S10A9_HUMAN CFAG ELISA tesk kit
- Known as:
- S10A9_HUMAN CFAG Enzyme-linked immunosorbent assay test tesk reagent
- Catalog number:
- gen17442
- Product Quantity:
- 1
- Category:
- Peptides
- Supplier:
- Other suppliers
- Gene target:
- S10A9_HUMAN CFAG ELISA tesk kit
Related genes to: S10A9_HUMAN CFAG ELISA tesk kit
- Gene:
- S100A8 NIH gene
- Name:
- S100 calcium binding protein A8
- Previous symbol:
- CAGA, CFAG
- Synonyms:
- P8, MRP8, 60B8AG, CGLA
- Chromosome:
- 1q21.3
- Locus Type:
- gene with protein product
- Date approved:
- 1989-05-19
- Date modifiied:
- 2018-05-02
- 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: S10A9_HUMAN CFAG ELISA tesk kit
Related articles to: S10A9_HUMAN CFAG ELISA tesk kit
- Psoriasis is a chronic immune-mediated inflammatory disorder with systemic implications. While transcobalamin 2 (TCN2) has been linked to several autoimmune diseases, its role in psoriasis remains unclear. Here, we investigated the contribution of TCN2 to psoriatic pathogenesis. TCN2 expression was significantly elevated in both lesional skin and peripheral blood mononuclear cells (PBMCs) from psoriasis patients, and its levels declined following biologic therapy. Similarly, increased TCN2 expression was observed in imiquimod (IMQ)-induced psoriatic lesions in mice. To further evaluate its function, we generated Tcn2-deficient (Tcn2-/-) mice and established an IMQ-induced psoriasis model. Compared with wild-type controls, Tcn2-/- mice developed attenuated skin lesions with reduced epidermal hyperplasia and inflammation. Transcriptomic analysis of lesional skin revealed downregulation of inflammatory mediators (S100A7, S100A8, S100A9, IL-1β, IL-6) and suppression of STAT3 signaling in Tcn2-/- mice. In parallel, TCN2-knockdown HaCaT cells exhibited impaired proliferation due to G1-phase arrest, along with reduced expression of proinflammatory factors. Together, these findings demonstrate that TCN2 promotes keratinocyte hyperproliferation and amplifies inflammatory responses in psoriasis. In conclusion, this study identifies TCN2 as a previously unrecognized regulator of psoriatic inflammation and keratinocyte biology, highlighting its potential as a novel therapeutic target. - Source: PubMed
Xu Jing-KaiZhou Xin-ZhuXue KeLi AngXia Qing-YueZhuang ZhouSong Xue-JiaoZuo Xian-BoCui Yong - The functional roles of the S100 protein family in colorectal cancer (CRC) are enigmatic, marked by widespread dysregulation but limited prognostic utility. This heterogeneity obscures their potential as therapeutic targets. - Source: PubMed
Publication date: 2026/07/01
Raeisi HamidehSaeedi Niasar MahsaNazemalhosseini Mojarad EhsanErfanian NafisehKhanabadi BinazirSaghafi SamiraSafarpour HosseinSadeghi Amir - Intestinal fibrosis presents a major clinical challenge in Crohn's disease (CD) due to the lack of effective pharmacological interventions. The underlying mechanisms of intestinal fibrosis remain largely elusive. Reanalysis of the single-cell RNA-seq data from full-thickness CD tissue identifies a distinct profibrotic macrophage subset characterized by high S100A8 and S100A9 expression. CellChat analysis indicates strong communication between this S100A8/A9-high (S100A8/A9) macrophage subset and fibroblasts. Adoptive transfer of S100A8/A9 macrophages exacerbate intestinal fibrosis in mice with chronic dextran sulfate sodium (DSS)-induced colitis. Consequently, pharmacological inhibition of S100A8/A9 significantly ameliorates intestinal fibrosis in murine chronic colitis. Proteomic analysis further identifies murine CCL6 (mCCL6) as the key pro-fibrotic mediator secreted by S100A8/A9 macrophages, which acts via CC chemokine receptor 1 (CCR1) to regulate fibroblasts. Antibody blockade of mCCL6 alleviates established intestinal fibrosis in a DSS-induced colitis model. Mechanistically, S100A8/A9 macrophages drive mCCL6 production via STAT3 activation. Similarly, the human ortholog of CCL6, CCL15 (hCCL15), exerts pro-fibrotic effects on fibroblasts via the CCR1 receptor. Our findings reveal that targeting S100A8/A9 macrophage may be a therapeutic strategy against intestinal fibrosis in CD. - Source: PubMed
Publication date: 2026/06/29
Wang ShuWang JiayunLin JunjieYe ZipingZhou GeyujiaMa JingjingSun JunjianYu JiangZhang YingdiTang NanaJiao ChunhuaZhao XiaojingZhang Hongjie - S100A8/A9, a critical danger-associated molecular pattern, amplifies inflammatory responses and exacerbates myocardial ischemia-reperfusion injury (MIRI) through Toll-like receptor 4 (TLR4) signaling. Although S100A8/A9-TLR4-related signaling has been implicated in MIRI pathogenesis, effective pharmacological interventions for MIRI remain limited. - Source: PubMed
Publication date: 2026/06/18
Hao QianyingYue JiashuLi PingHe Qingyong - Human calprotectin (CP, S100A8/S100A9 oligomer, MRP8/MRP14 oligomer) is a metal-sequestering protein that contributes to nutritional immunity. Each human CP subunit contains a single Cys residue-Cys42 in S100A8 and Cys3 in S100A9-and recent reports have revealed that these residues can undergo disulfide bond formation resulting in a covalently linked heterodimer species, hereafter referred to as disulfide-linked CP (dslCP). Nevertheless, the biochemical and functional consequences of this intradimer disulfide linkage are largely unknown. Here, we report a robust reconstitution and purification protocol affording dslCP and present initial biochemical and functional evaluation of the protein. Our investigations demonstrate that dslCP undergoes Ca(ii)-dependent self-association to form heterotetramers, depletes multiple metals from bacterial growth media, and induces an iron-starvation response in diverse bacterial pathogens. The intradimer disulfide linkage exhibits a midpoint potential of -213 mV, indicating that it can become oxidized in the extracellular space. Studies of enzymatic disulfide bond reduction reveal that divalent cation binding renders dslCP a poor substrate for the thioredoxin system. Investigations of proteolytic stability show that the intradimer disulfide linkage in dslCP enhances the susceptibility of the protein scaffold to digestion by human neutrophil elastase and trypsin, supporting a model wherein oxidative post-translational modifications direct protein lifetime. Our work expands upon the known roles of post-translational modifications of CP and highlights the need for further studies to define how oxidative modifications regulate the structure, stability, and function of this important host-defense protein. - Source: PubMed
Publication date: 2026/06/04
Mollo AurelioCool Emma YSakar BaharGupta KusholNolan Elizabeth M