CDNF, Human Recombinant proteins
- Known as:
- CDNF, Human Recombinant proteins
- Catalog number:
- 7127-50
- Product Quantity:
- 50 μg
- Category:
- Proteins
- Supplier:
- Biovis
- Gene target:
- CDNF Human Recombinant proteins
Related genes to: CDNF, Human Recombinant proteins
- Gene:
- CDNF NIH gene
- Name:
- cerebral dopamine neurotrophic factor
- Previous symbol:
- ARMETL1
- Synonyms:
- -
- Chromosome:
- 10p13
- Locus Type:
- gene with protein product
- Date approved:
- 2004-05-27
- Date modifiied:
- 2015-09-11
Related products to: CDNF, Human Recombinant proteins
Related articles to: CDNF, Human Recombinant proteins
- Chronic kidney disease (CKD) is highly prevalent among individuals with abnormal glucose metabolism. However, limited research has specifically investigated CKD-associated proteins within this high-risk population. To address this gap, our study aimed to identify proteins associated with CKD in participants with abnormal glucose metabolism, potentially informing early detection and targeted therapeutic strategies. - Source: PubMed
Publication date: 2025/09/09
Li NingLiu JingyangWu GuanghengZhang JieLiu LongZheng ManqiLi HaibinLi ChangweiWen YaluJi JianguangYu YangZhao KunZheng Deqiang - The cerebral dopamine neurotrophic factor (CDNF) is a neurotrophic factor extensively studied in the central nervous system because of its neuroprotective effects; however, its role in the peripheral nervous system (PNS) remains less explored. In this study, we used primary dorsal root ganglia (DRG) explants to investigate the neuritogenic potential of exogenous CDNF, as well as its neuroprotective activity under trophic factor deprivation. Our findings demonstrate that CDNF-mediated neuroprotection remains unaffected by the addition of a Trk (tropomyosin receptor kinase) inhibitor or anti-nerve growth factor (NGF) antibody, indicating that CDNF's neurotrophic activity is independent of TrkA signaling. Furthermore, CDNF binding to KDEL-receptor (KDEL-R) was essential for its protective effect, as the CDNF variant lacking the KDEL-R binding sequence (CDNF-ΔKTEL) displayed no significant neuroprotection. Additionally, the simultaneous administration of NGF and CDNF to DRG explants resulted in an additive enhancement of their trophic activities. Notably, both CDNF- and NGF-induced neurotrophic effects were PI3K-dependent, reinforcing the role of this signaling pathway in their mechanisms of action. Taken together, our findings highlight CDNF's crucial role in the PNS, ensuring that NGF-independent neurogenesis can occur. This suggests that CDNF could be further explored in conditions where NGF levels are low or where NGF signaling inhibition is desirable, such as in chronic pain management. - Source: PubMed
de Siqueira Santos RaphaelBorba Flávia Natalede Oliveira Dahienne FerreiraSantiago Marcelo Felippedo Nascimento Alexandre MartinsSchechtman DeborahFoguel Debora - Multidomain proteins containing both folded and intrinsically disordered regions are crucial for biological processes, but characterizing their conformational ensembles and dynamics remains challenging. We introduce the Quality Evaluation Based Simulation Selection (QEBSS) protocol, which combines MD simulations with NMR-derived protein backbone N T and T spin relaxation times and hetNOE values to interpret conformational ensembles and dynamics of multidomain proteins. We demonstrate the practical advantage of QEBSS by characterizing four flexible multidomain proteins: calmodulin, EN2, MANF, and CDNF. These biologically important proteins have been difficult to study due to their flexible nature. Our findings reveal new insights into their conformational landscapes and dynamics, providing mechanistic understanding of their biological functions. QEBSS offers quantitative quality evaluation of simulations and a systematic approach for resolving conformational ensembles of multidomain proteins with heterogeneous dynamics. Given the importance of such proteins in biology, biotechnology, and materials science, QEBSS should benefit fields from drug design to novel materials development. - Source: PubMed
Publication date: 2025/08/10
Sandelin Amanda ENencini RickyYasar EkremFudo SatoshiStratoulias VassilisKajander TommiOllila O H Samuli - In 2023, a workshop was organized by the UK charity Cure Parkinson's with The Michael J Fox Foundation for Parkinson's Research and Parkinson's UK to review the field of growth factors (GFs) for Parkinson's disease (PD). This was a follow up to a previous meeting held in 2019. This 2023 workshop reviewed new relevant data that has emerged in the intervening 4 years around the development of new GFs and better models for studying them including the merit of combining treatments as well as therapies that can be modulated. We also discussed new insights into GF delivery and trial design that have emerged from the analyses of completed GDNF trials, including the patient voice, as well as the recently completed CDNF trial. We then concluded with our recommendations on how GF studies in PD should develop going forward. - Source: PubMed
Publication date: 2024/12/27
Barker Roger ASaarma MartSvendsen Clive NMorgan CatherineWhone AlanFiandaca Massimo SLuz MatthiasBankiewicz Krystof SFiske BrianIsaacs LyndseyRoach ArthurPhipps ThomasKordower Jeffrey HLane Emma LHuttunen Henri JSullivan AideenO'Keeffe GerardYartseva ValeriaFederoff Howard - Myocardial ischemia-reperfusion (I/R) injury is a cause of high post-interventional mortality in patients with acute myocardial infarction (MI). Cerebral dopamine neurotrophic factor (CDNF) is an endoplasmic reticulum (ER) resident protein, and its expression and secretion are induced when tissues and cells are subjected to hypoxia, ischemia, or traumatic injury. As a novel cardiomyokine, CDNF plays a crucial role in the progression of myocardial I/R injury. In our previous study, we reported that the overexpression of CDNF inhibited tunicamycin-induced H9C2 cell apoptosis. Moreover, there is a unique N-glycosylation site at Asn57 in the CDNF protein, which likely affects its function in H9C2 cells. However, the detailed impact remains unexplored. In our current study, we observed elevated levels of CDNF in the serum of acute MI patients, myocardial tissue of I/R model mice, and H/R model H9C2 cells. To detect the effect of N-glycosylation on the CDNF protein, we constructed an Asn57 mutant (N57A) plasmid and found that the N57A protein presented similar intracellular localization to those of the wild-type CDNF protein. However, the N57A protein demonstrated reduced stability, and the mutant protein could not protect H/R-induced H9C2 cells from apoptosis. Moreover, this process may occur through the downregulation of the PI3K/Akt pathway. Therefore, N-glycosylation of CDNF may be essential for protein stability and its protective role in H/R injury in H9C2 cells. - Source: PubMed
Publication date: 2025/02/07
Huang QingwenDong HaibinJia WenjuanRen YanxinLi WeiZhong LinGong LeiYang Jun