CXCR4 polyclonal antibody
- Known as:
- CXCR4 pab (anti-)
- Catalog number:
- PAB9849
- Product Quantity:
- 100 ug
- Category:
- -
- Supplier:
- Abno
- Gene target:
- CXCR4 polyclonal antibody
Related genes to: CXCR4 polyclonal antibody
- Gene:
- CXCR4 NIH gene
- Name:
- C-X-C motif chemokine receptor 4
- Previous symbol:
- -
- Synonyms:
- LESTR, NPY3R, HM89, NPYY3R, D2S201E, fusin, HSY3RR, NPYR, CD184
- Chromosome:
- 2q22.1
- Locus Type:
- gene with protein product
- Date approved:
- 1998-09-17
- Date modifiied:
- 2019-04-23
Related products to: CXCR4 polyclonal antibody
Related articles to: CXCR4 polyclonal antibody
- - Source: PubMed
- G protein-coupled receptors (GPCRs) can form heteromeric assemblies, yet whether class A GPCR heteromerization is dictated by cellular context remains unclear. Here we identify CXCR4-CCR5 heteromerization as a cell-dependent, cholesterol-sensitive, and ligand-regulated feature of live-cell membrane organization. In cancer-derived MDA-MB-231 cells, CXCR4 and CCR5 formed stable, slow-diffusing higher-order assemblies, whereas in COS7, HEK293, and MCF-10A cells the receptors were detected mainly as weaker monomer-dimer mixtures. Cholesterol depletion selectively reduced CXCR4-CCR5 heteromerization in MDA-MB-231 cells, implicating membrane composition as a major determinant of receptor assembly. Agonists induced transient heteromerization coupled to receptor internalization, while antagonists, especially plerixafor together with maraviroc, stabilized persistent surface-associated complexes. Molecular dynamics simulations in asymmetric bilayers resembling MDA-MB-231 and MCF-10A membranes identified cholesterol-enriched receptor interfaces that prolong CXCR4-CCR5 dimer lifetimes in MDA-like membranes. These results show that GPCR heteromerization is not an intrinsic fixed property of receptor pairs, but an emergent behavior shaped by cell state, lipid environment, and ligand input. - Source: PubMed
Publication date: 2026/05/20
Smith AdamSeghiri MohamedAshiru MojeedHair ElizabethRuiz AndresWilkins CeyvionFarshadfar Chiako - The atypical receptor ACKR3 works together with the canonical chemokine receptor CXCR4 to drive cell migration along gradients of their shared agonist CXCL12. CXCR4 promotes chemotaxis by activating canonical G protein pathways and recruiting β-arrestins. ACKR3 indirectly regulates CXCR4-mediated chemotaxis by scavenging CXCL12. Unlike canonical chemokine receptors, ACKR3 does not couple to G proteins and instead is 100% biased towards β-arrestins. CXCR4 activation by CXCL12 is exquisitely sensitive to subtle changes in both receptor and ligand. By contrast, ACKR3 is activation-prone: it recruits β-arrestins in response to many ligands and is much less sensitive to mutations, suggesting distinct activation mechanisms compared to CXCR4. To explore the basis of these differences, we compared the dynamics of ACKR3 and CXCR4 complexes with chemokines using molecular dynamic (MD) simulations. Ten-microsecond atomistic MD simulations revealed that CXCR4 adopts a stable active state when bound to WT CXCL12 but transitions to an inactive state when in complex with the antagonist variant, [P2G]CXCL12. By comparison, ACKR3 exhibits a variable transmembrane (TM) 6 state distribution and persistently "active" TM7 when complexed with either WT CXCL12 or [P2G]CXCL12, the latter retaining substantial agonistic activity at ACKR3. We further identified ligand-mediated residue interaction networks in the TM core that regulate TM6 and TM7 activation in CXCR4 but are absent or disrupted in ACKR3, resulting in less constrained receptor dynamics. These findings were validated by BRET-based assays with CXCL12 and ACKR3 mutants. Together, the data suggests that the unique conformational dynamics of ACKR3 govern its activation propensity, its ligand promiscuity, and its atypical effector coupling. - Source: PubMed
Publication date: 2026/05/20
Wang KaiNgo TonyKhare EktaChitsazi RezvanRoy SuchismitaSchafer Christopher THandel Tracy MKufareva Irina - Benzalkonium chloride (BAC), a widely used disinfectant compound, has been clinically associated with granular parakeratosis (GP), yet the underlying molecular mechanisms remain poorly defined. To address this, this study integrated network toxicology, molecular docking, and molecular dynamics simulation to uncover potential targets and mechanisms underlying the skin toxicity of BAC, with further validation through in vitro experiments using human skin keratinocytes. Network toxicology analysis of public databases identified 38 overlapping candidate genes linking BAC to GP. Subsequent enrichment analysis revealed these genes were significantly involved in biological processes critical for skin homeostasis, including keratinocyte differentiation, inflammatory response, and key signaling pathways such as EGFR and JAK-STAT. Molecular docking and dynamics simulations suggested CXCR4 as a potential interacting target for BAC. This prediction was experimentally supported in human keratinocytes (HaCaT cells) using the Drug Affinity Responsive Target Stability (DARTS) assay, supporting a physical interaction between BAC and CXCR4. Functional in vitro studies demonstrated that BAC exposure induced dose-dependent cytotoxicity, impaired proliferation and migration, and disrupted intercellular tight junctions. Furthermore, BAC treatment triggered upregulation of IL-1β, IL-6, and TNF-α mRNA, and increased phosphorylation of STAT3. Most importantly, pharmacological and genetic inhibition of CXCR4 substantially mitigated all the aforementioned cytotoxic, functional, and inflammatory effects induced by BAC, and specifically blocked the activation of STAT3. In conclusion, our findings suggest that BAC exposure in keratinocytes induces barrier-related dysfunction and inflammatory responses, potentially involving CXCR4-associated STAT3 signaling. These results provide mechanistic insight into BAC-related skin toxicity and warrant further investigation in disease-relevant models. This work not only advances our understanding of the disease but also identifies a promising therapeutic target for future intervention. - Source: PubMed
Publication date: 2026/06/02
Wu MofanZhang ShuaiYan ZhenyuYang JinfangYang HuihuiLi JingHuang ZhenyaoYuan Jiali - Circular RNAs (circRNAs) play pivotal roles in post-transcriptional regulation by acting as molecular sponges for microRNAs (miRNAs) within the competitive endogenous RNA (ceRNA) network. However, the regulatory mechanisms in teleost immune responses remain poorly understood. In this study, circRNA-miRNA-mRNA networks were investigated in turbot (Scophthalmus maximus) following Vibrio anguillarum infection to elucidate host-pathogen interactions. Through high-throughput sequencing of intestinal tissues, a total of 50 differentially expressed circRNAs (DE-circRNAs) (18 at 2 hpi, 16 at 12 hpi, 16 at 48 hpi), 212 DE-miRNAs (11 at 2 hpi, 70 at 12 hpi, 15 at 48 hpi), and 1774 DE-mRNAs were identified. Functional enrichment analyses (GO/KEGG) revealed significant associations with immune pathways, including the MAPK signaling pathway and gap junction. An integrated circRNA-miRNA-mRNA regulatory network was constructed, highlighting key interactions including novel_circ_0002573/DE-miR-27a-3p/FGB and novel_circ_0002423/novel_347/GNE, which may regulate inflammatory and antibacterial responses. The expression patterns of selected circRNAs, miRNAs and mRNAs were validated using qRT-PCR, confirming the reliability of the sequencing results. Importantly, fibrinogen beta chain (FGB) and CXCR4/CXCL12 signaling were identified as critical immune modulators. These findings provide insights of the ceRNA regulatory networks involved in teleost intestinal immunity and provide potential molecular targets for selective breeding of disease resistance in this species. - Source: PubMed
Publication date: 2026/06/01
Liu YiyingZhang PeiChen ChonghuiZhang XiaoxuCao MinYang NingLi ChaoFu Qiang