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a novel ACD mutation(p.G223V)is detected; ACD is a novel gene involved in childhood pre-B acute lymphoblastic leukemia and may play a functional role in enhancing leukemia cell survival
The data support a causal relationship between a TPP1 (show TPP1 Proteins) mutation and bone marrow disorders in a family.
Clustering of novel mutations in the POT1 (show POT1 Proteins) binding domain of ACD was statistically higher (P = .005) in melanoma probands compared with population control individuals (n = 6785).
Shelterin protein TPP 1 (show TPP1 Proteins) interacts with hTERT and recruits hTERT onto the telomeres, suggesting that TPP 1 (show TPP1 Proteins) might be involved in regulation of telomere shortening.
POT1 (show POT1 Proteins)-TPP1 (show TPP1 Proteins) binds telomeric DNA in a coordinated manner to facilitate assembly of the nucleoprotein complexes into a state that is more accessible to enzymatic activity.
Study shows that the OB-fold domain of the telomere-binding protein TPP1 (show TPP1 Proteins) recruits telomerase to telomeres through an association with the telomerase reverse transcriptase TERT (show TERT Proteins); data define a potential interface for telomerase-TPP1 (show TPP1 Proteins) interaction required for telomere maintenance and implicate defective telomerase recruitment in telomerase-related disease.
a paper that firstly reported cloning of human TTP1 (show COPRS Proteins) (PTOP) and its biological function at telomere. TPP1 (show TPP1 Proteins) interacts with both POT1 (show POT1 Proteins) and TIN2 (show TINF2 Proteins), heterodimerizes with POT1 (show POT1 Proteins) and regulates POT1 (show POT1 Proteins) telomeric recruitment and telomere length.
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 (show TINF2 Proteins).
Results support a model in which POT1 (show POT1 Proteins)-TPP1 (show TPP1 Proteins) enhances telomerase processivity in a manner markedly different from the sliding clamps used by DNA polymerases.
TIN2 (show TINF2 Proteins)-anchored TPP1 (show TPP1 Proteins) plays a major role in the recruitment of telomerase to telomeres in human cells.
shelterin protein TIN2 (show TINF2 Proteins) can protect chromosome ends as a TRF2 (show TERF2 Proteins)-tethered TIN2 (show TINF2 Proteins)/TPP1 (show TPP1 Proteins)/POT1 (show POT1 Proteins) complex that lacks a physical connection to TRF1 (show TERF1 Proteins)
Mouse hematopoietic stem cells are acutely sensitive to inactivation of the shelterin gene Acd.
Tpp1 (show TPP1 Proteins) is required for the protective function of Pot1 (show POT1 Proteins) proteins.
Tumors from Acd(acd/acd) p53 (show TP53 Proteins)(+/-) mice show a striking switch from the classic spectrum of p53 (show TP53 Proteins)(-/-) mice toward carcinomas.
This gene encodes a protein that is involved in telomere function. This protein is one of six core proteins in the telosome/shelterin telomeric complex, which functions to maintain telomere length and to protect telomere ends. Through its interaction with other components, this protein plays a key role in the assembly and stabilization of this complex, and it mediates the access of telomerase to the telomere. Multiple transcript variants encoding different isoforms have been found for this gene. This gene, which is also referred to as TPP1, is distinct from the unrelated TPP1 gene on chromosome 11, which encodes tripeptidyl-peptidase I.
POT1 and TIN2 organizing protein
, POT1 and TIN2-interacting protein
, TIN2 interacting protein 1
, adrenocortical dysplasia protein homolog
, adrenocortical dysplasia homolog (mouse)
, adrenocortical dysplasia protein