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TRF-2 Antibody (4A794.15) - BSA Free

Novus Biologicals, part of Bio-Techne | Catalog # NB100-56506

Novus Biologicals, part of Bio-Techne
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NB100-56506
NB100-56506SS
Forumulation
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Key Product Details

Species Reactivity

Validated:

Human, Mouse, Rat, Deer, Marsupial

Cited:

Human, Mouse, Rat, Marsupial, Muntjac (deer)

Applications

Validated:

Chromatin Immunoprecipitation (ChIP), CyTOF-ready, ELISA, Flow (Intracellular), Flow Cytometry, Immunoblotting, Immunocytochemistry/ Immunofluorescence, Immunohistochemistry, Immunohistochemistry-Frozen, Immunohistochemistry-Paraffin, Immunoprecipitation, Proximity Ligation Assay, Simple Western, Western Blot

Cited:

Chemotaxis, Immunocytochemistry, Immunocytochemistry/ Immunofluorescence, Immunofluorescence, Immunohistochemistry-Paraffin, Immunoprecipitation, Proximity Ligation Assay, Western Blot

Label

Unconjugated

Antibody Source

Monoclonal Mouse IgG1 kappa Clone # 4A794.15

Format

BSA Free

Concentration

1 mg/ml

Product Specifications

Immunogen

This TRF-2 Antibody (4A794.15) was developed against Baculovirus expressed whole length TRF2 protein, used for immunizing mice and splenocytes used to generate the hybridoma clone (NP_005643).

Specificity

The TRF2 antibody recognizes full-length TRF2 as well as TRF2 forms lacking both the N-terminal basic domain (B) and the telobox Myb-like C-terminal DNA-binding domain (M). TRF2 forms missing the B and M domains are often referred to as mutant TRF2. Although the exact epitope recognized by the TRF2 antibody has not been mapped, the scientific literature indicates it is in the D or L domain, but not in the B or M domain.

Marker

Telomeres marker

Clonality

Monoclonal

Host

Mouse

Isotype

IgG1 kappa

Theoretical MW

59.6 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.

Description

The TRF2 antibody is referred to as both clone 4A794.15 and 4A794 in the published literature. The TRF2 antibody recognizes full-length TRF2 as well as TRF2 forms lacking both the N-terminal basic domain (B) and the telobox Myb-like C-terminal DNA-binding domain (M). TRF2 forms missing the B and M domains are often referred to as mutant TRF2. Although the exact epitope recognized by the TRF2 antibody has not been mapped, the scientific literature indicates it is in the D or L domain, but not in the B or M domain.

Scientific Data Images for TRF-2 Antibody (4A794.15) - BSA Free

Simple Western: TRF-2 Antibody (4A794.15)BSA Free [NB100-56506]

Simple Western: TRF-2 Antibody (4A794.15)BSA Free [NB100-56506]

Simple Western: TRF-2 Antibody (4A794.15) [NB100-56506] - Image shows a specific band for TRF2 in 1.0 mg/mL of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system. Non-specific interaction with the 230 kDa Simple Western standard may be seen with this antibody.
Western Blot: TRF-2 Antibody (4A794.15)BSA Free [NB100-56506]

Western Blot: TRF-2 Antibody (4A794.15)BSA Free [NB100-56506]

Western Blot: TRF-2 Antibody (4A794.15) [NB100-56506] - Analysis in human Jurkat cell lysate at 2 ug/mL. Goat anti-mouse Ig HRP secondary antibody and PicoTect ECL substrate solution were used.
Immunohistochemistry-Paraffin: TRF-2 Antibody (4A794.15) - BSA Free [NB100-56506]

Immunohistochemistry-Paraffin: TRF-2 Antibody (4A794.15) - BSA Free [NB100-56506]

Immunohistochemistry-Paraffin: TRF-2 Antibody (4A794.15) [NB100-56506] - Transitional cell carcinoma, urinary bladder, stained with TRF2 antibody (4 ug/mL), peroxidase-conjugate and DAB chromogen. Note specific nuclear staining. Tumor/normal adjacent tissue array slide was used for this test. Staining of formalin-fixed tissues is enhanced by boiling tissue sections in 10 mM sodium citrate buffer, pH 6.0 for 10-20 min followed by cooling at RT for 20 min.

Applications for TRF-2 Antibody (4A794.15) - BSA Free

Application
Recommended Usage

Chromatin Immunoprecipitation (ChIP)

1:10-1:500

ELISA

2 ug/ml

Flow Cytometry

0.1 ug/10^6 cells

Immunoblotting

reported in scientific literature (PMID 23708666)

Immunocytochemistry/ Immunofluorescence

1:10 - 1:500

Immunohistochemistry

1:10 - 1:500

Immunohistochemistry-Frozen

5 ug/ml

Immunohistochemistry-Paraffin

1:200

Immunoprecipitation

2 ug/10^6 cells

Proximity Ligation Assay

reported in scientific literature (PMID 27366950)

Simple Western

1:50

Western Blot

2-4 ug/ml
Application Notes
TRF-2 may be detected as a single band or as a doublet in Western blot. Okabe (2000) described the doublet as 65 and 69 kDa using clone 4A794.15. Observed molecular weights could vary depending on molecular weight standards used and gel conditions.

In Simple Western only 10 - 15 uL of the recommended dilution is used per data point. Separated by Size-Wes, Sally Sue/Peggy Sue.
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.
Please Note: Optimal dilutions of this antibody should be experimentally determined.

Reviewed Applications

Read 1 review rated 4 using NB100-56506 in the following applications:

Formulation, Preparation, and Storage

Purification

Protein G purified

Formulation

PBS

Format

BSA Free

Preservative

0.02% Sodium Azide

Concentration

1 mg/ml

Shipping

The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.

Stability & Storage

Store at 4C short term. Aliquot and store at -20C long term. 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, 4A794, 4A794 trf2, 4A794.15, 4A794.15 trf2, anti-trf2 4A794, anti-trf2 4A794.15, clone 4A794, clone 4A794.15, Telomeric repeat binding protein 2

Entrez Gene IDs

7014 (Human); 21750 (Mouse); 361403 (Rat)

Gene Symbol

TERF2

UniProt

Additional TRF-2 Products

Product Documents for TRF-2 Antibody (4A794.15) - BSA Free

Certificate of Analysis

To download a Certificate of Analysis, please enter a lot number in the search box below.

Product Specific Notices for TRF-2 Antibody (4A794.15) - BSA Free

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.

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