E9277
EphB1/Fc Chimera from rat
>95% (SDS-PAGE), recombinant, expressed in NSO cells, lyophilized powder
Synonym(s):
Cek6, Elk, Hek6, Net
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About This Item
MDL number:
UNSPSC Code:
51111800
biological source
rat
recombinant
expressed in NSO cells
assay
>95% (SDS-PAGE)
form
lyophilized powder
mol wt
monomer calculated mol wt 85.6 kDa
~110 kDa by SDS-PAGE (reducing)
packaging
pkg of 200 μg
storage condition
avoid repeated freeze/thaw cycles (Do not store in a frost-free freezer.)
technique(s)
ligand binding assay: suitable
impurities
endotoxin, tested
UniProt accession no.
storage temp.
−20°C
Gene Information
rat ... Ephb1(24338)
General description
Ephb1 (Epherin receptor B1) is a receptor tyrosine kinase (RTK), which is a part of the Eph family. It has a leader sequence at its N-terminal, an extracellular domain rich in cysteine, a transmembrane region, a tyrosine kinase domain in its cytoplasmic region and a C-terminal tail. In rats, its expression is exclusive to brain and testis, with higher expression in brain.[1]
Application
EphB1/Fc Chimera from rat has been used for the investigation of the role of ephrinB-EphB signaling in the induction and maintenance of hyperalgesia, hyperexcitability of neurons of DRG (dorsal root ganglion) and hyperexcitability and elevated synaptic plasticity of neurons of DH (dorsal horn) regions of brain.[2]
Biochem/physiol Actions
Ephb1 (Epherin receptor B1) signaling is essential for cell assembly and attachment, mediated through αvβ3 and α5β integrins.[3] It prevents the mixing of second and third neural crest, and is essential for the correct guiding of third neural crest.[4] In retina, it is involved in the formation of ipsilateral projections and axon divergence.[5] It also acts as an activator of c-Jun Kinase (JNK) signaling, through its interaction with the adaptor protein Nck (non-catalytic region of tyrosine kinase).[6]
Member of Eph receptor tyrosine kinase family shown to bind ephrin-A1, ephrin-A3, ephrin-A4, ephrin-B1, ephrin-B2, and ephrin-B3; involved in pattern formation and morphogenesis. EphB1 can be detected in endothelial cells and is activated by ephrin-B1, initiating the assembly of endothelial cells into capillary-like cords.
Other Notes
Extracellular domain of rat EphB1 (amino acids 18-538) fused to the C-terminal 6X histidine-tagged Fc region of human IgG1 via a polypeptide linker.
Physical form
Lyophilized from a 0.2 μm filtered solution in 20 mM Tris, pH 8.5.
Analysis Note
The biological activity is measured by its ability to bind recombinant mouse ephrin-B1/Fc in an ELISA assay.
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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A Smith et al.
Current biology : CB, 7(8), 561-570 (1997-08-01)
During vertebrate head development, neural crest cells migrate from hindbrain segments to specific branchial arches, where they differentiate into distinct patterns of skeletal structures. The rostrocaudal identity of branchial neural crest cells appears to be specified prior to migration, so
U Huynh-Do et al.
The EMBO journal, 18(8), 2165-2173 (1999-04-16)
Receptors of the Eph family and their ligands (ephrins) mediate developmental vascular assembly and direct axonal guidance. Migrating cell processes identify appropriate targets within migratory fields based on topographically displayed ephrin gradients. Here, EphB1 regulated cell attachment by discriminating the
E Stein et al.
The Journal of biological chemistry, 273(3), 1303-1308 (1998-01-27)
Eph family receptor tyrosine kinases signal axonal guidance, neuronal bundling, and angiogenesis; yet the signaling systems that couple these receptors to targeting and cell-cell assembly responses are incompletely defined. Functional links to regulators of cytoskeletal structure are anticipated based on
Xue-Jun Song et al.
Pain, 139(1), 168-180 (2008-05-02)
Bidirectional signaling between ephrins and Eph receptor tyrosine kinases was first found to play important roles during development, but recently has been implicated in synaptic plasticity and pain processing in the matured nervous system. We show that ephrinB-EphB receptor signaling
V Lhoták et al.
Molecular and cellular biology, 11(5), 2496-2502 (1991-05-01)
The elk gene encodes a novel receptorlike protein-tyrosine kinase, which belongs to the eph subfamily. We have previously identified a partial cDNA encompassing the elk catalytic domain (K. Letwin, S.-P. Yee, and T. Pawson, Oncogene 3:621-678, 1988). Using this cDNA
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