSCKETFTVFY YESDADTATA LTPAWMENPY IKVDTVAAEH LTRKRPGAEA TGKVNVKTLR LGPLSKAGFY LAFQDQGACM ALLSLHLFYK KCAQLTVNLT RFPETVPREL VVPVAGSCVV DAVPAPGPSP SLYCREDGQW AEQPVTGCSC APGFEAAEGN TKCRACAQGT FKPLSGEGSC QPCPANSHSN TIGSAVCQCR VGYFRARTDP RGAPCTTPPS APRSVVSRLN GSSLHLEWSA PLESGGREDL TYALRCRECR PGGSCAPCGG DLTFDPGPRD LVEPWVVVRG LRPDFTYTFE VTALNGVSSL ATGPVPFEPV NVTTDREVPP AVSDIRVTRS SPSSLSLAWA VPRAPSGAVL DYEVKYHEKG AEGPSSVRFL KTSENRAELR GLKRGASYLV QVRARSEAGY GPFGQEHHSQ TQLDESEGWR EQLAVEHHHH HH.
Product Science Overview
Mutations or dysregulation of EPHB4 have been associated with various diseases, including:
- Lymphatic Malformation 7: A disorder characterized by abnormal lymphatic vessel development.
- Capillary Malformation-Arteriovenous Malformation 2: A condition involving abnormal blood vessel formation .
EPHB4 is also implicated in cancer, where it can influence tumor growth, invasion, and metastasis .
