TRF-2 Antibody (4A794.15) [PE/Cy7]

Product Discontinued

TRF-2 Antibody (4A794.15) [PE/Cy7] Summary

• Immunogen: Baculovirus expressed whole length TRF2 protein was used for immunizing mice and splenocytes used to generate the hybridoma clone (NP_005643).
• Isotype: IgG1 Kappa
• Clonality: Monoclonal
• Host: Mouse
• Gene: TERF2
• Purity: Protein G purified

Applications/Dilutions

• Dilutions:
  • Chromatin Immunoprecipitation (ChIP)
  • CyTOF-ready
  • ELISA
  • Flow Cytometry
  • Immunoblotting
  • Immunocytochemistry/ Immunofluorescence
  • Immunohistochemistry
  • Immunohistochemistry-Frozen
  • Immunohistochemistry-Paraffin
  • Immunoprecipitation
  • Proximity Ligation Assay
  • Western Blot
• Application Notes: Optimal dilution of this antibody should be experimentally determined. For optimal results using our Tandem dyes, please avoid prolonged exposure to light or extreme temperature fluctuations. These can lead to irreversible degradation or decoupling. When staining intracellular targets, specific attention to the fixation and permeabilization steps in your flow protocol may be required. Please contact our technical support team at technical@novusbio.com if you have any questions.

Reactivity Notes

Muntjac (deer) reactivity reported in scientific literature (PMID: 15878333).

Packaging, Storage & Formulations

• Storage: Store at 4C in the dark. Do not freeze.
• Buffer: PBS
• Preservative: 0.05% Sodium Azide
• Purity: Protein G purified

Notes

Cy is a registered trademark of Global Life Sciences Solutions Germany GmbH.

Alternate Names for TRF-2 Antibody (4A794.15) [PE/Cy7]

• Telomeric DNA-binding protein
• telomeric repeat binding factor 2
• Telomeric repeat binding protein 2
• telomeric repeat-binding factor 2
• TERF2
• TRBF2
• TRF2
• TRF-2
• TTAGGG repeat binding factor 2
• TTAGGG repeat-binding factor 2

Background

Originally discovered as part of shelterin complex, telomeric repeat-binding factor 2 (TRF2, also called TERF2 or TRB2) is a ubiquitously expressed nuclear protein (55-60 kDa) involved in telomere homeostasis. TRF2 contains an N-terminal GAR domain, a central TRFH dimerization domain, and a C-terminal SAND/MYB-type DNA binding domain. Trf2 RNA has 10 exons and alternative splicing in rodents produces a truncated form, TRF2-S, which lacks the DNA binding domain and nuclear localization signal (NLS) (1).

Both TRF2 and TRF1 bind to telomeric double stranded 5'-TTAGGG-3' DNA repeats, then recruit RAP1, TIN2, TPP1, and POT1 for the assembly of the shelterin complex. The telomeric association of TRF2 is greatly increased in the S phase of the cell cycle (2). Loss of TRF2 leads to telomere shortening, the DNA damage response, chromosomal instability, and replicative senescence. Interestingly, the contribution of TRF2 to telomere shortening via a telomerase-independent mechanism has also been reported (3). In conjunction with the exonuclease, Apollo, TRF2 protects telomeres during replication and negatively regulates the accumulation of DNA topoisomerase (TOP1, TOP2A and TOP2B).

TRF2 has been implicated in cancer, shown to be a major oncogene in telomerase-deficient mice. A link to Werner syndrome, a premature aging disease caused by the loss of WRN, has been reported based on TRF2 recruitment of WRN for processing of telomeric DNA (4). TRF2 expression is increased during human embryonic stem cell differentiation and has been shown to interact with Repressor Element-1 Silencing Transcription Factor (REST), protecting it from proteasomal degradation (5).

References

1. Grammatikakis, I., Zhang, P., Mattson, M. P., & Gorospe, M. (2016). The long and the short of TRF2 in neurogenesis. Cell cycle (Georgetown, Tex.), 15(22), 3026-3032. PMID: 27565210

2. Li, F., Kim, H., Ji, Z., Zhang, T., Chen, B., Ge, Y., Hu, Y., Feng, X., Han, X., Xu, H., Zhang, Y., Yu, H., Liu, D., Ma, W., & Songyang, Z. (2018). The BUB3-BUB1 Complex Promotes Telomere DNA Replication. Molecular cell, 70(3), 395-407. PMID: 29727616

3. Ancelin, K., Brunori, M., Bauwens, S., Koering, C. E., Brun, C., Ricoul, M., Pommier, J. P., Sabatier, L., & Gilson, E. (2002). Targeting assay to study the cis functions of human telomeric proteins: evidence for inhibition of telomerase by TRF1 and for activation of telomere degradation by TRF2. Molecular and cellular biology, 22(10), 3474-3487. PMID: 11971978

4. Machwe A, Xiao L, & Orren DK. (2004) TRF2 recruits the Werner syndrome (WRN) exonuclease for processing of telomeric DNA. Oncogene. 23(1):149-56. PMID: 14712220.

5. Diotti, R., & Loayza, D. (2011). Shelterin complex and associated factors at human telomeres. Nucleus (Austin, Tex.), 2(2), 119-135. PMID: 21738835

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

FAQs for TRF-2 Antibody (NB100-56506PECY7). (Showing 1 - 3 of 3 FAQ).

1. Are the TRF-2 antibodies validated in Simple Western?
   • Yes, we offer a 2 TRF-2 antibodies that have been tested in Simple Western: NB100-56506 and NB110-57130.
2. Does TRF-2 antibodies comes in lyophilized form?
   • we carry 2 TERF2/TRBF2 antibodies in lyophilized form: AF5635, MAB5635.
3. What the theoretical molecular weight for TRF-2 antibodies?
   • The TMW of TRF-2 antibodies is approximately 55 - 56 kDa.

Bioinformatics

• Gene Symbol: TERF2