ERK2 (Dominant Negative) Recombinant Adenovirus
- Known as:
- ERK2 (Dominant Negative) Recombinant Adenovirus
- Catalog number:
- ADV-113
- Product Quantity:
- 50
- Category:
- -
- Supplier:
- Cell Biolabs
- Gene target:
- ERK2 (Dominant Negative) Recombinant Adenovirus
Related genes to: ERK2 (Dominant Negative) Recombinant Adenovirus
- Gene:
- EFNB1 NIH gene
- Name:
- ephrin B1
- Previous symbol:
- EPLG2, CFNS
- Synonyms:
- LERK2, Elk-L
- Chromosome:
- Xq13.1
- Locus Type:
- gene with protein product
- Date approved:
- 1995-01-17
- Date modifiied:
- 2016-10-05
- Gene:
- MAPK1 NIH gene
- Name:
- mitogen-activated protein kinase 1
- Previous symbol:
- PRKM2, PRKM1
- Synonyms:
- ERK, ERK2, p41mapk, MAPK2
- Chromosome:
- 22q11.22
- Locus Type:
- gene with protein product
- Date approved:
- 1993-11-05
- Date modifiied:
- 2019-04-23
Related products to: ERK2 (Dominant Negative) Recombinant Adenovirus
Related articles to: ERK2 (Dominant Negative) Recombinant Adenovirus
- Cell-penetrating peptides (CPPs) deliver cargo proteins into cells; however, most CPPs rely on nonspecific electrostatic interactions, limiting their cell-type specificity. The CPP Pas2r12 delivers cargo, such as enhanced green fluorescent protein (EGFP) and immunoglobulin G, into the cytosol, primarily through caveolae-dependent endocytosis. To elucidate the intracellular signaling underlying Pas2r12-mediated delivery, time-resolved phosphoproteomic analyses were performed following treatment with Pas2r12 or the Pas2r12-EGFP complex. Early phosphorylation of mitogen-activated protein kinase 1 (MAPK1) and ephrin B1 (EFNB1) was observed following stimulation with either Pas2r12 or the Pas2r12-EGFP complex, whereas F11R phosphorylation occurred only in response to Pas2r12. Notably, MAPK1 phosphorylation consistently increased at all timepoints after stimulation with either treatment. In addition, lysophosphatidic acid receptor 1 (LPAR1) phosphorylation was induced by both treatments at 30 min. EFNB1, F11R, and LPAR1 are cell surface ligands or receptors that are potential targets of Pas2r12 or the Pas2r12-EGFP complex. These results suggest that sustained MAPK1 phosphorylation may play a central role in cellular response to Pas2r12-based delivery. Future studies should aim at establishing Pas2r12 as an efficient and versatile protein delivery tool, with particular focus on exploiting specific cell-surface molecules to enhance targeting specificity. - Source: PubMed
Publication date: 2025/07/16
Okuda AkikoTakihara HayatoKuroiwa ReikaOkuda Shujiro - Most squamous cell carcinomas of the head and neck (HNSCC) overexpress ERBB1/EGFR, but EGF receptor (EGFR)-targeted therapies have yielded disappointing clinical results in treatment of this cancer. Here, we describe a novel interaction between EGFR and the ligand EphrinB1 (EFNB1), and we show that EFNB1 phosphorylation and downstream signaling persists in the presence of cetuximab. Mechanistically, cetuximab drives a shift in EGFR dimerization partners within the signaling complex, suggesting that targeted drugs may trigger partner rearrangements that allow persistent pathway activation. EFNB1 attenuation slowed tumor growth and increased survival in a murine model of HNSCC, suggesting a substantial contribution of EFNB1 signaling to HNSCC development. Together, our findings suggest that EFNB1 is part of the EGFR signaling complex and may mediate drug resistance in HNSCC as well as other solid tumors. - Source: PubMed
Publication date: 2013/06/28
Vermeer Paola DColbert Paul LWieking Bryant GVermeer Daniel WLee John H