MANF Antibody

1. Our data indicate that increased MANF concentrations in serum are associated with the clinical manifestation of type 1 diabetes in children, but the exact mechanism behind the increase remains elusive PMID: 27356471
2. Sulfatide binding promotes cellular MANF uptake and cytoprotection from hypoxia-induced cell death. PMID: 29497057
3. Serum MANF level was higher in patients with newly diagnosed prediabetes and T2 Diabetes Mellitus than in normal glucose tolerance controls. MANF appears to be associated with Matsuda Index, QUICKI and HOMA-IR in prediabetes patients. PMID: 28216543
4. the role of two short sequence motifs within the carboxy-(C) terminal domain of MANF in its neuroprotective activity, was studied. PMID: 26720341
5. the selective expression of MANF in splenocytes may be involved in plasma cell differentiation and immune regulation. PMID: 26429332
6. MANF is a protein that interacts with RTN1-C PMID: 25543119
7. We demonstrate that Armet and Creld2 are genotype-specific ER stress response proteins with substrate specificities, and that aggregation of mutant matrilin-3 is a key disease trigger in MED that could be exploited as a potential therapeutic target PMID: 23956175
8. MANF binding to the plasma membrane also required the RTDL sequence and was inhibited with a peptide known to interact with KDELRs, suggesting MANF binds KDELRs at the surface. PMID: 23255601
9. MANF and C-MANF protect neurons intracellularly as efficiently as Ku70. PMID: 21047780
10. Pretreatment with adeno-associated-virus vector containing human MANF reduces the volume of cerebral infarction and facilitates behavioral recovery in experimental stroke rats. PMID: 20685313
11. Armet is a novel secreted mediator of the adaptive pathway of unfolded protein response. PMID: 18561914
12. The widespread expression of MANF together with its evolutionary conserved nature and regulation by brain insults suggest that it has important functions both under normal and pathological conditions in many tissue types. PMID: 18718866
13. structures of MANF and CDNF were solved; structure explains why MANF and CDNF are bifunctional; neurotrophic activity may reside in the N-terminal domain and ER stress response in the C-terminal domain PMID: 19258449

Show More

Hide All

HGNC: 15461

OMIM: 601916

KEGG: hsa:7873

STRING: 9606.ENSP00000432799

UniGene: Hs.436446