Product nameAnti-TRF1 [572C] antibody
See all TRF1 primary antibodies
DescriptionRat monoclonal [572C] to TRF1
Tested applicationsSuitable for: ICC/IF, WBmore details
Species reactivityReacts with: Mouse
Recombinant full length protein (His-tag) corresponding to Mouse TRF1 aa 1-421.
MAETVSSAARDAPSREGWTDSDSPEQEEVGDDAELLQCQLQLGTPREMEN AELVAEVEAVAAGWMLDFLCLSLCRAFRDGRSEDFRRTRDSAEAIIHGLH RLTAYQLKTVYICQFLTRVASGKALDAQFEVDERITPLESALMIWNSIEK EHDKLHDEIKNLIKIQAVAVCMEIGSFKEAEEVFERIFGDPEFYTPLERK LKIISQKDVFHSLFQHFSYSCMMEKIQSYVGDVLSEKSSTFLMKAATKVV ENEKARTQASKDRPDATNTGMDTEVGLNKEKSVNGQQSTETEPLVDTVSS IRSHKNALSQLKHRRAPSDFSRNEARTGTLQCETTMERNRRTSGRNRLCV SENQPDTDDKSGRRKRQTWLWEEDRILKCGVKKYGEGNWAKILSHYKFNN RTSVMLKDRWRTMKRLKLI
Database link: P70371
- IHC: HEK-TRF1 and HEK-TRF2 transfected cell lines. WB: NIH-3T3 and Hek-TRF1 cell lysate, IPS-GFP-TRF1 homo cell lysate. ICC/IF: iPS cells,HRK-TRF1 and IPS-GFP-TRF1homo cell lines.
Storage instructionsShipped at 4°C. Upon delivery aliquot. Store at +4°C. Do Not Freeze.
PurityTissue culture supernatant
Our Abpromise guarantee covers the use of ab192629 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|ICC/IF||Use at an assay dependent concentration.|
|WB||Use at an assay dependent concentration. Predicted molecular weight: 50 kDa.|
FunctionBinds the telomeric double-stranded TTAGGG repeat and negatively regulates telomere length. Involved in the regulation of the mitotic spindle. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded TTAGGG 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.
Tissue specificityHighly expressed and ubiquitous. Isoform Pin2 predominates.
Sequence similaritiesContains 1 HTH myb-type DNA-binding domain.
DomainThe acidic N-terminal domain binds to the ankyrin repeats of TNKS1 and TNKS2. The C-terminal domain binds microtubules.
The TRFH dimerization region mediates the interaction with TINF2.
modificationsPhosphorylated preferentially on Ser-219 in an ATM-dependent manner in response to ionizing DNA damage.
ADP-ribosylation by TNKS1 or TNKS2 diminishes its ability to bind to telomeric DNA.
Ubiquitinated by RLIM/RNF12, leading to its degradation by the proteasome. Ubiquitinated by a SCF (SKP1-CUL1-F-box protein) ubiquitin-protein ligase complex, leading to its degradation by the proteasome.
Cellular localizationNucleus. Cytoplasm > cytoskeleton > spindle. Chromosome > telomere. Colocalizes with telomeric DNA in interphase and metaphase cells and is located at chromosome ends during metaphase. Associates with the mitotic spindle.
- Information by UniProt
- hTRF1 AS antibody
- NIMA interacting protein 2 antibody
- NIMA-interacting protein 2 antibody
All lanes : Anti-TRF1 [572C] antibody (ab192629)
Lane 1 : IPS-GFP-TRF1 homo at 100 µg
Lane 2 : IPS-GFP-TRF1 heter at 100 µg
Lane 3 : IPS-sh TRF1 at 100 µg
Lane 4 : IPS-sh TRF1 puro at 100 µg
Lane 5 : HEK-TRF1 at 20 µg
Lane 6 : HEK-FGFR2 at 20 µg
Lane 7 : NIH-3T3 at 100 µg
Predicted band size: 50 kDa
ab192629 used undiluted for all lanes.
Immunocytochemistry/ Immunofluorescent analysis of HEK-TRF1, HEK-GFP-TRF2, IPS-GFP-TRF1homo and IPS-shTRF1homo cell lines labeling TRF1 with undiluted ab192629.
Immunocytochemistry/ Immunofluorescent analysis of frozen cytospins preparations of mTRF1 expressed in HEK293T labeling TRF1 using ab192629. Negative control on right used mTRF2-GFP expressed in HEK293T.
All lanes : Anti-TRF1 [572C] antibody (ab192629) at 1/500 dilution
Lane 1 : Mefs TRF1 +/+ nuclear extract
Lane 2 : Mefs TRF1 KO nuclear extract
Lysates/proteins at 30 µg per lane.
Predicted band size: 50 kDa
Immunocytochemistry/ Immunofluorescent analysis of mouse blastocyte labeling TRF1 with ab192629 at a 1/100 dilution.
ab192629 has not yet been referenced specifically in any publications.