Anti-Human CD85h (ILT1) PE 100 tests
- Known as:
- Antibody toHuman CD85h (ILT1) PE 100 tests
- Catalog number:
- 12-5119-42
- Category:
- -
- Supplier:
- eBioscience
- Gene target:
- Anti-Human CD85h (ILT1) 100 tests
Related genes to: Anti-Human CD85h (ILT1) PE 100 tests
- Gene:
- LILRA2 NIH gene
- Name:
- leukocyte immunoglobulin like receptor A2
- Previous symbol:
- -
- Synonyms:
- LIR-7, ILT1, CD85h, LIR7
- Chromosome:
- 19q13.4
- Locus Type:
- gene with protein product
- Date approved:
- 2000-01-11
- Date modifiied:
- 2016-01-14
- Gene:
- LILRA5 NIH gene
- Name:
- leukocyte immunoglobulin like receptor A5
- Previous symbol:
- LILRB7
- Synonyms:
- ILT11, LIR9, CD85, CD85f
- Chromosome:
- 19q13.42
- Locus Type:
- gene with protein product
- Date approved:
- 2005-04-14
- Date modifiied:
- 2016-10-05
- Gene:
- LILRP2 NIH gene
- Name:
- leukocyte immunoglobulin-like receptor pseudogene 2
- Previous symbol:
- -
- Synonyms:
- ILT10, CD85m
- Chromosome:
- 19q13.42
- Locus Type:
- pseudogene
- Date approved:
- 2005-05-17
- Date modifiied:
- 2015-01-30
- Gene:
- TRAK1 NIH gene
- Name:
- trafficking kinesin protein 1
- Previous symbol:
- -
- Synonyms:
- OIP106, KIAA1042, MILT1
- Chromosome:
- 3p22.1
- Locus Type:
- gene with protein product
- Date approved:
- 2005-12-13
- Date modifiied:
- 2016-05-16
Related products to: Anti-Human CD85h (ILT1) PE 100 tests
Related articles to: Anti-Human CD85h (ILT1) PE 100 tests
- : Genetic generalized epilepsies (GGE) often remit in childhood, yet a subset of adults remain pharmacoresistant with substantial morbidity. The genetic basis of adult pharmacoresistant GGE is poorly defined. This descriptive study used whole-genome sequencing (WGS) to identify recurrent coding variants and pathways associated with pharmacoresistant adult GGE. : WGS was performed in ten racially diverse adults (mean age 37.2 years; range 20-52) with electroencephalographically confirmed, pharmacoresistant GGE (mean onset 13.7 years). Analysis prioritized variants present in at least 80% of participants and which were either (i) missense variants predicted deleterious with ANNOVAR or (ii) loss-of-function variants predicted high-impact from snpEff. Pathway enrichment and overlap with a commercial clinical epilepsy gene panel were assessed. : Filtering identified 133 unique, deleterious coding variants across 69 genes shared by at least eight participants. Four genes (APOL4, KMT2C, SON, VDR) overlapped a clinical epilepsy panel, supporting the capacity of WGS to recover clinically relevant loci. Prioritized loci implicated gastrointestinal and metabolic regulators (e.g., MUC6, PNLIPRP2), chemosensory receptors (OR10D3, OR8U1, TAS2R19), neuroimmune mediators (LILRA2, SIGLEC12, OAS2), and ion transporters (KCNJ12, P2RX5, RHBG), consistent with multifactorial mechanisms of pharmacoresistance. : This exploratory WGS study focused exclusively on adults with pharmacoresistant GGE, revealing shared high-impact variants and convergent pathways spanning absorption/metabolism, vitamin D signaling, immunity, and ion transport. Findings broaden the genetic landscape of pharmacoresistant GGE while motivating validation in larger, multiethnic cohorts. - Source: PubMed
Publication date: 2026/05/14
Kidder Benjamin LXu JianGeng RuiDlugas HunterVavilikolanu AnushaChen WeiWasade Vibhangini S - Leukocyte immunoglobulin (Ig)-like receptors (LILRs) constitute a family of 11 structurally related receptors predominantly expressed on immune cells. Despite their functional diversity, LILRs show a high degree of sequence homology within their extracellular domains, with amino acid sequence identities ranging from approximately 50% to nearly 100%. This molecular similarity poses a significant challenge for antibody-based detection, often resulting in cross-reactivity and misinterpretation of expression profiles. Nevertheless, a comprehensive assessment of antibody specificity across the entire LILR family has not been previously conducted. In this study, we performed a rigorous validation of commercially available antibodies to evaluate their specificity and cross-reactivity against all LILR family members. Using flow cytometry with LILR-transfected K562 cells, we reliably identified specific antibodies for LILRA2, LILRA4, LILRA5, LILRB1, LILRB2, and LILRB4. Notably, more than half of the commercial antibodies showed cross-reactivity. Given the lack of a reliable antibody for LILRA3, the only known soluble member of the family, we generated novel anti-LILRA3 monoclonal antibodies in mice. Three hybridoma clones exhibiting high specificity for LILRA3 were successfully isolated and validated. Using these antibodies, we established a sensitive sandwich ELISA, which successfully detected LILRA3 in individuals carrying functional alleles, while no protein was detected in those with the 6.7-kb deletion or premature termination codons. Moreover, serum concentrations of LILRA3 were substantially higher than previously reported. These findings not only provide essential tools for accurate detection of LILRA3 but also underscore the importance of rigorous antibody validation in LILR-related research. - Source: PubMed
Publication date: 2026/04/30
Tanimoto HiromuNguyen Thi Thu ThaoHasegawa GenHashikawa YukoHanayama RikinariHirayasu Kouyuki - Liver inflammation is a key driver of nonalcoholic fatty liver disease (NAFLD) and its progressive subtype, nonalcoholic steatohepatitis (NASH). Macrophages, as central players in the innate immune response, are crucial to disease pathogenesis; however, the upstream events that initiate their activation remain poorly defined. Here, we employed a cell-based chimeric receptor screening system and identified CD1d as a surface ligand for PIRA2. We subsequently demonstrated that CD1d stimulation activated macrophages both in vitro and in vivo. Co-immunoprecipitation assays further confirmed a direct interaction between CD1d and PIRA2. Using Pira2-deficient (Pira2) mice, we observed significantly reduced hepatic inflammation and lipid accumulation compared to wild-type controls. Importantly, macrophage-specific Pira2 conditional knockout mice similarly exhibited reduced macrophage activation and inflammatory cytokine production in vivo, confirming a macrophage-intrinsic role of PIRA2. Mechanistically, CD1d-PIRA2 interaction involves the α1 and α2 domains of CD1d and the D1 and D2 domains of PIRA2, leading to FcRγ ITAM tyrosine phosphorylation and downstream inflammatory signaling-events that are impaired in Pira2 macrophages. Additionally, CD1d and LILRA2 protein levels were elevated in NAFLD patients, and CD1d stimulation induced proinflammatory cytokine expression in human macrophages, which was attenuated by LILRA2 blockade. A recombinant LILRA2/Fc fusion protein effectively blocked CD1d-induced inflammatory gene expression in human macrophages, highlighting its potential as a therapeutic strategy for NAFLD. Collectively, our findings identify CD1d as a functional ligand of PIRA2 that promotes macrophage activation and inflammation, contributing to inflammatory progression in NAFLD. - Source: PubMed
Publication date: 2026/04/27
Tan XiaoshengLi QingwenMa ZhiboSun LingjuanZhao XiangliChen JianlinWang JingzengWeng XiufangChen LiChen ZhishuiLan Peixiang - Type 2 diabetes mellitus (T2DM) is a prevalent metabolic disorder, and identifying robust biomarkers is crucial for improving diagnosis and understanding its pathogenesis. - Source: PubMed
Publication date: 2026/03/10
Cui FangqinLi LiHu MingjiLi BaoDu BangFang QingqingHuang DakeZhang Xiaonan - Human leukocyte immunoglobulin-like receptors (LILRs) are cell surface receptors that are mainly expressed in immune cells. LILRs are involved in immune cell regulation. As a member of the LILR family, LILRA2 was reported to recognize the bacterially N-terminus truncated Ig (N-truncated Ig) for the induction of innate immune response. Fibrinogen, which is enzymatically converted to fibrin and forms fibrin-based blood clots, was recently shown to activate LILRA2-expressing immune cells. However, the molecular mechanisms of LILRA2-fibrinogen interaction remain unclear. In this study, we investigated the molecular recognition of fibrinogen by LILRA2, using biophysical methods. Surface plasmon resonance (SPR) analysis showed that LILRA2 specifically bound to fibrinogen with a relatively low dissociation constant (K) (∼10 μM), like N-truncated Ig. Furthermore, we found that high-molecular-weight fibrinogen exhibited a high-affinity interaction with immobilized LILRA2 owing to significant avidity effects. Domain-deletion and site-specific mutagenesis successfully identified the crucial amino acids of domains two and four of LILRA2 for fibrinogen binding. On the other hand, the D regions of fibrinogen are responsible for binding to LILRA2. These results enabled us to build a reasonable model of the LILRA2-fibrinogen complex, which provides insights into the molecular recognition and therapeutic potential of LILR-mediated immune responses. - Source: PubMed
Publication date: 2026/02/12
Wang JiaqiFurukawa AtsushiChen LiuanSuzuki RyoArase HisashiHirayasu KouyukiMaenaka Katsumi