1μg (R: reducing condition, N: non-reducing condition).
Biotinylated Ephrin-B3 Fc&Avi Tag Protein, Human
Biotinylated Ephrin-B3 Fc&Avi Tag Protein, Human
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Product Details
Product Details
Product Specification
| Species | Human |
| Synonyms | EFL6, EPLG8, LERK8 |
| Accession | Q15768 |
| Amino Acid Sequence | Leu28-Ser224, with C-terminal hIgG1 Fc and Avi tag |
| Expression System | HEK293 |
| Molecular Weight | 60kDa (Reducing) |
| Purity | ＞95% by SDS-PAGE |
| Endotoxin | <1EU/μg |
| Conjugation | Biotin |
| Tag | Human Fc Tag, Avi Tag |
| Physical Appearance | Lyophilized Powder |
| Storage Buffer | PBS, pH7.4. |
| Reconstitution | Reconstitute at 0.1-1 mg/ml according to the size in ultrapure water after rapid centrifugation. |
| Stability & Storage | · 12 months from date of receipt, lyophilized powder stored at -20 to -80℃. · 3 months, -20 to -80℃ under sterile conditions after reconstitution. · 1 week, 2 to 8℃ under sterile conditions after reconstitution. · Please avoid repeated freeze-thaw cycles. |
| Reference | 1. Nan-Jie Xu, Suya Sun, Jay R Gibson & Mark Henkemeyer: A dual shaping mechanism for postsynaptic ephrin-B3 as a receptor that sculpts dendrites and synapses. Nature Neuroscience volume 14, pages1421–1429 (2011). |
Background
Ephrin-B3 binds HSPGs on HEK-293T, HeLa, and CHO cells, where heparin blocks binding to HEK-293T cells independently of Eph receptors, and a heparin/HS-binding domain in ephrin-B3 was identified outside of the Eph-receptors binding domain. The two positively charged residues, Arg178 and Lys179, in the ephrin-B3's juxtamembrane region is important for heparin/HS binding. Changing the corresponding amino acids in the non-heparin binding ephrin-B1 to positively charged residues gave heparin binding. Ephrin-A3 also binds HS, where Lys176 corresponds to Lys179 in ephrin-B3. Ephrin-B3 binding to lymphocytes and lymphoma cell lines may also depend on other residues near the transmembrane domain, in particular Arg188 which is less affected by heparin, suggesting several mechanisms for ephrin-B3 binding to cells. Functional studies revealed that ephrin-B3 binding to cells induces signaling, influencing both cell rounding and spreading.
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SDS-PAGE
