Recombinant Human TRF-2 GST (N-Term) Protein

Name: Recombinant Human TRF-2 GST (N-Term) Protein
Brand: Novus Biologicals
SKU: H00007014-P01

Novus Biologicals, part of Bio-Techne | Catalog # H00007014-P01

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Product Datasheet / COA / SDS

Discontinued Product

H00007014-P01 has been discontinued. View all TRF-2 products.

Product Specifications
Scientific Data
Preparation & Storage
Background
Product Documents
Specific Notices

Key Product Details

Source

Wheat germ

Tag

GST (N-Term)

Conjugate

Unconjugated

Applications

ELISA, Affinity Purification, Microarray, Western Blot

View all TRF-2 Proteins and Enzymes »

Product Specifications

Description

A recombinant protein with GST tag at N-terminal corresponding to the amino acids 1-251 of Human TERF2

Source: Wheat Germ (in vitro)

Amino Acid Sequence: MAGGGGSSDGSGRAAGRRASRSSGRARRGRHEPGLGGPAERGAGEARLEEAVNRWVLKFYFHEALRAFRGSRYGDFRQIRDIMQALLVRPLGKEHTVSRLLRVMQCLSRIEEGENLDCSFDMEAELTPLESAINVLEMIKTEFTLTEAVVESSRKLVKEAAVIICIKNKEFEKASKILKKHMSKDPTTQKLRNDLLNIIREKNLAHPVIQNFSYETFQQKMLRFLESHLDDAEPYLLTVRLGPSPITMVCP

Purity

>80% by SDS-PAGE and Coomassie blue staining

Predicted Molecular Mass

54.7 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.

Activity

This protein was produced in an in vitro wheat germ expression system that should preserve correct conformational folding that is necessary for biological function. While it is possible that this protein could display some level of activity, the functionality of this protein has not been explicitly measured or validated.

Protein / Peptide Type

Recombinant Protein

Scientific Data Images for Recombinant Human TRF-2 GST (N-Term) Protein

Recombinant Human TRF-2 Protein [H00007014-P01] - 12.5% SDS-PAGE Stained with Coomassie Blue.

Formulation, Preparation and Storage

H00007014-P01

Preparation Method	in vitro wheat germ expression system
Formulation	50 mM Tris-HCl, 10 mM reduced Glutathione, pH 8.0 in the elution buffer.
Preservative	No Preservative
Concentration	Please see the vial label for concentration. If unlisted please contact technical services.
Shipping	The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage	Store at -80C. Avoid freeze-thaw cycles.

Background: TRF-2

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

Long Name

Telomeric Repeat Binding Factor 2

Alternate Names

TERF2, TRBF2, TRF2

Gene Symbol

TERF2

Additional TRF-2 Products

Product Documents for Recombinant Human TRF-2 GST (N-Term) Protein

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COA

SDS

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Product Specific Notices for Recombinant Human TRF-2 GST (N-Term) Protein

This product is produced by and distributed for Abnova, a company based in Taiwan.

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

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