Recombinant Human CAPN2
- Known as:
- Recombinant Human CAPN2
- Catalog number:
- CG02
- Product Quantity:
- 10ug
- Category:
- -
- Supplier:
- Novoprotein
- Gene target:
- Recombinant Human CAPN2
Related genes to: Recombinant Human CAPN2
- Gene:
- CAPN2 NIH gene
- Name:
- calpain 2
- Previous symbol:
- -
- Synonyms:
- mCANP, CANPml, CANPL2
- Chromosome:
- 1q41
- Locus Type:
- gene with protein product
- Date approved:
- 1989-06-30
- Date modifiied:
- 2016-10-05
Related products to: Recombinant Human CAPN2
Related articles to: Recombinant Human CAPN2
- Mitochondrial dysfunction and dysregulated proteolysis drive Huntington's disease (HD), tauopathy, and related neurodegenerative disorders. Calpain-2, a Ca-activated protease restrained by calpastatin (CAST), is pathologically overactivated, yet no therapies directly target this axis. We identify A36, a brain-penetrant small molecule derived from CHIR99021 that selectively stabilizes the CAST-calpain-2 complex without inhibiting GSK3. A36 acts as a protein-protein interaction stabilizer, enhancing CAST-calpain-2 binding, preventing CAST degradation, and thereby limiting calpain-2 activation and mitochondrial damage. In patients with HD induced pluripotent stem cell-derived neurons and mutant mouse striatal neurons, A36 normalized mitochondrial morphology and membrane potential, reduced oxidative stress, and improved survival. In vivo, A36 displayed favorable pharmacokinetics and central nervous system exposure; treatment reduced striatal neurodegeneration, mutant huntingtin aggregation, and motor deficits in HD R6/2 mice, and lowered phosphorylated tau, neuroinflammation, and cognitive decline in tauopathy PS19 mice. These findings establish pharmacological stabilization of CAST-calpain-2 as a therapeutic strategy and position A36 as a mechanism-selective modulator with broad neurodegenerative disease potential. - Source: PubMed
Publication date: 2026/03/27
Hu DiSun XiaoyanShang YutongLundberg KathleenAdams Drew JQi Xin - Pulmonary fibrosis represents a progressive interstitial lung disease marked by excessive extracellular matrix deposition and architectural distortion. Vascular endothelial cells critically contribute to fibrogenesis through paracrine secretion of pro-fibrotic mediators, yet their mechanobiological regulation remains elusive. Using integrated single-cell multi-omics profiling of human pulmonary fibrosis specimens and experimental fibrosis models induced by bleomycin or silica, we identify mechanosensitive Piezo1 upregulation in Endothelial cells as a hallmark of fibrotic progression. Endothelial-specific Piezo1 knockout significantly attenuates Bleomycin-induced fibrotic remodeling in male mice, establishing its pathogenic necessity. Mechanistically, PIEZO1 activation promotes pulmonary fibrosis development via CAPN2-mediated STAT3 phosphorylation, which may regulate the secretion of the pro-fibrotic molecule interleukin-33. These findings suggest that the endothelial PIEZO1-CAPN2-STAT3-IL33 axis is a potential therapeutic target for PF intervention. - Source: PubMed
Publication date: 2026/03/20
Zhang LanlanGui XuezhenHou RuijieJia LipingXia ShuZhang XinFu YingyunMeng Qian-FangLuo QunShi XingGuo BingxinLiang RuifangYue LudanChen XueXu HaizhaoWang PengboTong XiaLiu LujieWang LingweiLi BaicunChen ZiZhou LinfuZhang LinshuChen RongchangSun ChangbinXu WeiRao LangZhou HaiboDing Bi-SenChen Shanze - The gut-lung axis contributes to the progression of chronic obstructive pulmonary disease (COPD) by impairing intestinal barrier integrity and exacerbating systemic inflammation. Bufei Jianspi Formula (BJF), a traditional Chinese medicine, has been shown to improve lung function and alleviate gastrointestinal symptoms in patients with COPD, thereby enhancing their quality of life. - Source: PubMed
Publication date: 2026/02/26
Wang KunTao LiuyingZhang QinLiu LanShan BaixiZhao PengLi Jiansheng - The increasing accumulation of nanoplastics (NPs) in marine environment poses significant ecological and economic risks, particularly for commercially important species such as abalone (Haliotis discus hannai). This study investigated the effects of dietary polystyrene NPs (0,1, 10 and 100 mg/kg) on abalone over a 21-day exposure period, and the groups were designated as control, NPs1, NPs10 and NPs100, respectively. Results demonstrated that NPs impaired antioxidant capacity, as evidenced by elevated malondialdehyde (MDA) levels in cell-free hemolymph (1.83-fold higher in the NPs100 group than in control), together with reduced superoxide dismutase activity, decreased total antioxidant capacity, and inhibition of the Keap1/Nrf2 pathway. Immune suppression was observed through decreased lysozyme and acid phosphatase activities. Muscle texture deterioration was observed (muscle hardness decreased to 0.42-fold of the control level in NPs100 group), which was associated with reduced protein content, inhibition of the mTOR pathway, and upregulation of proteolytic genes (capn1, capn2, ctsl and ctsb). In the digestive gland, NPs induced lipid accumulation (increased to 1.20-fold of the control level in the NPs100 group), accompanied by suppressed lipolysis-related genes (atgl, hsl, cpt-1 and acox) and enhanced lipogenesis-related genes (srebp-1c, acc and scd) expression. Additionally, NPs upregulated inflammation-related genes (myd88, nf-κb, tnf-α and il-17) and apoptosis-related proteins (BAX, CytC and cleaved caspase-3), along with histopathological changes and reduced digestive enzyme activities. These findings indicate that NPs impair abalone health and muscle quality through oxidative stress, metabolic disruption, apoptosis and protein turnover. Primary adverse effects were mainly observed at ≥10 mg/kg after 21 days, with the most pronounced responses at 100 mg/kg. The mTOR, NF-κB, and Bax/caspase-3 signaling pathways were the main targets of the biological effects induced by NPs. - Source: PubMed
Publication date: 2026/01/26
Zhang JipingFu QiyuanCheng SisiRen HaiMu YeLiu Jiahuan - SPG76 is a complicated form of hereditary spastic paraplegia (HSP) associated with mutations in the CAPN1 gene. The encoded protein, calpain 1, is a calcium-activated cysteine protease that catalyzes the proteolytic cleavage of a variety of cellular proteins and is involved in a wide range of biological processes. Calpain 1 and calpain 2 isoforms are highly expressed in various tissues and have opposite effects on survival: calpain 1 induces the activation of Akt and ERK pro-survival pathways, regulates autophagy and is neuroprotective, while calpain 2 induces neurodegeneration. We characterized fibroblast cells derived from two SPG76 patients carrying a homozygous mutation (p.Tyr320Leufs73*) in the CAPN1 gene that leads to the absence of the protein. Loss of calpain 1 in SPG76 patient's derived cells increased calpain 2 activation and induced autophagosome formation and accumulation, inhibited Akt and ERK1/2 pro-survival pathways, reducing GSK3β inhibition, and increased cell susceptibility to ER stress. In ER stress conditions, SPG76 cells presented unfolded protein response (UPR) activation, increased apoptosis and cell death. We analysed the potential of targeting calpain 2 and the Akt pro-survival pathway to rescue the SPG76 deranged pathways in patient's derived cells. We found that the calpain inhibitors olesoxime and MDL28170, naringenin and the GSK3β inhibitor tideglusib were the most effective in increasing Akt activation and GSK3β inhibition and in rescuing apoptosis and cell death in SPG76 cells. Among these, olesoxime and MDL28170 reduced calpain activity, rescued apoptosis and locomotor deficits in vivo in a CalpB KO Drosophila model that replicates the SPG76 phenotype. - Source: PubMed
Publication date: 2026/01/29
Brivio FrancescaGuarato GiuliaPanzeri ElenaManganelli FioreFilosto MassimilianoVantaggiato ChiaraBassi Maria Teresa