S100A12, human, recombinant, full length, 15N
- Known as:
- S100A12, H. sapiens, Rec., length, 15N
- Catalog number:
- 201SA12_N
- Category:
- -
- Supplier:
- ProtEra
- Gene target:
- S100A12 human recombinant full length 15N
Related genes to: S100A12, human, recombinant, full length, 15N
- Gene:
- S100A12 NIH gene
- Name:
- S100 calcium binding protein A12
- Previous symbol:
- -
- Synonyms:
- p6, MRP6, CGRP, CAAF1, CAGC, ENRAGE
- Chromosome:
- 1q21.3
- Locus Type:
- gene with protein product
- Date approved:
- 1997-10-30
- Date modifiied:
- 2018-05-02
Related products to: S100A12, human, recombinant, full length, 15N
Related articles to: S100A12, human, recombinant, full length, 15N
- S100A12 as an indispensable molecular components inflammatory cytokines in human physiology. Notably, similar pathological mechanisms involving chronic low-grade inflammation are also observed in intervertebral disc degeneration (IVDD) and osteoporosis (OP), making the interplay between these diseases and inflammatory cytokines indisputable. Nevertheless, the precise identity of cytokines that concurrently fuel IVDD and OP remains elusive, hindering targeted therapeutic strategies. - Source: PubMed
Publication date: 2026/04/09
Wang ZexinChen BinLiu ZhenchuanZhang YuanqiangHan Leixiang - IgA vasculitis (IgAV) is a small-vessel vasculitis characterized by immune complex deposition, neutrophil activation, and endothelial injury. S100 proteins are recognized mediators of inflammation and vascular damage; however, their specific biological and clinical relevance in IgAV remains incompletely understood. - Source: PubMed
Publication date: 2026/03/25
Podraza ZofiaZłotnik-Szwech EmiliaMizerska-Wasiak Małgorzata - Joint use of multiple molecular layers can be useful to prioritize targets for mechanistic studies. Application of coronary disease in large populations is an emerging field. - Source: PubMed
Publication date: 2026/04/02
El-Sabawi BassimHuang XiaoningLin PhillipAnwar Mohammad YaserBetti MichaelKim NamjuPerry Andrew SPerera B Lakshitha AGajjar PriyaColangelo Laura AAmancherla KaushikSheng QuanhuZhao ShilinStolze LindsayFarber-Eger EricLandman Joshua MMiller Patricia ELiu Gabrielle YDas SumanWells Quinn STerry James GLloyd-Jones DonaldDas SaumyaKhan Sadiya SNorth Kari EBelow JenniferNayor MatthewKalhan RaviCarr John JeffreyGamazon Eric RShah Ravi V - High Mobility Group Box 1 (HMGB1) and Procathepsin L (pCTS-L) are crucial inflammatory mediators, yet their immunomodulating properties in human immune cells have not been systematically compared. This study employed RNA-sequencing to comparatively analyze their transcriptional effects on primary human peripheral blood mononuclear cells (PBMCs). Our findings demonstrate that while both mediators elicited significant transcriptional changes indicative of robust inflammatory responses, HMGB1 consistently induced a more extensive and diversified inflammatory program. Specifically, at a lower concentration of 0.5 µg/ml, HMGB1 triggered nearly four times more differentially expressed genes (DEGs) than pCTS-L (2.0 µg/ml). Despite this quantitative difference, an overlap of 412 DEGs (272 upregulated, 140 downregulated) revealed shared core inflammatory pathways, including the extensive upregulation of pro-inflammatory cytokines (e.g., IL1A, IL1B, and IL6), chemokines (e.g., CCL2 and CXCL1), and S100 proteins (e.g., S100A8, S100A9, and S100A12). Both mediators also converged on activating the non-canonical NF-κB pathway, evidenced by NFKB2 and RELB upregulation, suggesting a common underlying regulatory mechanism. Notably, HMGB1 uniquely upregulated CASP4 and CASP5-key components of the non-canonical inflammasome pathway-and a broader spectrum of cytokines and chemokines (e.g., IL23A, CXCL5). These findings delineate the distinct yet overlapping roles of HMGB1 and pCTS-L in orchestrating immune responses, offering a foundation for targeted therapeutic development for inflammatory diseases. - Source: PubMed
Publication date: 2026/03/16
Lou LiQiang XiaolingZhu Cassie ShuXiong BrianChen WeiqiangLi JianhuaTracey Kevin JWang Haichao - Invasive pulmonary aspergillosis (IPA) is a severe deep-seated fungal infection caused by of the genus . In recent years, its global incidence has shown a marked upward trend, posing a serious threat especially to immunocompromised patients, such as hematopoietic stem cell transplant recipients, cancer patients undergoing chemotherapy, and individuals on long-term glucocorticoid therapy. The core clinical dilemmas lie in the difficulty of early diagnosis and the narrow therapeutic window. Currently used clinical diagnostic indicators, including the galactomannan (GM) assay, (1,3)-β-D-glucan(G) assay, and imaging examinations, suffer from insufficient sensitivity or specificity, while traditional microbiological detection methods have a relatively long turnaround time. S100 calcium-binding protein A12 (S100A12) and Pentraxin 3 (PTX3) are both key molecules in the innate immune response of the human body, playing central roles in the immune regulation of infectious diseases. Recent studies have demonstrated that both molecules are abnormally expressed in IPA patients and may participate in the processes of infection recognition, immune clearance, and inflammatory regulation through synergistic effects, thereby providing new directions for the early diagnosis, disease assessment, and targeted therapy of IPA. This review will systematically elaborate on the molecular characteristics of S100A12 and PTX3, explore their synergistic mechanism and combined diagnostic value in IPA, and analyze their prospects for clinical application. - Source: PubMed
Publication date: 2026/03/05
Zhou Xiao-LianHu Xiao-BoLiu Hui