Recombinant Mouse Ephrin-B1 Fc Chimera Protein, CF Summary
Details of Functionality |
Measured by its binding ability in a functional ELISA. Immobilized recombinant mouse EphB3 Fc Chimera at 2 µg/mL (100 µL/well) can bind Recombinant Mouse Ephrin-B1 Fc Chimera with a linear range of 0.01-0.5 ng/mL. |
Source |
Mouse myeloma cell line, NS0-derived mouse Ephrin-B1 protein
Mouse Ephrin-B1 (Lys30-Ser229) Accession # AAA53231 |
IEGRMD |
Human IgG1 (Pro100-Lys330) |
6-His tag |
N-terminus |
|
|
C-terminus |
|
|
Accession # |
|
N-terminal Sequence |
Lys30 |
Structure / Form |
Disulfide-linked homodimer |
Protein/Peptide Type |
Recombinant Proteins |
Gene |
Efnb1 |
Purity |
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Endotoxin Note |
<0.01 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
49.2 kDa (monomer). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
SDS-PAGE |
60 kDa, reducing conditions |
Publications |
Read Publications using 473-EB in the following applications:
|
|
Packaging, Storage & Formulations
Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 3 months, -20 to -70 °C under sterile conditions after reconstitution.
|
Buffer |
Lyophilized from a 0.2 μm filtered solution in PBS. |
Purity |
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Reconstitution Instructions |
Reconstitute at 100 μg/mL in sterile PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse Ephrin-B1 Fc Chimera Protein, CF
Background
Ephrin-B1, also known as Elk Ligand, LERK2, and Eplg2, is an approximately 45 kDa member of the Ephrin-B family of transmembrane ligands that bind and induce the tyrosine autophosphorylation of Eph receptors. The extracellular domains (ECD) of Ephrin-B ligands are structurally related to GPI-anchored Ephrin-A ligands. Eph‑Ephrin interactions are widely involved in the regulation of cell migration, tissue morphogenesis, and cancer progression. Ephrin-B1 preferentially interacts with receptors in the EphB family. The binding of Ephrin-B1 to EphB proteins also triggers reverse signaling through Ephrin-B1 (1, 2). Mature mouse Ephrin-B1 consists of a 212 amino acid (aa) ECD, a 21 aa transmembrane segment, and an 88 aa cytoplasmic domain (3, 4). Within the ECD, mouse Ephrin-B1 shares 94% and 98% aa sequence identity with human and rat Ephrin-B1, respectively. Ligation by EphB2 enhances shedding of a 35 kDa fragment of the Ephrin-B1 ECD (5). The residual membrane-bound portion is then cleaved by gamma-secretase to release the intracellular domain (6). Ephrin-B1 also associates
in cis with Claudin-1, -4, and -5 (7, 8). It is expressed on glomerular podocyte slit diaphragms, developing thymocytes, peripheral T cells, monocytes, macrophages, vascular endothelial cells, cardiomyocytes, osteoclasts, and luteinizing granulosa cells in the ovary (8-13). In the developing nervous system, Ephrin-B1 plays a role in cellular migration, axon guidance, and presynaptic development (14-16). It also regulates developing thymocyte survival, monocyte migration, osteoclast differentiation and function, cardiac muscle morphogenesis, and tumorigenesis (5, 8, 10-12). Ephrin-B1 is up-regulated on reactive astrocytes and on macrophages and T cells found in atherosclerotic plaques (11, 17).
- Miao, H. and B. Wang (2009) Int. J. Biochem. Cell Biol. 41:762.
- Pasquale, E.B. (2010) Nat. Rev. Cancer 10:165.
- Shao, H. et al. (1994) J. Biol. Chem. 269:26606.
- Fletcher, F.A. et al. (1994) Genomics 24:127.
- Tanaka, M. et al. (2007) J. Cell Sci. 120:2179.
- Tomita, T. et al. (2006) Mol. Neurodegen. 1:2.
- Tanaka, M. et al. (2005) EMBO J. 24:3700.
- Genet, G. et al. (2012) Circ. Res. 110:688.
- Hashimoto, T. et al. (2007) Kidney Int. 72:954.
- Yu, G. et al. (2006) J. Biol. Chem. 281:10222.
- Sakamoto, A. et al. (2008) Clin. Sci. 114:643.
- Cheng, S. et al. (2012) PLoS ONE 7:e32887.
- Egawa, M. et al. (2003) J. Clin. Endocrinol. Metab. 88:4384.
- Davy, A. et al. (2004) Genes Dev. 18:572.
- Bush, J.O. and P. Soriano (2009) Genes Dev. 23:1586.
- McClelland, A.C. et al. (2009) Proc. Natl. Acad. Sci. USA 106:20487.
- Wang, Y. et al. (2005) Eur. J. Neurosci. 21:2336.
Customers Who Viewed This Item Also Viewed...
Species: Hu
Applications: CyTOF-ready, Flow, ICC, WB
Species: Hu, Mu, Rt
Applications: CyTOF-ready, Flow, ICC, WB
Species: Hu, Mu
Applications: CyTOF-ready, Flow, ICC, IHC, Simple Western, WB
Species: Rt
Applications: Bind
Species: Mu
Applications: Bind
Species: Hu
Applications: IHC, WB
Species: Mu
Applications: CyTOF-ready, Flow, ICC, WB
Species: Hu
Applications: IHC, IHC-P
Species: Mu
Applications: BA
Species: Mu
Applications: IHC, WB
Species: Hu
Applications: Bind
Species: Mu
Applications: CyTOF-ready, Flow, IHC, WB
Species: Hu
Applications: CyTOF-ready, Flow, IHC, KO, WB
Species: Hu
Applications: IHC, WB
Species: Hu, Mu
Applications: ICC/IF, IHC, IHC-P, IP, WB
Species: Hu, Mu
Applications: CyTOF-ready, ELISA, Flow-IC, Flow, ICC/IF, IHC, IHC-P, KD, WB
Species: Hu
Applications: Bind
Species: Ca, Hu, Mu, Pm, Rt
Applications: IHC, IHC-P, WB
FAQs for Ephrin-B1 (473-EB) (0)
Additional Ephrin-B1 Products
Blogs on Ephrin-B1