RAP1 (Telomeric Repeat-Binding Factor 2-interacting Protein 1,TERF2-interacting telomeric Protein 1,TRF2-interacting telomeric Protein 1,Dopamine Receptor-interacting Protein 5,Repressor/Activator Protein 1 Homolog,RAP1 Homol

Antibodies / Antibodies-Binding Proteins

-20°C

Supplied as a liquid in PBS, pH 7.3, 0.02% sodium azide, 50% glycerol.

Recombinant human Telomeric repeat-binding factor 2-interacting protein 1 protein (1-280aa)

Acts both as a regulator of telomere function and as a transcription regulator. Involved in the regulation of telomere length and protection as a component of the shelterin complex (telosome). In contrast to other components of the shelterin complex, it is dispensible for telomere capping and does not participate in the protection of telomeres against non-homologous end-joining (NHEJ)-mediated repair. Instead, it is required to negatively regulate telomere recombination and is essential for repressing homology-directed repair (HDR), which can affect telomere length. Does not bind DNA directly: recruited to telomeric double-stranded 5'-TTAGGG-3' repeats via its interaction with TERF2. Independently of its function in telomeres, also acts as a transcription regulator: recruited to extratelomeric 5'-TTAGGG-3' sites via its association with TERF2 or other factors, and regulates gene expression. When cytoplasmic, associates with the I-kappa-B-kinase (IKK) complex and acts as a regulator of the NF-kappa-B signaling by promoting IKK-mediated phosphorylation of RELA/p65, leading to activate expression of NF-kappa-B target genes.

Applications:
Suitable for use in ELISA and Immunohistochemistry. Other applications not tested.

Recommended Dilution:
Immunohistochemistry: 1:20-1:200
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for 12 months after receipt. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.