Rabbit Anti-TERF2 Recombinant Antibody (CBYJT-2529) (CBMAB-T1685-YJ)

Rabbit

Human

CBYJT-2529

IgG

WB, IP, FC

A synthetic peptide corresponding to residues in human TRF2 was used as an immunogen

Human

IgG

Monoclonal

The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

PBS, 0.05% BSA, 50% Glycerol

0.01% Sodium Azide

Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

TERF2

TERF2 is a telomere specific protein, TERF2, which is a component of the telomere nucleoprotein complex. TERF2 is present at telomeres in metaphase of the cell cycle, is a second negative regulator of telomere length and plays a key role in the protective activity of telomeres. While having similar telomere binding activity and domain organization, TERF2 differs from TERF1 in that its N terminus is basic rather than acidic.

Telomeric Repeat Binding Factor 2; TTAGGG Repeat-Binding Factor 2; Telomeric DNA-Binding Protein; TRBF2; TRF2; Telomeric Repeat Binding Protein 2; Telomeric Repeat-Binding Factor 2

Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and plays a central role in telomere maintenance and protection against end-to-end fusion of chromosomes. In addition to its telomeric DNA-binding role, required to recruit a number of factors and enzymes required for telomere protection, including the shelterin complex, TERF2IP/RAP1 and DCLRE1B/Apollo. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded 5'-TTAGGG-3' repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. Together with DCLRE1B/Apollo, plays a key role in telomeric loop (T loop) formation by generating 3' single-stranded overhang at the leading end telomeres: T loops have been proposed to protect chromosome ends from degradation and repair. Required both to recruit DCLRE1B/Apollo to telomeres and activate the exonuclease activity of DCLRE1B/Apollo. Preferentially binds to positive supercoiled DNA. Together with DCLRE1B/Apollo, required to control the amount of DNA topoisomerase (TOP1, TOP2A and TOP2B) needed for telomere replication during fork passage and prevent aberrant telomere topology. Recruits TERF2IP/RAP1 to telomeres, thereby participating in to repressing homology-directed repair (HDR), which can affect telomere length.

Biological Process anterograde axonal transport of messenger ribonucleoprotein complexSource:Ensembl
Biological Process cell cycleSource:UniProtKB-KW
Biological Process cellular senescenceSource:BHF-UCL1 Publication
Biological Process in utero embryonic developmentSource:Ensembl
Biological Process negative regulation of beta-galactosidase activitySource:BHF-UCL1 Publication
Biological Process negative regulation of cellular senescenceSource:BHF-UCL1 Publication
Biological Process negative regulation of exonuclease activitySource:BHF-UCL1 Publication
Biological Process negative regulation of gene expressionSource:BHF-UCL1 Publication
Biological Process negative regulation of t-circle formationSource:BHF-UCL1 Publication
Biological Process negative regulation of telomere cappingSource:BHF-UCL1 Publication
Biological Process negative regulation of telomere maintenanceSource:UniProtKB1 Publication
Biological Process negative regulation of telomere maintenance via recombinationSource:BHF-UCL1 Publication
Biological Process negative regulation of telomere maintenance via semi-conservative replicationSource:BHF-UCL1 Publication
Biological Process negative regulation of telomere maintenance via telomeraseSource:BHF-UCL1 Publication
Biological Process negative regulation of telomere maintenance via telomere lengtheningSource:BHF-UCL1 Publication
Biological Process negative regulation of telomere single strand break repairSource:BHF-UCL1 Publication
Biological Process negative regulation of telomeric D-loop disassemblySource:BHF-UCL1 Publication
Biological Process positive regulation of gene expressionSource:BHF-UCL1 Publication
Biological Process positive regulation of nitric-oxide synthase activitySource:BHF-UCL1 Publication
Biological Process positive regulation of telomere maintenanceSource:ComplexPortal1 Publication
Biological Process protection from non-homologous end joining at telomereSource:BHF-UCL2 Publications
Biological Process protein localization to chromosome, telomeric regionSource:BHF-UCL1 Publication
Biological Process regulation of telomere maintenanceSource:CACAO1 Publication
Biological Process regulation of telomere maintenance via telomeraseSource:BHF-UCL1 Publication
Biological Process RNA-templated DNA biosynthetic processSource:GOC
Biological Process telomere cappingSource:ComplexPortal1 Publication
Biological Process telomere maintenanceSource:UniProtKB1 Publication
Biological Process telomeric D-loop disassemblySource:BHF-UCL1 Publication
Biological Process telomeric loop formationSource:BHF-UCL1 Publication

Nucleus
Chromosome, telomere
Colocalizes with telomeric DNA in interphase cells and is located at chromosome ends during metaphase.

Phosphorylated upon DNA damage, most probably by ATM. Phosphorylated TERF2 is not bound to telomeric DNA, and rapidly localizes to damage sites.
Methylated by PRMT1 at multiple arginines within the N-terminal Arg-rich region. Methylation may control association with telomeres.