S100A9 _ Calgranulin_B _ MRP14
- Known as:
- S100A9 _ Calgranulin_B _ MRP14
- Catalog number:
- BM4027
- Product Quantity:
- 0.1 mg
- Category:
- -
- Supplier:
- ACR
- Gene target:
- S100A9 _ Calgranulin_B MRP14
Related genes to: S100A9 _ Calgranulin_B _ MRP14
- Gene:
- S100A9 NIH gene
- Name:
- S100 calcium binding protein A9
- Previous symbol:
- CAGB, CFAG
- Synonyms:
- P14, MIF, NIF, LIAG, MRP14, MAC387, 60B8AG, CGLB
- Chromosome:
- 1q21.3
- Locus Type:
- gene with protein product
- Date approved:
- 1989-05-19
- Date modifiied:
- 2018-05-02
Related products to: S100A9 _ Calgranulin_B _ MRP14
Related articles to: S100A9 _ Calgranulin_B _ MRP14
- Major depressive disorder (MDD) has been increasingly associated with low-grade inflammation, with neutrophils playing a central role. Calprotectin is a mainly neutrophil-derived inflammatory mediator. We investigated whether serum calprotectin levels are higher in patients with MDD than in healthy controls and whether the S100A9 rs3014866 polymorphism is associated with serum calprotectin levels and with MDD. - Source: PubMed
Publication date: 2026/05/13
Akbas FurkanBaykan OzgurAvcikurt Ayla SolmazBaykan Hayriye - Acute pancreatitis (AP) frequently progresses to systemic inflammation and acute lung injury, but the circulating mediators that couple pancreatic inflammation to remote organ damage remain poorly characterized. Following our finding that plasma exosomes induce AP-associated lung injury by triggering NOD-like receptor protein 3 (NLRP3)-dependent pyroptotic death in alveolar macrophages (AMs), this study aims to identify exosome-encapsulated S100A8/A9 derived from Kupffer cells (KCs) as a critical propagator of this inflammatory cascade. - Source: PubMed
Publication date: 2026/05/12
He Wen-QiLiu YiTang Ying-RuiWang RuiChen Chang-PingLv Xiao-QinSha Yuan-FeiRen Jian-Dong - The differentiation of HL-60 cells into neutrophil-like cells is widely used to study neutrophil functions, yet no comprehensive proteomic analysis has been conducted on dimethylformamide (DMF)-induced differentiation. This study provides the first detailed proteomic characterization of DMF-differentiated (df)-HL-60 cells, demonstrating its distinct molecular and functional profiles compared to the well-established dimethyl sulfoxide (DMSO)-df-HL-60 cell model. HL-60 cells were differentiated using 1.25% DMSO or 70 mM DMF for five days. Cell proliferation, granulocytic differentiation (CD11b expression), superoxide anion production, myeloperoxidase (MPO) protein expression and enzymatic activity, and neutrophil extracellular trap (NET) formation were evaluated. Proteomic profiling was performed using LC-MS/MS, followed by gene ontology and pathway enrichment analysis to identify key molecular changes associated with differentiation. DMF-df-HL-60 cells maintained higher proliferation rates than DMSO-df-HL-60 cells. Both agents successfully induced granulocytic differentiation, with DMSO producing greater CD11b expression. Functionally, both differentiation methods enhanced superoxide anion production, but DMF-df-HL-60 cells generated distinct superoxide radical spectra when evaluated with EPR spectroscopy. MPO protein expression and activity were significantly reduced in both differentiation models, indicating a transition to a mature neutrophil-like phenotype. Proteomic analysis revealed that neutrophil degranulation was the most significantly enriched pathway in DMF-df-HL-60 cells, alongside pathways involved in oxidant production and receptor tyrosine kinase signaling. Furthermore, S100 calcium-binding protein A9 (S100A9) abundance was significantly higher in DMF-df-HL-60 cells, suggesting a novel role of DMF in modulating neutrophil differentiation. DMF-df-HL-60 cells also showed activation of MAPK, Ras, and Rap1 signaling pathways, similar to the DMSO-df-HL-60 cell model, which is crucial for differentiation and immune responses. DMF-df-HL-60 cells generated more NETs than the DMSO-df-HL-60 cell model with phorbol myristate acetate. This study emphasizes the importance of selecting the appropriate differentiation model to accurately mimic neutrophil biology and highlights DMF's unique role in neutrophil differentiation, providing novel insights into differentiation-induced functional adaptations. - Source: PubMed
Publication date: 2026/05/13
Eldalal OthmanTabana YasserBabu DineshTran Newton HLockhart StevenKranrod JoshuaSeubert John MTonoyan LusineFahlman Richard PSiraki Arno G - Neutrophils are the most abundant circulating leukocytes and are characterized by a proteome in which granule-associated proteins synthesized during granulopoiesis constitute a major fraction of total cellular protein, reflecting their preloaded effector nature in innate immune defense. A striking feature of neutrophil biology is the unusual abundance of the calcium-binding proteins S100A8 and S100A9, which together form the heterodimeric complex known as calprotectin. Early biochemical studies estimated that S100A8/A9 constitutes a substantial fraction of the soluble cytosolic proteome in neutrophils, with later studies often describing it as one of the most abundant protein complexes in these cells. Despite extensive studies on the antimicrobial and inflammatory activities of calprotectin, the biological rationale for this unusual abundance remains incompletely understood. In this review, we examine the structural, biochemical, and regulatory features of S100A8/A9 and explore the potential explanations for its high abundance in the neutrophil cytosol. We first discuss the unique organization of the neutrophil proteome and the transcriptional programs governing granulopoiesis that lead to large-scale production of neutrophil effector proteins. We then review the structural and biochemical properties of S100A8/A9, including its calcium-dependent conformational dynamics and high-affinity transition metal binding, which contribute to antimicrobial defense through nutritional immunity. Several functional hypotheses are considered to explain calprotectin abundance, including roles as an antimicrobial reservoir, a metal-sequestering molecule, a regulator of oxidative stress, and a source of damage-associated molecular patterns. Finally, we discuss the evolutionary logic of neutrophil protein preloading and the implications of calprotectin biology in inflammatory diseases and the tumor microenvironment. Resolving the abundance paradox of S100A8/A9 may reveal fundamental principles governing the organization of innate immune cell proteomes and provide new insights into the strategies used by neutrophils to achieve rapid and effective host defense. - Source: PubMed
Publication date: 2026/04/27
Kim Kyung-HeeYoo Byong Chul - Vesicular cutaneous lupus erythematosus (VCLE) is a rare autoimmune disease in dogs and is considered the canine counterpart of human subacute cutaneous lupus erythematosus (SCLE). However, the molecular mechanisms underlying VCLE remain incompletely defined. - Source: PubMed
Publication date: 2026/05/11
Keating TreasaStranahan LaurenWiener DominiqueKeating M KellyLeon RenatoBanovic Frane