Ephrin B2 Protein, Human, Recombinant

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Ephrin B2 Protein, Human, Recombinant: Product Information

Purity
> 95 % as determined by SDS-PAGE
Endotoxin
< 1.0 EU per μg of the protein as determined by the LAL method
Activity
1.Measured by its binding ability in a functional ELISA.
2.Immobilized human EFNB2 (Cat:10881-HCCH) at 10μg/mL (100μL/well) can bind biotinylate human EphB4-Fc (Cat:10235-H02H), the EC50 of biotinylate human EphB4-Fc is 5-60 ng/mL.
Protein Construction
A DNA sequence encoding the human EFNB2 (NP_004084.1) (Met1-Ala229) was expressed with six amino acids (ENLYFQ) at the C-terminus was expressed and purified.
Accession#
Expressed Host
HEK293 Cells
Species
Human
Predicted N Terminal
Ile 28
Molecule Mass
The recombinant human EFNB2 consists of 209 amino acids and predicts a molecular mass of 23.1 KDa. It migrates as an approximately 32-36 KDa band in SDS-PAGE under reducing conditions.
Formulation
Lyophilized from sterile PBS, pH 7.4.
Please contact us for any concerns or special requirements.
Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization.
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.

Ephrin B2 Protein, Human, Recombinant: Images

1.Measured by its binding ability in a functional ELISA. 2.Immobilized human EFNB2 (Cat:10881-HCCH) at 10μg/mL (100μL/well) can bind biotinylate human EphB4-Fc (Cat:10235-H02H), the EC50 of biotinylate human EphB4-Fc is 5-60 ng/mL.

Ephrin B2 Protein, Human, Recombinant: Alternative Names

EPLG5 Protein, Human; Htk-L Protein, Human; HTKL Protein, Human; LERK5 Protein, Human

Ephrin B2 Background Information

EphrinB2 also known as EFNB2 is a member of the ephrin family. EphrinB2 is involved in establishing arterial versus venous identity and perhaps in anastamosing arterial and venous vessels at their junctions. The transmembrane-associated ephrin ligands and their Eph family of receptor tyrosine kinases are expressed by cells of the SVZ. Eph/ephrin interactions are implicated in axon guidance, neural crest cell migration, establishment of segmental boundaries, and formation of angiogenic capillary plexi. Eph receptors and ephrins are divided into two subclasses, A and B, based on binding specificities. Ephrin subclasses are further distinguished by their mode of attachment to the plasma membrane: ephrin-A ligands bind EphA receptors and are anchored to the plasma membrane via a glycosylphosphatidylinositol (GPI) linkage, whereas ephrin-B ligands bind EphB receptors and are anchored via a transmembrane domain. An exception is the EphA4 receptor, which binds both subclasses of ephrins. EphrinB2 expression progressively extends from the arterial endothelium to surrounding smooth muscle cells and to pericytes, suggesting that ephrin-B2 may play an important role during formation of the arterial muscle wall.
Full Name
ephrin-B2
References
  • Wang HU, et al. (1998) Molecular distinction and angiogenic interaction between embryonic arteries and veins revealed by ephrin-B2 and its receptor Eph-B4. Cell. 93(5): 741-53.
  • Gale NW, et al. (2001) Ephrin-B2 selectively marks arterial vessels and neovascularization sites in the adult, with expression in both endothelial and smooth-muscle cells. Dev Biol. 230(2): 151-60.
  • Shin D, et al. (2001) Expression of ephrinB2 identifies a stable genetic difference between arterial and venous vascular smooth muscle as well as endothelial cells, and marks subsets of microvessels at sites of adult neovascularization. Dev Biol. 230(2): 139-50.
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