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EphrinA3 / EFNA3 Protein
| Catalog | Size (Price) | Quantity | In Stock | Operation | Other Information |
| 10188-H03H |
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YES |
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EphrinA3 Protein Datasheet
EphrinA3 Protein Price Information
- ≥1mg Bulk: Inquiring Price
EphrinA3 Protein Product Information
| EphrinA3 Synonym: | EFNA3, EFL2, EPLG3, Ehk1-L, LERK3 |
| Protein Construction: | A DNA sequence encoding the human EphrinA3 (NP_004943.1) (Met 1- Ser 213 ) with the C-terminal propeptide removed was fused with the C-terminal polyhistidine-tagged Fc region of human IgG1 at the C-terminus. |
| Source: | Human |
| Expression Host: | Human Cells |
EphrinA3 Protein QC Testing
| Purity: | > 97%, as determined by SDS-PAGE | SDS-PAGE:![]() |
| Endotoxin: | < 1.0 EU per 1μg 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: | Gln 23 | |
| Molecular Mass: | The recombinant human EphrinA3/Fc is a disulfide-linked homodimer after removal of the signal peptide. The reduced monomer consists of 439 amino acids and has a predicted molecular mass of 49.5 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rhEphrinA3/Fc monomer is approximately 60-65 kDa due to glycosylation. | |
| Formulation: | Lyophilized from sterile PBS , pH 7.4
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EphrinA3 Protein Usage Guide
| Storage: | Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage and usage. 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. |
EphrinA3 Protein Related Products &Topics
Ephrin-A3 / EFNA3 / EFL2 Protein Related Areas:
Neuroscience>>Axon Guidance>>Ephrin & Eph Receptor>>Ephrin-A3/EFNA3
Cancer>>Growth Factor & Receptor>>Ephrin & Eph Receptor>>Ephrin-A3/EFNA3
Proteins:
| Molecule | Species | Description //For Detailed Info. and Price------CLICK! | Cat. No |
| Ephrin-A3/EFNA3 | Human | Ephrin-A3/EFNA3/Fc Protein, Recombinant |
10188-H02H |
| Ephrin-A3/EFNA3 | Human | Ephrin-A3/EFNA3/Fc Protein, Recombinant | 10188-H03H |
| Ephrin-A3/EFNA3 | Human | Ephrin-A3/EFNA3 Protein, Recombinant![]() |
10188-H08H |
| Ephrin-A3/EFNA3 | Human | Ephrin-A3/EFNA3 Protein, Recombinant | 10188-HCCH |
| Ephrin-A3/EFNA3 | Mouse | Ephrin-A3/EFNA3 Protein, Recombinant![]() |
50594-M08H |
Antibodies:
| Molecule | Application | Description //For Detailed Info. and Price------CLICK! | Cat. No |
| Human Ephrin-A3/EFNA3 |
WB, ELISA | Ephrin-A3/EFNA3 Antibody, Rabbit PAb | 10188-RP01 |
| Human Ephrin-A3/EFNA3 |
WB, ELISA | Ephrin-A3/EFNA3 Antibody, Rabbit Pab (Antigen Affinity Purified) | 10188-RP02 |
EphrinA3 Protein Description
The ephrins (EPH) and EPH-related receptors comprise the largest subfamily of receptor protein-tyrosine kinases (RTKs), and have been involved in a variety of biological processes, especially in the nervous system and in erythropoiesis, such as axon guidance and topographic map formation, synaptic plasticity, angiogenesis, and meanwhile have possible contributions to tumor growth and metastasis. Based on their structures and sequence relationships, ephrins are divided into the ephrin-A (EFNA) class which are anchored to the membrane by a GPI linkage, and the ephrin-B (EFNB) class, which are transmembrane proteins. 14 receptors and 8 ligands have been reported in mammals, and EphrinA3 is capable of binding EphA2, EphA3, EphA4, EphA5, EphA6, EphA7, EphA8, and EphB1. The EphrinA3 ligand may interact with the EphA5 receptor to restrict entorhinal axon terminals in the outer molecular layer of the dentate gyrus. Furthermore, Research evidences indicated that ephrin-A3, but not other ligands, binds to heparan sulfate, and the presence of cell surface heparan sulfate is required for the full biological activity of ephrin-A3.
References
- Zhou, R. Pharmacol. Ther. 77: 151-181.
- Stein, E. et al., 1999, J. Neurosci. 19: 8885-8893.
- Cheng, N. et al., 2002, Cytokine. Growth. Factor. Rev. 13: 75-85.
- Irie, F. et al., 2008, Proc. Nat. Acad. Sci. 105: 12307-12312.
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