Monoclonal anti_human EphA2 antibody (clone 3D7)
- Known as:
- Monoclonal anti_human EphA2 (anti-) (clonality 3D7)
- Catalog number:
- AEA0909
- Product Quantity:
- 100ul
- Category:
- -
- Supplier:
- ATGen
- Gene target:
- Monoclonal anti_human EphA2 antibody (clone 3D7)
Related genes to: Monoclonal anti_human EphA2 antibody (clone 3D7)
- Gene:
- EPHA2 NIH gene
- Name:
- EPH receptor A2
- Previous symbol:
- ECK
- Synonyms:
- -
- Chromosome:
- 1p36.13
- Locus Type:
- gene with protein product
- Date approved:
- 1991-08-07
- Date modifiied:
- 2016-10-05
Related products to: Monoclonal anti_human EphA2 antibody (clone 3D7)
Related articles to: Monoclonal anti_human EphA2 antibody (clone 3D7)
- Gliosarcoma (GSM) is a rare, highly invasive glioblastoma subtype with limited therapeutic options and a poor prognosis. We report the first dual-ligand hybrid solid lipid nanoparticle (HSLN) system for blood-brain barrier (BBB) penetration and targeted delivery of curcin, a type I ribosome-inactivating protein (RIP), to orthotopic GSM. - Source: PubMed
Publication date: 2026/03/04
Mohamed Mohamed SheikhVeeranarayanan SrivaniSakamoto YasushiSuge RieHirosawa NarumiPoulose Aby CheruvathoorMizuki ToruMaekawa Toru - Natural killer (NK) cells are promising candidates for cancer immunotherapy due to their safety and potent anti-tumor activity. However, their therapeutic efficacy is often limited by poor persistence and activity within the tumor microenvironment (TME) caused by a lack of essential cytokines. - Source: PubMed
Publication date: 2026/03/30
Wang ChunliKim SeokminKong Ling-ZuJang InhwanJo SeonaLee SunyoungLee Soo YunKim Kee KKim Tae-Don - Erythropoietin-producing hepatocellular receptor A2 (EphA2) has emerged as a key mediator that promotes tumor malignant progression. EphA2 overexpression and its non-canonical signaling lead to oncogenic transformation, metabolic reprogramming, resistance to treatments, and metastasis. Therefore, strategies targeting EphA2 have been evaluated in clinical trials. However, the clinical effects were not sufficient. An anti-EphA2 monoclonal antibody (mAb), EaMab-7 (mouse IgG, κ), demonstrated high affinity and specificity among Eph receptors. In this study, we produced recombinant class-switched EaMab-7 variants, including EaMab-7-mG (mouse IgG) and EaMab-7-hG (human IgG). Both EaMab-7-mG and EaMab-7-hG recognized human triple-negative breast cancer MDA-MB-231, pancreatic cancer MIA PaCa-2, and colorectal cancer HCT-15 in flow cytometry. Furthermore, both EaMab-7-mG and EaMab-7-hG exerted significant antibody-dependent cellular cytotoxicity and complement-dependent cytotoxicity against these tumors. In mouse xenograft models of breast, pancreatic, and colorectal cancers, both mAbs demonstrated antitumor activity. These results indicate the potential of EaMab-7 variants for the treatment of EphA2-positive cancers. - Source: PubMed
Publication date: 2026/04/02
Li GuanjieSuzuki HiroyukiOhishi TomokazuSatofuka HiroyukiIshikawa KenichiroShimizu KaiNomura AiriAraki HarutoKojo NaokiSuzuki KaitoHanda SaoriNakamura TakuroYanaka MiyukiTanaka TomohiroKaneko Mika KKato Yukinari - Ephrin (Eph) receptors play key regulatory roles in physiological processes, such as tissue development, cell migration, and angiogenesis. Upregulation of specific Eph receptors has been identified in many different cancers, highlighting Eph receptors as promising targets for new cancer therapeutics. Though targeting individual Eph receptors is challenging because of the high sequence homology among the 14 Eph receptors in humans, peptides have been isolated through phage display that target specific receptors (EphA2, EphA4, EphB2, EphB4). While many of these peptides have been further optimized based on the original phage display hits, the EphB2 receptor-targeting SNEW peptide has received less attention. Here we describe parallel strategies to modify SNEW, leading to improved affinity for the EphB2 receptor and greater stability in human serum while retaining SNEW's high specificity for the EphB2 receptor. Specifically, replacement of the N-terminal serine residue with cyclic α-amino acids, particularly those with saturated, six-membered rings, increased inhibitory potency against the EphB2 receptor-ephrin B2 interaction. Replacement of a central proline residue with 4,4-difluoroproline led to a significant increase in serum stability in the context of SNEW and its more potent N-terminally modified variants. SNEW variants with greater potency and serum stability offer lead candidates for targeting the EphB2 receptor in associated cancers and other diseases. Additionally, the modification approaches employed for SNEW may be extensible for N-terminal serine/threonine/cysteine substitution and/or proline substitution to improve protein targeting by other peptides. - Source: PubMed
Publication date: 2026/04/03
Garcia Brian EEpstein Sophie RLegarreta Sofia ATennett Jessica CCain Jenna MSawyer Nicholas - Both PRMT5 and EphA2 proteins are overexpressed and play a crucial role in multiple cancers, and have been used as targets to develop new anticancer drugs. However, the function and significance of the PRMT5-EphA2 interaction are unclear. Here, we report that PRMT5 bound to EphA2, catalyzed the dimethylation of EphA2 at arginine 816, and then stabilized EphA2 via inhibiting Cbl-mediated EphA2 ubiquitination and degradation in nasopharyngeal carcinoma (NPC) cells. Functionally, PRMT5 promoted in vitro and in vivo NPC stem cell properties by methylating and stabilizing EphA2. Based on the interacting regions of PRMT5 and EphA2 proteins, we developed a 20 amino acid-long PRMT5-derived peptide, P20, which disrupted the connection of PRMT5 with EphA2, degraded EphA2, and suppressed NPC stem cell properties in vitro and in mice. Moreover, the expression levels of PRMT5 and EphA2 in the NPC tissues were significantly higher than those in the normal nasopharyngeal mucosal tissues, and both proteins for predicting the patient's prognosis are superior to individual proteins. Our findings suggest that PRMT5 methylates and stabilizes EphA2 to promote NPC stem cell properties, and the PRMT5-derived peptide P20 can serve as a novel strategy for targeting EphA2 degradation and inhibiting NPC stem cell properties. - Source: PubMed
Publication date: 2026/03/28
Yu Zheng-ZhengMao Xue-LiLu Shan-ShanLu Ruo-HuangZhu WeiWu DiYi HongHuang WeiWen QiLin Guo-XiangZeng TingPeng Yun-XiYuan LiRan TingFeng JuanPeng JinwuXiao Zhi-Qiang