EFNB1 Antibody

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Description

Introduction to EFNB1 Antibody

EFNB1 (Ephrin B1) is a membrane-bound ligand within the Eph-Ephrin receptor tyrosine kinase family, involved in cell adhesion, tissue patterning, and synaptic plasticity . EFNB1 antibodies target this protein, enabling its detection and functional analysis in experimental settings. These antibodies are widely used in Western Blot (WB), Immunohistochemistry (IHC), and Enzyme-Linked Immunosorbent Assays (ELISA) .

Biological Role and Mechanisms

EFNB1 facilitates bidirectional signaling through interactions with Eph receptors, influencing:

  • Developmental patterning: Critical for craniofacial and neural tube development .

  • Cancer progression: Modulates drug sensitivity in B-cell lymphomas by regulating phosphorylation of SRC and STMN1, impacting chemotherapeutic efficacy .

  • Cell differentiation: Acts as a biomarker for germinal center B-cell differentiation, correlating with cell-of-origin (COO) scores in diffuse large B-cell lymphoma (DLBCL) .

Clinical Significance

EFNB1 dysfunction is linked to:

  • Craniofrontonasal syndrome (CFNS): Over 115 EFNB1 mutations cause craniosynostosis and developmental defects, predominantly in females .

  • Cancer prognosis: High EFNB1 levels in DLBCL associate with poor prognosis and chemoresistance, while low levels correlate with sensitivity to PI3K/AKT inhibitors .

Key Research Findings

Recent studies highlight EFNB1's multifaceted roles:

FindingMechanismImpactSource
EFNB1 overexpression enhances VCR sensitivityPhosphorylates STMN1 (Ser28), destabilizing microtubulesSupports EFNB1 as a chemosensitizer target
EFNB1 levels predict DLBCL drug responseHigh EFNB1 increases SRC phosphorylation; low EFNB1 upregulates PI3K/AKTStratifies patients for targeted therapies (e.g., SRC inhibitors)
EFNB1-COO score correlationEFNB1 expression quantifies B-cell differentiation (GCB vs. ABC subtypes)Refines lymphoma classification and prognostic models

Applications in Research

  • Drug response studies: EFNB1 antibodies validate protein levels in cell lines treated with SRC/PI3K inhibitors .

  • Tissue staining: IHC confirms EFNB1 localization in tumor microenvironments .

  • Mechanistic studies: Co-immunoprecipitation identifies EFNB1 interactions (e.g., SDCBP) .

Challenges and Future Directions

Current limitations include cross-reactivity with Ephrin-B2/B3 and variable performance across tissue types . Future research aims to:

  • Develop isoform-specific antibodies.

  • Validate EFNB1 as a companion diagnostic for chemotherapy regimens.

  • Explore EFNB1 agonists to enhance cytotoxic drug efficacy .

Product Specs

Buffer
PBS with 0.02% Sodium Azide, 50% Glycerol, pH 7.3. Store at -20°C. Avoid freeze/thaw cycles.
Lead Time
Typically, we can ship your orders within 1-3 business days of receiving them. Delivery times may vary depending on your location and purchasing method. Please contact your local distributors for specific delivery timelines.
Synonyms
EFNB1; EFL3; EPLG2; LERK2; Ephrin-B1; EFL-3; ELK ligand; ELK-L; EPH-related receptor tyrosine kinase ligand 2; LERK-2
Target Names
EFNB1
Uniprot No.

Target Background

Function
Ephrin-B1 is a cell surface transmembrane ligand for Eph receptors. These receptors are a family of receptor tyrosine kinases that play crucial roles in cell migration, repulsion, and adhesion during the development of neuronal, vascular, and epithelial tissues. When Ephrin-B1 binds to Eph receptors on neighboring cells, it triggers contact-dependent bidirectional signaling, influencing the behavior of both interacting cells. Ephrin-B1 exhibits high affinity for the receptor tyrosine kinase EPHB1/ELK, but can also bind to EPHB2 and EPHB3. In vitro studies have shown that Ephrin-B1 can bind to and induce the collapse of commissural axons/growth cones. This suggests that Ephrin-B1 may play a role in guiding the orientation of longitudinally projecting axons.
Gene References Into Functions
  • Lymphomas with low UTX expression exhibit high levels of Efnb1, and are associated with significantly poorer survival. PMID: 30006524
  • Chronic hypoxia-induced slug promotes invasive behavior of prostate cancer cells by activating the expression of ephrin-B1. PMID: 30058095
  • Research indicates that EphB2 cells experience a transient increase in migration after heterotypic activation. This phenomenon is believed to underlie a shift in the EphB2-ephrinB1 border, although it is not considered essential for cell segregation or border sharpening. PMID: 28747399
  • Studies suggest that the expression of EFNB1 and EFNB2 is involved in Th cell differentiation and migration to inflammatory sites in both EAE and MS. PMID: 27039370
  • Evidence demonstrates that mosaicism for EPHRIN-B1 expression, induced by random X inactivation in heterozygous females, results in robust cell segregation in human neuroepithelial cells. This finding supports the hypothesis that Eph/ephrin-mediated cell segregation plays a role in the pathogenesis of human CFNS patients. PMID: 28238796
  • Two mutations in EFNB1 have been identified: one novel (IVS2+3G>T) and one previously reported (p.Gly151Ser). Both cases were de novo and without a family history of Craniofrontonasal syndrome. PMID: 27650623
  • While ephrin-B1 deficiency leads to abnormal visual pathways in mice, the human visual system, with the exception of deficits in binocular vision, remains largely unaffected. PMID: 26580852
  • Studies have revealed that EphrinB1 (EFNB1) co-localizes with microtubules (MTs) during all phases of the cell cycle. PMID: 25436983
  • Researchers have identified a G151S mutation in the EFNB1 gene within a family. The mutation was observed in two severely affected sisters and, paradoxically, in their clinically unaffected father. PMID: 25486017
  • T cells from rheumatoid arthritis (RA) patients have been found to express higher levels of EFNB1 mRNA, which correlated with RA symptoms and laboratory findings. This suggests that EFNB1 expression in T cells could potentially serve as a parameter for monitoring RA disease activity and treatment responses. PMID: 25779027
  • Research indicates that EphrinB1 is uniquely dysregulated in medulloblastoma and promotes oncogenic responses in medulloblastoma cells, highlighting ephrinB1 as a potential therapeutic target. PMID: 25258252
  • EphB2/ephrin-B1 pathways were implicated in dental pulp stem cells treated with TNF-alpha via the JNK-dependent pathway, but not NF-kB, p38 MAPK, or MEK signaling. PMID: 25643922
  • Patients with EFNB1 mutations exhibit a distinct phenotype. This research facilitates genetic counseling for parents and patients, and contributes to the diagnostic and screening processes for individuals suspected of having CFNS. PMID: 24281372
  • CNK1 mediates ephrinB1 signaling, which promotes cell migration through RhoA and JNK activity. PMID: 24825906
  • EphrinB1 expression is associated with metastasis in breast cancer, and its enhanced expression is linked to a poor prognosis, suggesting that EphrinB1 could be a relevant therapeutic target for breast cancers. PMID: 24240587
  • High EFNB1 expression is associated with squamous cell carcinomas of the head and neck. PMID: 23811940
  • Researchers have identified mosaic EFNB1 mutations in every individual diagnosed with craniofrontonasal syndrome, confirming the diagnosis and supporting the hypothesis of cellular interference in humans. PMID: 23335590
  • Data indicate that EphrinB1, a PTPN13 substrate, interacts with ErbB2, and Src kinase mediates EphrinB1 phosphorylation and subsequent MAP Kinase signaling. PMID: 22279592
  • Studies suggest that X-linked cases resembling Teebi hypertelorism may share a similar mechanism to CFNS. Cellular mosaicism for varying levels of ephrin-B1 (including its simple presence or absence) is believed to contribute to craniofacial abnormalities. PMID: 21542058
  • An unreported mutation in EFNB1 is predicted to cause congenital diaphragmatic hernia, with phenotypic differences observed between males and females. PMID: 20734337
  • The impact of craniofrontonasal syndrome-causing EFNB1 mutations on ephrin-B1 function has been reported. PMID: 20565770
  • Research suggests that ephrin-B1 expression is regulated by a feedback loop involving posttranscriptional regulatory mechanisms. PMID: 20308325
  • A combination of SDF-1, PTN, IGF2, and EFNB1 has been found to mimic the DA phenotype-inducing property of SDIA and promote the differentiation of hESC into functional midbrain DA neurons. PMID: 19672298
  • Human platelets express EphA4 and EphB1, as well as the ligand ephrinB1. Forced clustering of EphA4 or ephrinB1 leads to cytoskeletal reorganization, adhesion to fibrinogen, and alpha-granule secretion. PMID: 12084815
  • Studies have explored the expression profile of this ligand of EPHB2 in gastric cancer. PMID: 12136247
  • The expression of ephrin-B1 was correlated with a poorer clinical prognosis. Ephrin-B1 protein was expressed by osteosarcoma cells and blood vessels. PMID: 12209731
  • Research identified a novel interaction between EphB1 and the adaptor molecule Grb7. This interaction is proposed to play a role in the regulation of cell migration by EphB1. PMID: 12223469
  • Studies have examined the expression of Eph-B1 in plasmacytoid dendritic cells. PMID: 12384430
  • Ephrin B1 induces human aortic endothelial cells migration through a pathway involving the Crk adaptor protein. PMID: 12475948
  • Research suggests that ephrinB1 and B class Eph receptors provide positional cues crucial for the normal morphogenesis of skeletal elements. PMID: 12919674
  • Eph/ephrin signaling enhances the ability of platelet agonists to cause aggregation by activating Rap1. These effects require oligomerization of ephrinB1 but not phosphotyrosine-based interactions with the ephrinB1 cytoplasmic domain. PMID: 14576067
  • Ephrin-B1 may be involved in in vivo tumor progression by promoting neovascularization in hepatocellular carcinoma. PMID: 14642617
  • Mutations in the ephrin-B1 gene cause craniofrontonasal syndrome. PMID: 15124102
  • Ephrin-B1 internalization is an active receptor-mediated process that utilizes the clathrin-mediated endocytic pathway. PMID: 15351694
  • Upon ephrinB1 stimulation, the small GTPases Rho and Ras are activated, while Rap1 is inactivated. PMID: 15725075
  • EFNB1 mutations have been implicated in both familial and sporadic craniofrontonasal syndrome (CFNS). PMID: 15959873
  • EphB/ephrin-B molecules play a role in restricting dental pulp stem cell attachment and migration, maintaining these cells within their stem cell niche under steady-state conditions. PMID: 17204606
  • The C-terminus of ephrin-B1 regulates the activation of extracellular release of MMP-8 without requiring de novo protein synthesis. PMID: 17567680
  • Research suggests that tyrosine phosphorylation of ephrin-B1 promotes the invasion of cancer cells in vivo. PMID: 17591954
  • Silencing of EphB expression is associated with colorectal tumorigenesis. PMID: 17906625
  • EphrinB1 may play a significant role in the inflammatory states of rheumatoid arthritis by influencing the population and function of T cells. PMID: 17942634
  • EFNB1 mutant transcripts with nonsense codons are degraded by the nonsense-mediated mRNA decay pathway, leading to craniofrontonasal syndrome. PMID: 18043713
  • Ephrin-B1 is believed to play a crucial role in the regulation of malignant T lymphocytes by controlling lipid-raft-associated signaling, adhesion, and invasive activity. PMID: 18314490
  • Several novel EFNB1 mutations have been identified in craniofrontonasal syndrome. PMID: 18627045

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Database Links

HGNC: 3226

OMIM: 300035

KEGG: hsa:1947

STRING: 9606.ENSP00000204961

UniGene: Hs.144700

Involvement In Disease
Craniofrontonasal syndrome (CFNS)
Protein Families
Ephrin family
Subcellular Location
Cell membrane; Single-pass type I membrane protein. Membrane raft.; [Ephrin-B1 C-terminal fragment]: Cell membrane; Single-pass type I membrane protein.; [Ephrin-B1 intracellular domain]: Nucleus.
Tissue Specificity
Widely expressed. Detected in both neuronal and non-neuronal tissues. Seems to have particularly strong expression in retina, sciatic nerve, heart and spinal cord.

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