CXCL12 _ SDF1
- Known as:
- CXCL12 _ SDF1
- Catalog number:
- GTX10395
- Product Quantity:
- 25 µg
- Category:
- -
- Supplier:
- ACR
- Gene target:
- CXCL12 _ SDF1
Related genes to: CXCL12 _ SDF1
- Gene:
- CXCL12 NIH gene
- Name:
- C-X-C motif chemokine ligand 12
- Previous symbol:
- SDF1A, SDF1B, SDF1
- Synonyms:
- SCYB12, SDF-1a, SDF-1b, PBSF, TLSF-a, TLSF-b, TPAR1
- Chromosome:
- 10q11.21
- Locus Type:
- gene with protein product
- Date approved:
- 1994-11-30
- Date modifiied:
- 2016-10-05
Related products to: CXCL12 _ SDF1
Anserine Stromal Cell Derived Factor 1 Elisa Kit (SDF1)Anserine anti - Stromal Cell Derived Factor 1 Elisa Kit (SDF1)anti-CXCL12(1F7)Anti-human CXCL12, Source: Monoclonal Murine, MABAnti-human SDF-1 alpha (CXCL12), bt, Source: Polyclonal bt. Rabbit, PABAnti-human SDF-1 alpha (CXCL12), bt, Source: Polyclonal bt. Rabbit, PABAnti-human SDF-1 alpha (CXCL12), bt, Source: Polyclonal bt. Rabbit, PABAnti-human SDF-1 alpha (CXCL12), Source: Polyclonal Rabbit, PABAnti-human SDF-1 alpha (CXCL12), Source: Polyclonal Rabbit, PABAnti-human SDF-1 alpha (CXCL12), Source: Polyclonal Rabbit, PABAnti-human SDF-1 beta (CXCL12), bt, Source: Polyclonal bt. Goat, PABAnti-human SDF-1 beta (CXCL12), bt, Source: Polyclonal bt. Goat, PABAnti-human SDF-1 beta (CXCL12), bt, Source: Polyclonal bt. Goat, PABAnti-human SDF-1 beta (CXCL12), Source: Polyclonal Goat, PABAnti-human SDF-1 beta (CXCL12), Source: Polyclonal Goat, PAB Related articles to: CXCL12 _ SDF1
- Cisplatin response in gastric cancer is shaped by malignant cell programs, stromal states, and mutation-immune crosstalk, but the CAF subtypes linked to platinum tolerance and their epithelial effectors remain incompletely defined. We integrated single-cell RNA sequencing, epithelial CNV-like inference, fibroblast reclustering, CellChat analysis, signature scoring, hdWGCNA, CAF-epithelial coupling, exploratory GSE14209 evaluation, TCGA-STAD mutation/copy-number contextualization, and DepMap CRISPR virtual knockout analysis, followed by experimental validation in AGS and HGC-27 cells. IGF1+ CXCL12+ CAFs showed resistance-supportive stromal features, and CAF-epithelial coupling prioritized ARPC1A as a tumor epithelial candidate associated with this stromal program. In TCGA-STAD, ARPC1A mutations were rare and consisted of three missense and two frameshift variants without a recurrent hotspot; the mutant tumors were confined to the MSI subtype and showed an immune-activated, high TMB/MSI context, indicating mutation-immune crosstalk rather than a clear mutation-specific CAF, EMT, drug resistance, or cisplatin response phenotype. By contrast, ARPC1A copy-number gain/amplification was more frequent and tracked with ARPC1A expression, CIN enrichment, aneuploidy, and fraction of genome altered. DepMap CRISPR data indicated mostly weak-to-mild baseline ARPC1A dependency in upper GI and gastric/GEJ models. Experimentally, ARPC1A knockdown increased cisplatin sensitivity, promoted cisplatin-induced apoptosis, and suppressed migration and invasion. These findings identify a CAF-associated ARPC1A epithelial program linked to cisplatin response and support a mutation-immune/copy-number framework in which ARPC1A is interpreted mainly through immune-contextual mutation patterns and expression dosage rather than recurrent gain-of-function mutation. - Source: PubMed
Publication date: 2026/08/19
Lu DeyiMeng FanlaiZhou WeiyingHu YifeiLi GaoshaGe JiahaoZhang QingMin Qi - Macrophages facilitate blastema and wound epithelium formation by clearing debris and remodeling the immune and extracellular matrix. The M1-to-M2 transition is well documented in amphibians, but its occurrence and timing in diverse lizards remain unclear. This study examined macrophage function during tail regeneration in . - Source: PubMed
Publication date: 2026/08/06
Li QingZhang YiwenShi TingtingLi RongnanYang YongqingYang Chun - Ischemic stroke is a global health crisis necessitating targeted therapeutic strategies. Central to post-stroke pathology and repair is the CXCL12 signaling axis. In this review, we discuss the context-dependent roles of CXCL12 and its canonical receptor, CXCR4, within the post-ischemic microenvironment. The CXCL12/CXCR4 axis exhibits a temporal duality across the evolution of the neurovascular lesion; however, current evidence necessitates moving beyond a strictly binary framework. While the acute phase involves pathological cascades, such as blood-brain barrier disruption and leukocyte infiltration, the axis is simultaneously essential for recruiting protective innate immune subsets. During subsequent subacute and chronic phases, it governs essential restorative processes, including neurogenesis, angiogenesis, and remyelination. This complex temporal shift is mediated by the interplay between distinct CXCL12 isoforms and the regulatory influence of the atypical receptor ACKR3/CXCR7. Furthermore, these endogenous repair mechanisms exhibit synergies with non-pharmacological interventions, notably environmental enrichment and remote ischemic postconditioning. Our multidimensional model suggests that the functional outcome of CXCL12/CXCR4 signaling is determined by the intersection of timing, cell type, receptor availability, and adaptive responses to physiological stimuli. We synthesize fundamental mechanistic data with translational insights to evaluate the therapeutic potential of this axis and the pharmacological barriers to future regenerative strategies. - Source: PubMed
Publication date: 2026/08/20
Eisa-Beygi ShahramWu HaoCui KuiArulsamy KulandaisamyZhu BoWang BeibeiSingh BandanaGupta KrishanGao JianingWong ScottBischoff JoyceDeng HanqiangChen Hong - We report a cloud-executed, ligand-guided virtual screening workflow for practical and rapid experimental testing of CXCR4 antagonists. Using the Rush platform, an Enamine purchasable library (274,092 compounds) was standardized and pre-filtered to remove assay-interfering substructures, yielding 264,953 molecules for screening. A set of 18,378 compounds was identified through AMD070-based similarity filtering (Tanimoto ≥ 0.2, ECFP4). These candidates were then docked into the IT1t-bound CXCR4 structure using Gnina. A CNN pose-score cutoff (> 0.8) was applied as a pose-confidence filter, and the retained compounds were ranked by docking affinity (kcal/mol). The top 50 were triaged by pharmacokinetic-focused in silico assessment (SwissADME) to prioritize lead-like profiles and exclude structural alerts, resulting in 9 purchasable candidates for biological testing. Flow cytometry-based 12G5 competitive binding in Jurkat cells identified CUEN-837 as the initial hit (IC = 8.50 μM, 52.31% inhibition at 10 μM). CUEN-837 also inhibited CXCL12-driven chemotaxis (32.8% inhibition at 10 μM). It reduced the viability of three colorectal cancer organoid strains in a dose-dependent manner (IC 7.97-11.16 µM), providing supportive phenotypic evidence of activity in patient-derived organoid models. Overall, this end-to-end workflow efficiently compresses large libraries into a confirmed micromolar CXCR4 hit while lowering computational and infrastructure barriers for early-stage discovery. - Source: PubMed
Publication date: 2026/08/20
Nalinratana NonthanethSangsawat MonsinChong Kian CheeXu YichunHan JunsongDing YantingCai ZhaiThitikornpong WorathatZhu HuaVajragupta OpaRojsitthisak Pornchai - Fully reduced high-mobility group box 1 (HMGB1) binds CXCL12 and signals via CXCR4 when released into the extracellular space. It acts as a chemokine and transitions stem cells from quiescent G to a primed G state. Cells in G rapidly enter G in response to activating factors released by tissue injury to promote tissue repair. However, oxidative conversion of FR-HMGB1 into the disulfide form activates proinflammatory pathways via TLR-2, TLR-4 and RAGE. Peptide mapping and nuclear magnetic resonance (NMR) spectroscopy identified a conserved CXCL12-binding motif within each Box and adjacent flanking regions. We decoupled the regenerative and inflammatory functions using an engineered construct (dBB12L), comprising tandem Box B domains with a flexible linker. dBB12L exhibited CXCL12 binding and accelerated repair equivalent to FR-HMGB1. Importantly, dBB12L lacked detectable RAGE binding and did not signal via TLR-2 and TLR-4, establishing it as a potential therapeutic to promote tissue repair without deleterious inflammation. - Source: PubMed
Publication date: 2026/08/11
Viñals Guitart ÁlvaroLee CarlEspírito Santo Ana IsabelRuan Jia-LingMao Shih-HsuanWilliam LynnRedfield ChristinaFedorov OlegBurgess-Brown Nicola AYue Wyatt WNanchahal Jagdeep