CAPNS1 ELISA kit
- Known as:
- CAPNS1 Enzyme-linked immunosorbent assay test reagent
- Catalog number:
- DL-CAPNS1-Hu
- Product Quantity:
- 96T
- Category:
- Elisa Kits
- Supplier:
- WDSTD
- Gene target:
- CAPNS1 ELISA kit
Related genes to: CAPNS1 ELISA kit
- Gene:
- CAPNS1 NIH gene
- Name:
- calpain small subunit 1
- Previous symbol:
- CAPN4
- Synonyms:
- CANP, CANPS, 30K, CDPS
- Chromosome:
- 19q13.12
- Locus Type:
- gene with protein product
- Date approved:
- 1989-06-30
- Date modifiied:
- 2016-10-05
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- Androglobin (ADGB), a protein essential for spermatogenesis, is one of the most structurally unusual members of the vertebrate globin superfamily. It combines a calpain-like domain with a circularly permuted globin domain containing an embedded calmodulin-binding IQ motif, an architecture suggesting complex regulatory functions that remain poorly understood. Here, we investigated whether ADGB undergoes calcium-dependent post-translational processing, as described for other calpains. ADGB displayed a characteristic proteolytic processing pattern following calcium stimulation, generating several stable cleavage products following ectopic expression in mammalian cells. In vitro proteolysis assays demonstrated that ADGB cleavage requires cytoplasmic factor(s) and is enhanced by Ca. Broad protease inhibitors with activity against calpains reduced ADGB processing, whereas the more selective inhibitor PD150606 and siRNA-mediated depletion of CAPN1 or CAPN2 did not substantially affect cleavage, arguing against these classical calpains as its principal mediators. In contrast, CAPNS1 downregulation reduced calcium-dependent ADGB processing in both cellular and cell-free assays, indicating a contribution of CAPNS1 without establishing a direct role in the proteolytic reaction. Domain-mapping analyses localized major cleavage regions between the N-terminal calpain-like and globin-containing regions of ADGB. The experimentally isolated globin domain displayed enhanced interaction with calmodulin compared with full-length ADGB, and preferential localization to centrosomal structures. Collectively, these findings identify calcium-dependent cytoplasmic proteolytic processing as a previously unrecognized property of ADGB and suggest that such processing may influence the biochemical accessibility and cellular behavior of its constituent domains. - Source: PubMed
Publication date: 2026/09/18
Koay Teng WeiOsterhof CarinaClerc AngèleHoogewijs David - Neuronal Intranuclear Inclusion Disease (NIID) is caused by GGC repeat expansions in the 5' untranslated region of the notch 2 N-terminal like C (NOTCH2NLC) gene. An upstream open reading frame within the mutant transcript produces the NOTCH2NLC upstream open reading frame-derived polyglycine protein (uN2CpolyG) containing expanded polyglycine (polyG), which forms intranuclear inclusions. Although uN2CpolyG is thought to play a critical role in disease pathogenesis, the mechanisms underlying its toxicity and inclusion formation remain incompletely understood. In this study, we first expressed a pure GGC repeat encoding polyG in Neuro2a cells and identified aggregate-associated proteins by mass spectrometry. We then confirmed the formation of intracellular aggregates using both transient expression and drug-inducible expression systems for uN2CpolyG. Among the proteins identified by mass spectrometry, Calpain small subunit 1 (Capns1), the regulatory subunit of calpain, was found to be sequestered into uN2CpolyG aggregates. Notably, the N-terminus of Capns1 contains a glycine-rich sequence, which mediated its co-aggregation with uN2CpolyG. Furthermore, knockdown of Capns1 appeared to reduce the accumulation of uN2CpolyG aggregates. Collectively, these findings identify Capns1 as a potential modifier of NIID pathology. - Source: PubMed
Kubokawa ArisaOhki AiOno RisaAraki MakotoYanaizu MotoakiKino Yoshihiro - Dysregulated calpains and cathepsins contribute to adverse cardiac remodeling following chronic pathological stress, but their interplay and the specific contributions of the classical calpain isoforms remain undefined. Here, we tested whether calpain-2 initiates a lysosome-cathepsin proteolytic axis that promotes pathological hypertrophy through mTORC1-dependent signaling. - Source: PubMed
Publication date: 2026/08/07
Martí-Boltaina AnnaAluja DavidDelgado-Tomás SaraMiró-Casas ElisabetRodriguez-Lecoq RafaelRuiz-Meana MarisolRodriguez-Sinovas AntonioBenito BegoñaGarcia-Trevijano ElenaGutierrez-Calabres ElenaBaudry MichelBarrabés José AFerreira-González IgnacioInserte Javier - Alzheimer's disease (AD), a progressive neurodegenerative disorder characterized by brain atrophy and cognitive decline. While the amyloid cascade hypothesis remains the dominant framework, accumulating evidence indicates that mitochondrial dysfunction critically contributes to AD progression. Although improving mitochondrial function has been shown to rescue cognitive deficits in AD models, the underlying molecular mechanisms remain elusive. In this study, we identified a significant reduction in calpain small subunit 1 (CAPNS1) expression in both AD patient samples and male transgenic mouse models. Decreased CAPNS1 levels were strongly correlated with mitochondrial ultrastructural damage, reduced mitochondrial DNA (mtDNA) copy number, and progressive synaptic loss. Mechanistically, we found that CAPNS1 positively regulated mtDNA transcription and mitochondrial gene expression, and pharmacological data suggested the involvement of the Ca-CaMKIIβ-MAPK-PGC-1α signaling axis, a master pathway governing mitochondrial biogenesis and respiratory capacity. This activation subsequently restored cellular ATP production and reduced mitochondrial reactive oxygen species accumulation. Importantly, neuronal-specific CAPNS1 upregulation in APP/PS1 transgenic mice markedly improved mitochondrial cristae integrity, reversed hippocampal long-term potentiation deficits, increased dendritic spine density, and partially alleviated spatial memory deficits in behavioral tests. We noted that loss-of-function experiments (e.g., CAPNS1 knockdown or knockout) were not performed in this study, and the proposed Ca-CaMKIIβ-MAPK-PGC-1α axis should therefore be interpreted as a suggestive working model requiring further validation. Collectively, our findings indicate that CAPNS1 serves as a key regulator of mitochondrial function. By linking Ca signaling to mitochondrial gene expression and synaptic integrity, CAPNS1 represents a promising therapeutic target for ameliorating synaptic loss and cognitive decline in AD. - Source: PubMed
Publication date: 2026/07/11
Han JialinWu ShuangCui XiaolinZhou XinyiYu QianCheng QianLu ZhimingZong Shuai - Calpains are a family of 15 calcium-activated cysteine proteases that have emerged as potential antimetastatic targets in breast cancer. Calpain-1 and calpain-2 are ubiquitously expressed heterodimers composed of unique catalytic subunits (encoded by and , respectively) and a common regulatory subunit (encoded by ). Genetic disruption of abolishes calpain-1 and calpain-2 activity. Using CRISPR-Cas9 mediated knockout, we validated calpains-1/2 as promising therapeutic targets in a mouse model of mammary carcinoma. knockout impaired cell invasion by 53 ± 10% and reduced lung metastasis by 68 ± 12% in an orthotopic engraftment mouse model. - Source: PubMed
Publication date: 2026/06/09
Harper DanielleShapovalov IvanCockburn SamanthaAaron AnyaGao YanGreer Peter A