产品名称
Anti-Ephrin-B2 antibody ,Mouse monoclonal, clone EFR-163M, purified from hybridoma cell culture
biological source
mouse
conjugate
unconjugated
antibody form
purified from hybridoma cell culture
antibody product type
primary antibodies
clone
EFR-163M, monoclonal
form
buffered aqueous solution
mol wt
antigen ~56 kDa
species reactivity
human
concentration
~1.0 mg/mL
technique(s)
western blot: 0.5-1.0 μg/mL using whole extracts of HEK-293T cells overexpressing a human Ephrin-B2 fusion protein
isotype
IgG1
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... EFNB2(1948)
Application
Anti-Ephrin-B2 antibody may be used for immunoblotting at a working concentration of 0.5-1.0 μg/ml using whole cell lysates of HEK-293T cells over-expressing human Ephrin-B2. It is also suitable for immunohistochemistry of formalin-fixed, paraffin-embedded human skin sections.
Biochem/physiol Actions
Ephrin-B2 and EphB4 are essential for proper development of the cardiovascular system. It is implicated in regulating erythropoiesis. Mutations in these genes are linked to embryonic lethality, defects in the angiogenic remodeling of the peripheral vasculature and defective myocardial trabeculation in the heart.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
General description
Eph family of tyrosine kinase receptors mediates cell-cell attachment and aggregation by binding to specific ligands, ephrins. The Eph family consists of 14 structurally related receptors that are either membrane linked or are transmembrane with overlapping affinity for ligands. The transmembrane receptor Ephrin-B2 signals through its cognate receptor EphB4. The signalling via EphB4 receptor ensures is crucial in the initial stages of vasculogenesis in marking specific arterial and venous domains. Ephrin-B2 is also essential in the development stages for neural crest formation, angiogenesis, vascular cell assembly, migration and synapse development in central nervous system
Anti-Ephrin-B2 recognizes human Ephrin-B2 protein (~56 kDa).
Anti-Ephrin-B2 recognizes human Ephrin-B2 protein (~56 kDa).
Ephrin-B2 is a member of the ephrin-B (EPH) family. The ephrins and EPH-related receptors comprise the largest subfamily of receptor protein-tyrosine kinases. Ephrins are divided into ephrin-A (EFNA) class, which are anchored to the membrane by a glycosylphosphatidylinositol linkage and the ephrin-B (EFNB) class, which are transmembrane proteins. Ephrin-B2 binds the tyrosine kinase receptors EphB4 and EphA3 and is expressed by arteries whereas its receptor tyrosine kinase EphB4 is expressed by veins.
Immunogen
human Ephrin-B2 recombinant protein. The human protein shares 97% homology with the mouse protein.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
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存储类别
10 - Combustible liquids
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
新产品
此项目有
Functions of ephrin/Eph interactions in the development of the nervous system: emphasis on the hippocampal system
Martinez A and Soriano E
Brain Research Reviews, 49(2), 211-226 (2005)
Ephrin-B2 is a candidate ligand for the Eph receptor, EphB6
Munthe E, et al.
Febs Letters, 466(1), 169-174 (2000)
Regulation of angiogenesis by Eph-ephrin interactions
Kuijper S, et al.
Trends in Cardiovascular Medicine, 17(5), 145-151 (2007)
A role of EphB4 receptor and its ligand, ephrin-B2, in erythropoiesis
Suenobu S, et al.
Biochemical and Biophysical Research Communications, 293(3), 1124-1131 (2002)
Regulation of vasculogenesis and angiogenesis by EphB/ephrin-B2 signaling between endothelial cells and surrounding mesenchymal cells
Oike Y, et al.
Blood, 100(4), 1326-1333 (2002)
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