a1AT ELISA kit
- Known as:
- a1AT Enzyme-linked immunosorbent assay test reagent
- Catalog number:
- DL-a1AT-Hu
- Product Quantity:
- 96T
- Category:
- Elisa Kits
- Supplier:
- WDSTD
- Gene target:
- a1AT ELISA kit
Related genes to: a1AT ELISA kit
- Gene:
- SERPINA1 NIH gene
- Name:
- serpin family A member 1
- Previous symbol:
- PI
- Synonyms:
- AAT, A1A, PI1, alpha-1-antitrypsin, A1AT, alpha1AT
- Chromosome:
- 14q32.13
- Locus Type:
- gene with protein product
- Date approved:
- 1986-01-01
- Date modifiied:
- 2016-10-05
Related products to: a1AT ELISA kit
Human ELC ELISA KIT 96 TEST
OxiSelect In Vitro ROS/RNS Assay Kit (Green Fluorescence), Trial Size
OxiSelect Methylglyoxal (MG) Competitive ELISA Kit
OxiSelect Methylglyoxal (MG) Competitive ELISA Kit
OxiSelect TBARS Assay Kit (MDA Quantitation), Trial Size
OxiSelect Total Antioxidant Capacity (TAC) Assay Kit, Trial Size
OxiSelect™ In Vitro ROS RNS Assay Kit (Green Fluorescence), Trial Size(1-3)-beta-D-glucan Sandwich ELISA, Double Antibody(1-Kit )11,12-EET DHET Immunoassay Kit(1-Kit )11,12-EET_DHET Immunoassay Kit(1-Kit) 11,12-DHET Immunoassay Kit(1-Kit) 14,15-DHET Human Urine ELISA Kit(1-Kit) 14,15-DHET Hypertension ELISA Kit(1-Kit) 14,15-DHET sEH activity ELISA Kit(1-Kit) 14,15-EET DHET Hypertension ELISA Kit Related articles to: a1AT ELISA kit
- Alpha-1 antitrypsin (AAT), encoded by the SERPINA1 gene, is primarily synthesized in the liver and secreted into the blood. The SERPINA1 Z allele encodes Z-AAT (Glu342Lys), a variant that self-associates into polymers that are retained in hepatocytes and trigger inflammation and hepatic injury. Targeting and preventing Z-AAT polymerization allows a therapy to directly address the pathophysiology of AAT deficiency (AATD) associated liver disease. - Source: PubMed
Publication date: 2026/05/01
Handyside BrittaWenzel HeatherMackenzie DonaldChang CatherineGreenslade AnnieVan Vleet JeremyHeglar BrianChen Joseph CZhang LeningLarimore KevinZhou HuiyuTrantcheva IvaSims LawrenceEvans KristinFong SylviaKumar GyanendraAnnu KavyaRonzoni RiccardoIrving James AWang BingBunting StuartLomas David A - Patients with alpha-1 antitrypsin deficiency (AATD) have a 20- to 50-fold higher risk of developing primary liver cancer (PLC), such as hepatocellular carcinoma (HCC), in both cirrhotic and noncirrhotic livers, highlighting AATD as a potential oncogenic factor. In this exploratory study, we aimed to describe the frequency and characteristics of AATD alleles in patients with HCC arising in noncirrhotic livers. - Source: PubMed
Publication date: 2026/04/03
Beaufrère AurélieLeon CelineDecreaker MariePossenti LaurentEvain ManonCoilly AudreySchneider Carolin VFeurer ZoéOdou Marie-FrançoiseBalduyck MalikaPayancé AudreySchneider Kai MBioulac PauletteBlanc Jean-FrédéricLe Bail BrigitteGuettier CatherineAmintas SamuelBouchecareilh Marion - Ferroptosis is a critical contributor to various cardiomyopathies; however, broad-spectrum endogenous inhibitors remain largely undefined. Although human alpha-1-antitrypsin (hAAT) exhibits cytoprotective properties, its involvement in cardiac ferroptosis remains unexplored. To directly assess endogenous hAAT function in vivo, we generated CRISPR/Cas9-mediated humanized knock-in mouse models expressing either functional (SERPINA1) or loss-of-function (SERPINA1) hAAT, and subjected them to doxorubicin-induced cardiomyopathy and myocardial infarction. SERPINA1 mice exhibited robust protection against cardiac dysfunction, fibrosis, and remodeling, whereas SERPINA1 mice conferred no benefit, establishing that protection is strictly dependent on functional protein integrity. This protective effect was mediated through potent suppression of ferroptosis, as evidenced by reduced lipid peroxidation and iron accumulation. Mechanistically, endogenous hAAT activated the Nrf2 signaling pathway, upregulating key anti-ferroptotic effectors including GPX4, HO-1, and xCT; this protection was abolished by the Nrf2 inhibitor ML385. Our findings identify functional hAAT as a novel, broad-spectrum ferroptosis inhibitor operating through the Nrf2/GPX4 axis, highlighting its potential as a therapeutic target for diverse ferroptosis-driven cardiomyopathies. - Source: PubMed
Publication date: 2026/04/24
Li YanxiaoChen HongxiaAbudouwayiti AihaidanTang BoJiang ZhihuiPan YingWen ZhiyingTuerhongjiang GulinigaerGao WeitongGuo XiaoxiaHe ShuangshuangJiang WenhanZhang JinyingXie XiangZheng Yingying - Individuals homozygous for the "Z" mutation with alpha-1 antitrypsin deficiency (AATD) are highly susceptible to emphysema. This predisposition has classically been attributed to a relative deficiency of circulating alpha-1 antitrypsin (AAT) reaching the lungs and associated protease-antiprotease imbalance. Accumulating evidence suggests that the presence of misfolded Z-AAT protein either in the circulation, the lung interstitium, or within resident lung cells could contribute to emphysema pathogenesis. We have shown that type 2 alveolar epithelial cells (AT2s), progenitor cells of the lung alveolus, heterogeneously retain Z-AAT and exhibit a transcriptional disease signature in AATD patient samples. However, a lack of model systems that faithfully recapitulate AT2 biology and associated Z-AAT expression has limited our ability to study this phenomenon. Here, we apply syngeneic induced pluripotent stem cell-derived AT2s (iAT2s) and a novel mouse model featuring AT2-specific inducible human expression to interrogate the cell-instrinsic consequences of Z-AAT expression, validating findings in an independent dataset of human COPD lung tissue comparing ZZ to MM genotypes. We find further evidence of Z-AAT retention within AT2s and identify shared AT2 transcriptomic disease signatures conserved across model systems, characterized by innate immune and inflammatory signaling, NF-κB activation, and endoplasmic reticulum stress. Mice with AT2-specific Z-AAT expression additionally demonstrate increased susceptibility to elastase-induced emphysema, providing functional evidence for AT2-intrinsic contributions to AATD-associated lung disease. Within iAT2s, a subpopulation of Z-AAT expressing cells exhibits activation of the PERK-eIF2α signaling axis and markers of an alveolar basal intermediate (ABI) state, emerging cell-autonomously in the absence of mesenchymal co-culture. Together, these data provide evidence that Z-AAT expression in AT2s induces heterogenous cell-intrinsic stress responses including proteotoxic stress, inflammatory signaling, and aberrant cell fate adoption, and is sufficient to result in predisposition to injury, supporting a potential contribution of AT2-intrinsic Z-AAT toxicity to human AATD-associated emphysema pathogenesis. - Source: PubMed
Publication date: 2026/04/08
Merritt CarlyGriffin Rose PAbo Kristine MKaserman Joseph EBawa Pushpinder SinghMartin Carlos VillacortaWang FeiyaMorley MichaelCho MichaelBasil Maria CSauler MaorWilson Andrew A - Contrast-induced acute kidney injury (CI-AKI) is a major cause of hospital-acquired AKI, but its molecular pathogenesis remains incompletely understood. In this study, we used quantitative 4D proteomics, integrating ion mass-to-charge ratio (m/z), retention time, ion intensity, and ion mobility, to profile renal tissues from a novel rat CI-AKI model based on renal venous congestion and contrast exposure, with sham-operated rats as controls. Differentially expressed proteins were identified and analyzed using pathway enrichment and protein-protein interaction (PPI) network approaches, followed by experimental validation. Using nominal screening criteria (|log2FC| ≥ 1.5 and < 0.05), we identified 180 candidate differentially expressed proteins, including 92 upregulated and 88 downregulated proteins. Pathway-level analyses showed coordinated upregulation of complement-related proteins, including C3/C5 convertase-related components and terminal pathway proteins, such as C9, together with a C4 isoform annotated as C4a in the reference database. Coagulation and fibrinolysis pathways were also markedly altered, including fibrinogen chains (FGA, FGB, FGG), PLAU, SERPINA1, and SERPINF2. In contrast, proteins associated with AMPK and MAPK signaling (including HNF4α, PRKAA2, PRKAB1, and MAP2K3) were reduced. These pathway-level changes were supported by RT-qPCR and immunohistochemical analyses. Collectively, our findings support a multidimensional injury network in rat CI-AKI involving complement activation, coagulation-fibrinolysis dysregulation, and impaired metabolic/stress-response signaling, and provide a proteomic resource for future mechanistic and translational studies. - Source: PubMed
Publication date: 2026/04/14
Yang QiangSun LimingZhang ZhijianYan ZhixinZhang JianHu JiachangDing Xiaoqiang