S100A10, human, recombinant, full length
- Known as:
- S100A10, H. sapiens, Rec., length
- Catalog number:
- 201SA10
- Product Quantity:
- 100ug
- Category:
- -
- Supplier:
- ProtEra
- Gene target:
- S100A10 human recombinant full length
Related genes to: S100A10, human, recombinant, full length
- Gene:
- S100A10 NIH gene
- Name:
- S100 calcium binding protein A10
- Previous symbol:
- ANX2LG, CAL1L
- Synonyms:
- P11, 42C, CLP11
- Chromosome:
- 1q21.3
- Locus Type:
- gene with protein product
- Date approved:
- 1992-09-10
- Date modifiied:
- 2018-05-02
Related products to: S100A10, human, recombinant, full length
Related articles to: S100A10, human, recombinant, full length
- We previously demonstrated that patients with scleroderma or systemic sclerosis (SSc) have elevated autoreactive transitional B cells, including against topoisomerase I (anti-topoisomerase I autoantibody [ATA]). This suggests that defective transitional B cell tolerance could drive autoimmunity in SSc. To investigate this, we used single-cell transcriptomic and B cell receptor (BCR) sequencing on sorted transitional B cells from treatment-naive SSc patients and healthy controls (HCs). Four transitional B cell clusters were identified as T1, T2, CD27, and marginal zone precursors (MZPs). T1 B cells were significantly expanded in SSc with a 2-fold increase compared with HCs. Additionally, pro-survival genes (IL4R, TCL1A, and S100A10) and IFN-responsive genes (IFITM1 and IFITM2) were upregulated in SSc. BCR analysis revealed increased complementarity determining region 3 (CDR3) hydrophobicity and altered κ/λ ratios with proximal Jκ gene usage in the SSc patients. Collectively, our findings support divergent transitional B cell development and activation in SSc with an AKT-driven pathway likely promoting autoreactive transitional B cell survival. - Source: PubMed
Publication date: 2026/09/15
Beesley ClaireGoldman NinaGabernet GiselaAron EdelÇubuk CankutLewis Myles JJames Louisa KYaari GurKleinstein Steven HAbraham David JDenton Christopher PMageed Rizgar AOng Voon - - Source: PubMed
Publication date: 2026/08/07
Waisman David M - Immune evasion in hepatocellular carcinoma (HCC) represents a major biological barrier limiting the efficacy of immunotherapy, yet its molecular basis remains incompletely understood. Increasing evidence indicates that tumor metabolic reprogramming and ferroptosis-related signaling play critical roles in shaping an immunosuppressive tumor microenvironment (TME); however, the specific regulatory factors involved remain unclear. This study aims to systematically elucidate the functional role of S100 calcium-binding protein A10 (S100A10) in immune evasion in HCC, with a particular focus on the molecular mechanisms by which S100A10 regulates CD8 T-cell exhaustion through arachidonic acid (AA) metabolism and ferroptosis, as well as its potential therapeutic implications. To this end, data from The Cancer Genome Atlas Liver Hepatocellular Carcinoma (TCGA-LIHC) cohort are integrated to analyze the expression patterns of S100A10, its prognostic value, and its association with the immune microenvironment. S100A10 overexpression and knockout models are established in HCCLM3 and MHCC97L cell lines, and S100A10-mediated metabolic pathway reprogramming is characterized using transcriptomic profiling, untargeted metabolomics, and ferroptosis-related functional assays. In parallel, single-cell RNA sequencing (scRNA-seq) and spatial transcriptomics are employed to delineate the cell-type specificity and spatial distribution of S100A10. Furthermore, human CD8 T-cell co-culture systems and orthotopic mouse HCC models are used to evaluate the impact of S100A10 on immune function and responsiveness to anti-programmed cell death protein 1 (anti-PD-1) therapy. The results demonstrate that S100A10 is significantly upregulated in HCC and is closely associated with poor prognosis and an immunosuppressive state. Mechanistically, S100A10 activates cytosolic phospholipase A-arachidonate 5-lipoxygenase (cPLA-5-LOX)-mediated AA oxidative metabolism, leading to the accumulation of lipid peroxidation products and ferroptosis-associated signals, thereby driving CD8 T-cell exhaustion and promoting immune evasion. Significantly, inhibition of S100A10 reshapes the tumor immune microenvironment (TIME) and enhances the therapeutic efficacy of anti-PD-1 treatment. Collectively, these findings identify S100A10 as a critical regulator of metabolic-immune coupling in HCC and provide a theoretical basis for combinatorial strategies targeting metabolism and immunotherapy. - Source: PubMed
Publication date: 2026/09/13
Zhang JingxuWang GanggangZhou ZhijiePu BingbingZhang XinJi XinyuWang Xiaoliang - Astrocytes are significantly activated after peripheral nerve injury (PNI) and affect the nerve repair by mediating neuroinflammation. DJ-1 is highly expressed in astrocytes, and its binding compounds exert significant neuroprotective effects by regulating antioxidant and anti-inflammatory responses. This study is designed to investigate the therapeutic effects of DJ-1-binding compound P-DJ-1A in a rat PNI model induced by spared nerve injury (SNI) surgery. The results revealed that SNI surgery induced the aggregation of activated astrocytes and the phosphorylated form of STAT3 in the ipsilateral dorsal spinal horn (DSH), which was concentrated mainly in the projection area of the injured nerve. Moreover, SNI surgery led to the extensive induction of proinflammatory and neurotoxic mediators, including IL-1β, TNF-α, IL-6, IL-18, and C3, while reducing the expression of TGF-β, IL-10, and S100A10. Treatment with P-DJ-1A or AG490 alleviated mechanical hyperalgesia and thermal hyperalgesia induced by SNI surgery, reduced "A1" astrocyte activation, and inhibited the expression of proinflammatory cytokines but increased the levels of TGF-β, IL-10, and S100A10. Mechanistically, P-DJ-1A or AG490 inhibited STAT3 activation and the NF-κB/NLRP3/IL-18 pathway. Collectively, the DJ-1-binding compound P-DJ-1A can alleviate SNI-induced injury by modulating neurotoxic astrocyte activation and inhibiting neuroinflammation, highlighting its potential as a novel therapeutic strategy. - Source: PubMed
Publication date: 2026/09/10
Wang ShengtaoCai JieyongZhou QingsongZhao MingZhou Wei - Ceramide-1-phosphate (C1P), once considered a minor metabolic intermediate, is now recognized as a relevant regulator of cell survival, inflammation, migration, oxidative stress, glucose uptake and adipogenesis. These diverse functions are mediated by direct interactions between C1P and specific protein targets, including enzymes, lipid transfer proteins, and signaling effectors (typically proteins). While C1P was demonstrated to regulate a variety of signaling pathways, including phosphatidylinositol 3-kinase (PI3K)/Akt, mitogen-activated protein kinase kinase (MEK)/extracellularly regulated kinases (ERK) 1-2, or sphingomyelin synthase (SMS)/protein kinase-C-alpha (PKCα), this review namely focuses on the eight major proteins that directly interact with C1P: acidic sphingomyelinase (ASMase), serine palmitoyl transferase (SPT), Ca²⁺-dependent cytosolic phospholipase A 2 -alpha (cPLA 2 α), Gi protein-coupled receptors, C1P transfer protein (CPTP), sphingomyelinase phosphodiesterase like 3b (SMPDL3b), annexin A2-p11 (S100A10), and Kelch-like ECH-associated protein 1 (KEAP1). Understanding C1Pprotein interactions provides a conceptual framework for targeting sphingolipid signaling in inflammation, cancer and metabolic diseases. Here, we summarize current evidence for C1P binding or functional modulation of these proteins, and highlight the implications of these interactions in inflammation, oxidative stress control, and disease pathogenesis. - Source: PubMed
Publication date: 2026/09/09
Gomez-Muñoz AntonioBenito-Vicente AsierUribe Kepa BLarrea-Sebal AsierGomez-Larrauri AnaMartín César