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Human Monoclonal TINF2 Primary Antibody für GS, ICC - ABIN269685
Choi, Farrell, Lakamp, Ouellette: Characterization of the DNA binding specificity of Shelterin complexes. in Nucleic acids research 2011
Show all 12 Pubmed References
Human Monoclonal TINF2 Primary Antibody für WB - ABIN531985
Roig, Garcia, Robles, Cortvrindt, Egozcue, Smitz, Garcia: Human fetal ovarian culture permits meiotic progression and chromosome pairing process. in Human reproduction (Oxford, England) 2006
Show all 5 Pubmed References
The TIN2 plays an important role in maintaining the stable shelterin complex required for proper telomere end protection.
study suggests that, gallstone does not affect telomere length and even after having increased telomere length, decreased expression of some shelterin genes in inflamed tissue might cause telomeres to cap improperly, possibly leading to telomere dysfunction and further, gallbladder carcinogenesis
We report ophthalmic findings in twins with Revesz syndrome due to a previously unreported mutation in TINF2 and propose that phenotypic and molecular overlaps between DKC spectrum disorders and pediatric retinal vasculopathies may reflect a shared pathophysiologic basis.
demonstrate here the presence of a novel spliced isoform of TIN2 in chronic lymphocytic leukemia (CLL), related to deletion of exon 2 in the TIN2 gene
data supports a mechanism whereby telomerase deficiency and subsequent shortened telomeres initiate a DNA damage response and create a pro-oxidant environment, especially in Dyskeratosis Congenita cells carrying TINF2 mutations
telomerase elongates telomeres at a reduced frequency in TIN2-R282H heterozygous cells; this recruitment defect is further corroborated by examining the effect of this mutation on telomerase-telomere co-localization.
Our findings identify TINF2 as a mutant telomere gene in familial pulmonary fibrosis and suggest that infertility may precede the presentation of pulmonary fibrosis in a small subset of adults with telomere syndromes
A potential mitotic regulation of TIN2 by phosphorylation, is reported.
results suggest a link between telomeric proteins (TIN2)and metabolic control, providing an additional mechanism by which telomeric proteins regulate cancer and aging
Results suggests that the disruption of TIN2-TRF1 interaction may contribute to the severe dyskeratosis congenita phenotype observed in the context of the TIN2 truncation mutation.
The positive correlation between telomere length in dyskeratosis congenital and percent of LINE-1 methylation was restricted to TINF2 mutations.
Frameshift or nonsense mutations in TIN2 gene having very short telomeres are found in patients with dyskeratosis congenita.
Siah2 acts as an E3 ligase to directly ubiquitylate TIN2 in vitro.
These results demonstrate the important roles that Sp1 and NF-kappaB play in regulating the expression of the human telomere-binding protein TIN2.
Mouse gene deletion experiments revealed DNA-damage-response pathways that threaten chromosome ends and how the components of the telomeric shelterin complex prevent activation of these pathways.[Shelterin]
The presence of dysfunctional telomeres in chronic lymphocytic leukemia did not correlate with telomere shortening or chromatin marks deregulation but with a down-regulation of 2 shelterin genes: ACD and TINF2.
TIN2 mutations in DC may compromise the telomere recruitment of telomerase, leading to telomere shortening and the associated pathogenesis.
exon 6 of TINF2 natural mutations in 2/142 Japanese patients with acquired acquired bone marrow failure syndromes
TINF2 mutation of shelterin complex is associated with dyskeratosis congenita.
The expression of TINF2 may work to reduce the telomere length in precancerous lesions and offer new insight into the mechanism of carcinogenesis in gastric cancer.
Gene dosage reductions of Trf1 and/or Tin2 induce telomere DNA damage and lymphoma formation in aging mice.
demonstrated that cells expressing TIN2DeltaTPP1 instead of wild-type TIN2 phenocopy the POT1a,b knockout setting without showing additional phenotypes
shelterin protein TIN2 can protect chromosome ends as a TRF2-tethered TIN2/TPP1/POT1 complex that lacks a physical connection to TRF1
telomere shortening was accelerated in TIN2(+/DC) mTR(-/-) mice and MEFs compared with TIN2(+/+) mTR(-/-) controls, establishing that the TIN2(DC) telomere maintenance defect was not solely due to diminished telomerase action
Telomere protection by TPP1/POT1 requires tethering to TIN2.
TIN2 has a role independent of telomere length regulation that is essential for embryonic development and cell viability
This gene encodes one of the proteins of the shelterin, or telosome, complex which protects telomeres by allowing the cell to distinguish between telomeres and regions of DNA damage. The protein encoded by this gene is a critical part of shelterin\; it interacts with the three DNA-binding proteins of the shelterin complex, and it is important for assembly of the complex. Mutations in this gene cause dyskeratosis congenita (DKC), an inherited bone marrow failure syndrome.
TERF1-interacting nuclear factor 2
, TRF1-interacting nuclear protein 2
, TRF1-interacting nuclear factor 2