AFfirm™ EFNB1/2 Mouse Monoclonal Antibody - #BF8156
Product Info
*The optimal dilutions should be determined by the end user.
*Tips:
WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.
Fold/Unfold
CFND; CFNS; Craniofrontonasal syndrome (craniofrontonasal dysplasia); EFL 3; EFL-3; EFL3; EFNB1; EFNB1_HUMAN; Elk L; ELK ligand; ELK-L; Eph related receptor tyrosine kinase ligand 2; EPH-related receptor tyrosine kinase ligand 2; Ephrin-B1; EPLG2; LERK 2; LERK-2; LERK2; Ligand of eph related kinase 2; MGC8782;EFN B2; EFNB 2; Efnb2; EFNB2_HUMAN; Eph related receptor tyrosine kinase ligand 5; EPH-related receptor tyrosine kinase ligand 5; ephrin B2; Ephrin-B2; EphrinB2; EPLG 5; EPLG5; Htk L; HTK ligand; HTK-L; HTKL; LERK 5; LERK-5; LERK5; Ligand of eph related kinase 5; MGC126226; MGC126227; MGC126228; OTTMUSP00000024973;
Immunogens
Widely expressed (PubMed:8070404, PubMed:7973638). Detected in both neuronal and non-neuronal tissues (PubMed:8070404, PubMed:7973638). Seems to have particularly strong expression in retina, sciatic nerve, heart and spinal cord (PubMed:7973638).
P52799 EFNB2_HUMAN:Lung and kidney.
- P98172 EFNB1_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MARPGQRWLGKWLVAMVVWALCRLATPLAKNLEPVSWSSLNPKFLSGKGLVIYPKIGDKLDIICPRAEAGRPYEYYKLYLVRPEQAAACSTVLDPNVLVTCNRPEQEIRFTIKFQEFSPNYMGLEFKKHHDYYITSTSNGSLEGLENREGGVCRTRTMKIIMKVGQDPNAVTPEQLTTSRPSKEADNTVKMATQAPGSRGSLGDSDGKHETVNQEEKSGPGASGGSSGDPDGFFNSKVALFAAVGAGCVIFLLIIIFLTVLLLKLRKRHRKHTQQRAAALSLSTLASPKGGSGTAGTEPSDIIIPLRTTENNYCPHYEKVSGDYGHPVYIVQEMPPQSPANIYYKV
- P52799 EFNB2_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MAVRRDSVWKYCWGVLMVLCRTAISKSIVLEPIYWNSSNSKFLPGQGLVLYPQIGDKLDIICPKVDSKTVGQYEYYKVYMVDKDQADRCTIKKENTPLLNCAKPDQDIKFTIKFQEFSPNLWGLEFQKNKDYYIISTSNGSLEGLDNQEGGVCQTRAMKILMKVGQDASSAGSTRNKDPTRRPELEAGTNGRSSTTSPFVKPNPGSSTDGNSAGHSGNNILGSEVALFAGIASGCIIFIVIIITLVVLLLKYRRRHRKHSPQHTTTLSLSTLATPKRSGNNNGSEPSDIIIPLRTADSVFCPHYEKVSGDYGHPVYIVQEMPPQSPANIYYKV
PTMs - P98172,P52799 As Substrate
| Site | PTM Type | Enzyme | Source |
|---|---|---|---|
| Y11 | Phosphorylation | Uniprot | |
| N36 | N-Glycosylation | Uniprot | |
| T69 | Phosphorylation | Uniprot | |
| T180 | O-Glycosylation | Uniprot | |
| T189 | O-Glycosylation | Uniprot | |
| S260 | Phosphorylation | Uniprot | |
| T264 | Phosphorylation | Uniprot | |
| S268 | Phosphorylation | Uniprot | |
| S270 | Phosphorylation | Uniprot | |
| T274 | Phosphorylation | Uniprot | |
| Y304 | Phosphorylation | P29323 (EPHB2) | Uniprot |
| S308 | Phosphorylation | Uniprot | |
| Y311 | Phosphorylation | Uniprot | |
| Y316 | Phosphorylation | Uniprot | |
| S325 | Phosphorylation | Uniprot | |
| Y330 | Phosphorylation | Uniprot | |
| Y331 | Phosphorylation | Uniprot | |
| K332 | Ubiquitination | Uniprot |
| Site | PTM Type | Enzyme | Source |
|---|---|---|---|
| Y79 | Phosphorylation | Uniprot | |
| K163 | Ubiquitination | Uniprot | |
| T172 | O-Glycosylation | Uniprot | |
| T177 | O-Glycosylation | Uniprot | |
| T178 | O-Glycosylation | Uniprot | |
| S179 | O-Glycosylation | Uniprot | |
| T188 | O-Glycosylation | Uniprot | |
| S201 | O-Glycosylation | Uniprot | |
| T211 | O-Glycosylation | Uniprot | |
| S218 | Phosphorylation | Uniprot | |
| S223 | Phosphorylation | Uniprot | |
| S226 | Phosphorylation | Uniprot | |
| S227 | Phosphorylation | Uniprot | |
| S281 | Phosphorylation | Uniprot | |
| S283 | Phosphorylation | Uniprot | |
| T284 | Phosphorylation | Uniprot | |
| S287 | Phosphorylation | Uniprot | |
| K289 | Ubiquitination | Uniprot | |
| Y313 | Phosphorylation | Uniprot | |
| Y317 | Phosphorylation | Uniprot | |
| K319 | Ubiquitination | Uniprot | |
| S321 | Phosphorylation | Uniprot | |
| Y324 | Phosphorylation | Uniprot | |
| Y329 | Phosphorylation | Uniprot | |
| S338 | Phosphorylation | Uniprot | |
| Y343 | Phosphorylation | Uniprot | |
| Y344 | Phosphorylation | Uniprot | |
| K345 | Ubiquitination | Uniprot |
Research Backgrounds
Cell surface transmembrane ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binding to Eph receptors residing on adjacent cells leads to contact-dependent bidirectional signaling into neighboring cells. Shows high affinity for the receptor tyrosine kinase EPHB1/ELK. Can also bind EPHB2 and EPHB3. Binds to, and induces collapse of, commissural axons/growth cones in vitro (By similarity). May play a role in constraining the orientation of longitudinally projecting axons (By similarity).
Inducible phosphorylation of tyrosine residues in the cytoplasmic domain.
Proteolytically processed. The ectodomain is cleaved, probably by a metalloprotease, to produce a membrane-tethered C-terminal fragment. This fragment is then further processed by the gamma-secretase complex to yield a soluble intracellular domain peptide which can translocate to the nucleus. The intracellular domain peptide is highly labile suggesting that it is targeted for degradation by the proteasome.
Cell membrane>Single-pass type I membrane protein. Membrane raft.
Note: May recruit GRIP1 and GRIP2 to membrane raft domains.
Cell membrane>Single-pass type I membrane protein.
Nucleus.
Note: Colocalizes with ZHX2 in the nucleus.
Widely expressed. Detected in both neuronal and non-neuronal tissues. Seems to have particularly strong expression in retina, sciatic nerve, heart and spinal cord.
Interacts (via PDZ-binding motif) with GRIP1 and GRIP2 (via PDZ domain 6). Interacts with TLE1. The intracellular domain peptide interacts with ZHX2; the interaction enhances ZHX2 transcriptional repression activity (By similarity).
Belongs to the ephrin family.
Cell surface transmembrane ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Binds to receptor tyrosine kinase including EPHA4, EPHA3 and EPHB4. Together with EPHB4 plays a central role in heart morphogenesis and angiogenesis through regulation of cell adhesion and cell migration. EPHB4-mediated forward signaling controls cellular repulsion and segregation from EFNB2-expressing cells. May play a role in constraining the orientation of longitudinally projecting axons.
(Microbial infection) Acts as a receptor for Hendra virus and Nipah virus.
Inducible phosphorylation of tyrosine residues in the cytoplasmic domain.
Cell membrane>Single-pass type I membrane protein. Cell junction>Adherens junction.
Lung and kidney.
Interacts with PDZRN3 (By similarity). Binds to the receptor tyrosine kinases EPHA4, EPHB4 and EPHA3.
(Microbial infection) Interacts with Hendra virus and Nipah virus G protein.
Belongs to the ephrin family.
Research Fields
· Organismal Systems > Development > Axon guidance. (View pathway)
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