EphB1 Protein, Mouse, Recombinant (His Tag)

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EphB1 Protein, Mouse, Recombinant (His Tag): Product Information

Purity
> 98 % as determined by SDS-PAGE
Endotoxin
< 1.0 EU per μg of the protein as determined by the LAL method
Activity
Immobilized mouse EPHB1-His at 10 μg/ml (100 μl/well) can bind mouse EFNB1-Fc (Cat:50580-M02H), The EC50 of mouse EFNB1-Fc (Cat:50580-M02H) is 0.04-0.08 μg/ml.
Protein Construction
A DNA sequence encoding the mouse EPHB1 (Q8CBF3-1) extracellular domain (Met 1-Leu 539) was expressed, with a polyhistidine tag at the C-terminus.
Accession#
Expressed Host
HEK293 Cells
Species
Mouse
Predicted N Terminal
Met 18
Molecule Mass
The secreted recombinant mouse EPHB1 consists of 533 amino acids and has a predicted molecular mass of 59.6 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rm EPHB1 is approximately 64 kDa due to glycosylation.
Formulation
Lyophilized from sterile PBS, pH 7.4
1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
2. Please contact us for any concerns or special requirements.
Please refer to the specific buffer information in the hard copy of CoA.
Shipping
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.
Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Stability & Storage
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃
Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Reconstitution
A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

EphB1 Protein, Mouse, Recombinant (His Tag): Images

EphB1 Protein, Mouse, Recombinant (His Tag): Alternative Names

9330129L11 Protein, Mouse; AW488255 Protein, Mouse; C130099E04Rik Protein, Mouse; Cek6 Protein, Mouse; Elk Protein, Mouse; Elkh Protein, Mouse; ENSMUSG00000074119 Protein, Mouse; Hek6 Protein, Mouse; Net Protein, Mouse

EphB1 Background Information

Ephrin type-B receptor 1, also known as EphB1, belongs to the ephrin receptor subfamily of the protein-tyrosine kinase family which 16 known receptors (14 found in mammals) are involved: EPHA1, EPHA2, EPHA3, EPHA4, EPHA5, EPHA6, EPHA7, EPHA8, EPHA9, EPHA1, EPHB1, EPHB2, EPHB3, EPHB4, EPHB5, EPHB6. EphB2 receptor tyrosine kinase phosphorylates syndecan-2 and that this phosphorylation event is crucial for syndecan-2 clustering and spine formation. The Eph family of receptor tyrosine kinases (comprising EphA and EphB receptors) has been implicated in synapse formation and the regulation of synaptic function and plasticity6. Ephrin receptors are components of cell signalling pathways involved in animal growth and development, forming the largest sub-family of receptor tyrosine kinases (RTKs). Ligand-mediated activation of Ephs induce various important downstream effects and Eph receptors have been studied for their potential roles in the development of cancer. EphB receptor tyrosine kinases are enriched at synapses, suggesting that these receptors play a role in synapse formation or function. We find that EphrinB binding to EphB induces a direct interaction of EphB with NMDA-type glutamate receptors. This interaction occurs at the cell surface and is mediated by the extracellular regions of the two receptors, but does not require the kinase activity of EphB.
Full Name
EPH receptor B1
References
  • Dalva MB, et al. (2000) EphB receptors interact with NMDA receptors and regulate excitatory synapse formation. Cell. 103(6): 945-56.
  • Takasu MA, et al. (2002) Modulation of NMDA receptor-dependent calcium influx and gene expression through EphB receptors. Science. 295(5554): 491-5.
  • Adams RH, et al. (1999) Roles of ephrinB ligands and EphB receptors in cardiovascular development: demarcation of arterial/venous domains, vascular morphogenesis, and sprouting angiogenesis. Genes Dev. 13(3): 295-306.
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