UBQLN2 Antibody, HRP conjugated

1. The genome of Drosophila contains a single UBQLN homolog (dUbqn) that shows high similarity to UBQLN1 and UBQLN2; therefore, the fly is a useful model for characterizing the role of UBQLN in vivo in neurological disorders affecting locomotion and learning abilities. PMID:29247619
2. Its PXX domain missense mutations linked to amyotrophic lateral sclerosis and atypical hereditary spastic paraplegia phenotype through defective HSP70-mediated proteolysis. PMID:28716533
3. Its mutation is a cause of amyotrophic lateral sclerosis in New Zealand. PMID:27480424
4. Ubiquilins are a family of chaperones for cytosolically exposed transmembrane domains and use ubiquitin to triage clients for degradation via coordinated intra- and intermolecular interactions. PMID:27345149
5. We analyzed mutations in the UBQLN2 gene in a Chinese cohort with sporadic ALS (sALS). A novel missense mutation was detected in one sALS patient. The p.M392V mutation substitutes a highly conserved residue, has not been reported in the population databases, and previously, at the same residue, a missense mutation p.M392I was detected in two Turkey ALS patients and was considered to be pathogenic. PMID:28125704
6. Frontotemporal dementia -linked mutations in gene ubiquilin 2 encoding autophagy adaptor proteins , indicate that impaired autophagy might cause Frontotemporal dementia. PMID:27166223
7. excess UBQLN2 is toxic rather than protective to neurons and that uncontrolled enhancement of UBQLN2 function is involved in UBQLN2 pathogenesis PMID:27456931
8. Ubiquilin-2 immunostaining - a new marker as a diagnostic supplement in urine cytology? PMID:27168037
9. UBQLN2 is specifically expressed in the urine of urothelial carcinoma patients. PMID:26303000
10. Results showed that UBQLN2 is selectively recruited to nuclear inclusions in Huntington's disease but not spinocerebellar ataxia type 3 PMID:26141599
11. These findings provide a molecular basis for the development of ALS/FTD-associated proteinopathy and establish novel therapeutic targets for ALS. PMID:26944018
12. Mutations in UBQLN2 gene cause dominant inheritance of amyotrophic lateral sclerosis due to Defective Proteasome Delivery. PMID:26075709
13. UBQLN2 may be a new molecular target for chemotherapeutics and a useful clinicopathological marker in human osteosarcoma. PMID:25672654
14. ALS-linked mutations in ubiquilin-2 or hnRNPA1 reduce interaction between ubiquilin-2 and hnRNPA1 PMID:25616961
15. A single putative mutation of UBQLN2 in a cohort of patients with front temporal lobar degeneration was found. PMID:25179229
16. Data indicate cognitive deficits in mutant ubiquilin 2 protein UBQLN2P497H transgenic mice. PMID:25246588
17. Causative mutation in the UBQLN2 gene is rare in Korean patients with either familial or sporadic ALS. PMID:24684794
18. As ubiquilin-2-positive inclusions are identified in brain, this mutant peptide predisposes to protein misfolding and accumulation. PMID:24771548
19. The P506S mutation in UBQLN2 can affect both males and females with frontotemporal dementia/amyotrophic lateral sclerosis (FTD/ALS). PMID:23944734
20. no evidence for involvement of ubiquilin 2 in tau pathology PMID:24086754
21. The dtat of study suggest that UBQLN2 is generally involved in the pathogenesis of ALS. PMID:24085347
22. Its mutations are not frequent cause of amyotrophic lateral sclerosis in Ireland. PMID:23973441
23. results were confirmed by similar findings for ubiquilin-1 and -2 in human brain tissue sections, where accumulation was observed in huntingtin inclusions PMID:23774650
24. Genetic variations in UBQLN2 in a predominantly Flanders-Belgian cohort of frontotemporal lobar degeneration patients are extremely rare. PMID:23312802
25. Its mutations related to ALS/FTLD are extremely rare in French FTLD and FTLD-ALS patients. PMID:23582661
26. No causative mutations within the PXX domain of the UBQLN2 gene are found in familial frontotemoral dementia patients. PMID:22729385
27. data support the role of the UBQLN2 gene in the pathogenesis of FALS, being conversely a rare genetic cause in SALS even when complicated by FTD. PMID:23138764
28. This study reported 3 novel UBQLN2 mutations, accounting for 1.2% (2/161) ALS and 2.2% (1/45) FTD patients, including a patient with pure FTD. PMID:22892309
29. A novel missense UBQLN2 mutation (c.1460C>T, p.T487I) was identified in 2 apparently unrelated multigenerational amyotrophic lateral sclerosis families with no evidence of frontotemporal dementia. This mutation segregated with the disease. PMID:22717235
30. The results of this study support support a causative role of the UBQLN2 gene in the pathogenesis of ALS and suggest that UBQLN2 mutations are rare in the French and French-Canadian population. PMID:22560112
31. The results of this study suggested that UBQLN2 was not found to be a cause of familial ALS in the Netherlands. PMID:22676852
32. Found a pathophysiological link between C9ORF72 expansions and ubiquilin-2 (UBQLN) proteins in amyotrophic lateral sclerosis and frontotemporal lobar degeneration that is associated with a highly characteristic pattern of UBQLN pathology. PMID:22426854
33. The results of this study suggested that UBQLN2 gene mutations are rare in French amyotrophic lateral sclerosis. PMID:22169395
34. findings link abnormalities in ubiquilin 2 to defects in the protein degradation pathway, abnormal protein aggregation and neurodegeneration, indicating a common pathogenic mechanism that can be exploited for therapeutic intervention PMID:21857683
35. solution structure of the ubl domain of hPLIC-2 PMID:11827521
36. hPLIC-2 interferes with the ubiquitin-mediated proteolysis of p53 and interacts with proteasomes PMID:12972570
37. Ubiquilin is capable of forming dimers. Dimerization requires the central region of ubiquilin, but not its UBL or the UBA domains. Monomeric ubiquilin is likely to be the active form that is involved in binding presenilin proteins. PMID:16813565
38. hHR23a and hPLIC2 interact via UBL/UBA domain interactions PMID:17098253
39. Ubiquitin-like protein PLIC-2 is identified as a negative regulator of G protein-coupled receptor endocytosis. PMID:18199683
40. siRNA-mediated UBQLN2 depletion made cells more susceptible to starvation-induced cell death. UBQLN2 regulates cell survival during starvation. PMID:19148225

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HGNC: 12509

UNIGENE: Hs.179309

KEGG: hsa:29978

STRING: 9606.ENSP00000345195

OMIM: 300264