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> Recombinant Protein > InsectCell Expressed > EPHB3 / HEK2 (aa 585-998) Protein (GST Tag) EPHB3 / HEK2 (aa 585-998) Protein (GST Tag)
| Catalog | Size (Price) | Quantity | In Stock | Operation | Other Information |
| 13925-H20B1 |
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EPH receptor B3 Protein Datasheet
EPHB3 / HEK2 Protein Price Inquiry ( Available Sizes )
- 50μg: Inquiring Price;
- 200μg: Inquiring Price;
- ≥1mg Bulk: Inquiring Price
EPHB3 / HEK2 Protein Product Information
| Synonym : | EPHB3, ETK2, HEK2, TYRO6 |
| Protein Construction: |
A DNA sequence encoding the human EPHB3 (P54753) (Gln585-Val998) was fused with the N-terminal polyhistidine-tagged GST tag at the N-terminus. |
| Source: | Human |
| Expression Host: | Baculovirus-Insect cells |
EPHB3 / HEK2 Protein QC Testing
| Purity: | > 90% as determined by SDS-PAGE | SDS-PAGE:![]() EPHB3 / HEK2 protein |
| Endotoxin: | < 1.0 EU per μg of the protein as determined by the LAL method | |
| Stability: | Samples are stable for up to twelve months from date of receipt at -70℃ | |
| Predicted N terminal: | Met | |
| Molecular Mass: |
The recombinant human EPHB3 /GST chimera consists of 651 amino acids and has a calculated molecular mass of 74.7 kDa. The recombinant protein migrates as an approximately 64 kDa band in SDS-PAGE under reducing conditions. |
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| Formulation: | Lyophilized from sterile 20mM Tris, 500mM NaCl, pH7.4, 10%gly.
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EPHB3 / HEK2 Protein Usage Guide
| Storage: | Store it under sterile conditions at -70℃. 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. |
EPHB3 / HEK2 Protein Related Products & Topics
Related Areas:
Enzyme>>Protein Kinase>>Receptor Tyrosine Kinase>>EphB3/HEK2
Signal Transduction>>Protein Kinase>>Receptor Tyrosine Kinase>>EphB3/HEK2
Neuroscience>>Axon Guidance>>Ephrin & Eph Receptor>>EphB3/HEK2
Cancer>>Growth Factor & Receptor>>Receptor Tyrosine Kinase>>EphB3/HEK2
Cancer>>Growth Factor & Receptor>>Ephrin & Eph Receptor>>EphB3/HEK2
Proteins:
| Molecule | Species | Description //For Detailed Info. and Price------CLICK! | Cat. No |
| EphB3/HEK2 | Human | EPHB3 / HEK2 (aa 585-998) Protein, Recombinant, with GST Tag | 13925-H20B1 |
| EphB3/HEK2 | Mouse | EphB3/HEK2 Protein, Recombinant![]() |
50581-M08H |
Antibodies:
| Molecule | Application | Description //For Detailed Info. and Price------CLICK! | Cat. No |
| Mouse EphB3/HEK2 | WB, ELISA | EphB3 / HEK2 Antibody (Antigen Affinity Purified) | 50581-RP02 |
EPHB3 / HEK2 Protein Description
Ephrin type-B receptor 3, EPH-like kinase 2, Tyrosine-protein kinase TYRO6, EPHB3, ETK2, HEK2 and TYRO6, is a single-pass type I membrane protein which belongs to the protein kinase superfamily, tyr protein kinase family, ephrin receptor subfamily. EPHB3 contains two fibronectin type-III domains, one protein kinase domain and one SAM (sterile alpha motif) domain. EphB3 is initially expressed in the sclerotome, but later is expressed predominantly in the dermatome. It is prominent expression is also detected in the developing heart, liver, posterior ventral limb bud mesenchyme, pharyngeal arches, and head mesenchyme. The EphB3 receptors are expressed during embryonic development in multiple regions of the central nervous system. The spatial profile of EphB3 receptors is co-localized to regions of the brain that had a high level of EphB3 receptor binding ligands. Its expression pattern suggests that EphB3 may play a role in the maintenance of mature neuronal connections or re-arrangement of synaptic connections during late stages of development. EphB3-ephrin-B interaction promotes MET by re-establishing epithelial cell-cell junctions and such an MET-promoting effect contributes to EphB3-mediated tumor suppression.
References
- Baker RK. et al., 2001, Mech Dev. 104 (1-2): 129-32.
- Willson CA. et al., 2003, Cell Transplant. 12 (3): 279-90.
- Willson CA. et al., 2006, J Mol Histol. 37 (8-9): 369-80.
- Risley M. et al., 2009, Mech Dev. 126 (3-4): 230-9.
- Chiu ST. et al., 2009, Carcinogenesis. 30 (9): 1475-86.

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