Polyclonal Rabbit CAMKK2 Antibody
- Known as:
- Polyclonal Rabbit CAMKK2 Antibody
- Catalog number:
- KA0517
- Product Quantity:
- 100ul
- Category:
- -
- Supplier:
- KareBay
- Gene target:
- Polyclonal Rabbit CAMKK2 Antibody
Related genes to: Polyclonal Rabbit CAMKK2 Antibody
- Gene:
- CAMKK2 NIH gene
- Name:
- calcium/calmodulin dependent protein kinase kinase 2
- Previous symbol:
- -
- Synonyms:
- CAMKK, KIAA0787, CAMKKB, MGC15254
- Chromosome:
- 12q24.31
- Locus Type:
- gene with protein product
- Date approved:
- 1999-08-27
- Date modifiied:
- 2016-06-08
Related products to: Polyclonal Rabbit CAMKK2 Antibody
Related articles to: Polyclonal Rabbit CAMKK2 Antibody
- AMP-activated protein kinase (AMPK) is a crucial regulator of cellular energy balance, affecting numerous downstream targets across various subcellular locations. Under cellular energy stress, AMPK becomes fully activated when it binds AMP and is phosphorylated by upstream kinases, including liver kinase B1 and calcium/calmodulin-dependent protein kinase kinase 2 (CaMKK2), and works to restore metabolic equilibrium. Additionally, CaMKK2 can activate AMPK independent of AMP in response to calcium signaling. In the present review, we summarize how genetically encoded kinase activity reporters for measuring AMPK activity have evolved for a comprehensive measurement of spatial and temporal AMPK activity in single cells. These reporters have provided important insights into AMPK activity dependent upon upstream kinases, location, and signaling cues. We also discuss the use of genetic actuators such as the AMPK inhibitory peptide that can be targeted to suppress AMPK activity at specific compartments. Together, these advances have established AMPK as a key regulator of metabolism with distinct spatial and temporal signaling patterns, suggesting compartmentalization of AMPK activity in the cell. - Source: PubMed
Jhawar ArnavParks KaseySchmitt Danielle L - This study explores the neuroprotective effects of Stanniocalcin-1 (STC1) in the context of ischemic stroke, a major cause of death and disability worldwide. Although STC1 is recognized for its cytoprotective properties, its role in cerebral ischemia/reperfusion (I/R) injury has not been fully characterized. Our objective was to clarify the effects and underlying mechanisms of STC1 using a mouse model of middle cerebral artery occlusion/reperfusion (MCAO/R). We administered recombinant human STC1 (rh-STC1) intranasally and assessed cerebral injury through various methods including neurological scoring, behavioral tests, and TUNEL/Nissl staining. Additionally, we evaluated markers of oxidative stress and ferroptosis. The results demonstrated that endogenous STC1 levels were decreased following ischemia. Treatment with rh-STC1 led to significant improvements in neurological function, reduction in infarct volume, and decreased permeability of the blood-brain barrier. Furthermore, rh-STC1 treatment mitigated neuronal apoptosis, oxidative stress, and ferroptosis. Mechanistically, rh-STC1 was found to interact with calreticulin (CRT), activating the CAMKK2/AMPK/GSK-3β/Nrf2 signaling pathway. Notably, the neuroprotective effects of rh-STC1 were abolished by an AMPK inhibitor. In conclusion, our findings indicate that rh-STC1 protects against cerebral I/R injury by inhibiting apoptosis and ferroptosis, primarily via the CRT/CAMKK2/AMPK/GSK-3β/Nrf2 pathway. This positions STC1 as a promising therapeutic target for ischemic stroke. - Source: PubMed
Publication date: 2026/05/06
Xu YunhaoLiu ChangLi JiachenMa YaoLi HongLi MeixuanLi ZongzeYao QilongWang ZhanyouLiang JiaWang Peng - Chronic kidney disease (CKD) is increasingly linked to environmental toxins, including the cyanobacterial toxin microcystin-LR (MC-LR), particularly in populations with pre-existing renal injury. We have previously demonstrated that MC-LR promotes CKD, however the full underlying mechanism remains poorly understood. This study investigated how MC-LR exacerbates adenine-induced kidney disease in animal models using an integrative multi-omics approach. Male Sprague-Dawley rats were assigned to four groups: control, MC-LR, adenine, and adenine + MC-LR. Histopathology showed that MC-LR alone caused only mild, focal interstitial inflammation and fibrosis, whereas adenine alone induced granulomatous interstitial nephritis with tubular atrophy and acute tubular necrosis. The most severe lesions were in the co-exposure group, with widespread tubular injury, dense granulomatous inflammation, and extensive interstitial fibrosis. Proteomic analysis revealed distinct clustering and overexpression of Ctss, Wipf3, and Hmgcs2 in kidney tissue from the co-exposure group, together with enrichment of pathways related to DNA repair, p53 signaling, and integrin-HMGB1 complexes. Urinary metabolomics and peptidomics revealed metabolic and peptide signatures associated with CAMKK2 signaling, Farnesyl CoQ10, ferroptosis, and immune activation. Integrative multi-omics analysis demonstrated strong cross-omics correlations, highlighting coordinated oxidative stress, mitochondrial dysfunction, ferroptosis, altered mitophagy, and fibrotic remodeling as key mechanisms of MC-LR-enhanced nephrotoxicity. Together, these findings show that even sub-toxic, environmentally relevant MC-LR exposure can amplify kidney injury through tightly interconnected metabolic and inflammatory networks. This work provides mechanistic insight into cyanotoxin-associated kidney disease and supports the need for stricter monitoring and prevention strategies in regions affected by harmful algal blooms. - Source: PubMed
Publication date: 2026/05/04
Kongsintaweesuk SuppakritIntuyod KittiRoytrakul SittirukSeubwai WunchanaSangkhamanon SakkarnCharoenlappanit SawanyaCha'on UbonSurapinit AchirawitThongpon PhonpilasTanasuka PakornkiatChomwong SasitornBlair DavidPinlaor SomchaiPinlaor Porntip - MRE11 safeguards genome stability at stalled replication forks, where its activity must be tightly controlled to prevent nascent strand DNA degradation (NSD). However, the upstream signaling mechanisms that limit NSD remain poorly defined. Here, we identify Ser649 (S649) as a previously unrecognized phosphorylation site that limits MRE11 association with stalled forks. We show that S649 phosphorylation is robustly induced by replication stress or elevated cytosolic calcium levels, and is mediated by the calcium-responsive CaMKK2-AMPKα axis in concert with ATR, but independently of CHK1. Loss of S649 phosphorylation enhances MRE11 binding to DNA and increases its association with stalled forks, driving excessive NSD, elevated DNA damage, and increased sensitivity to PARP inhibition. We find that the ATM-mediated S676/S678 phosphorylation primes S649 phosphorylation, which in turn facilitates subsequent phosphorylation of SQ/TQ sites in MRE11. Moreover, we find that CaMKK2-AMPKα activation requires ATR but is independent of ATM. Collectively, our findings reveal a hierarchical signaling mechanism that couples calcium signaling with ATM/ATR pathways to prevent NSD at stalled forks and preserve genome integrity. - Source: PubMed
Publication date: 2026/04/22
Chai Weihang ValerieRay ManobendroChang Chih-ChunWang Zhen-GuoLi ZhiguoChi Peter - Aldosterone-producing adenomas (APA) are a major cause of primary aldosteronism. While gene mutations in APA trigger aldosterone overproduction via calcium signaling, their precise regulatory mechanisms remain unclear. Our prior proteomic analysis identified significant upregulation of tumor protein D52 (TPD52), an oncogene protein implicated in cancer progression, in APA. This study investigates the role of TPD52 in regulating aldosterone synthesis and its molecular mechanism. - Source: PubMed
Xie LingMa LinqiangKang BingChen ZhihaoQi ShuangxinDu ManmanLi JiayuLi JunlongHe YifanXu YongHuang WeiGao RufeiHu JinboYang ShuminLi QifuPeng Chuan