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AB111584

Anti-Telomerase reverse transcriptase (phospho S227) antibody

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(1 Publication)

Rabbit Polyclonal Telomerase reverse transcriptase phospho S227 antibody. Suitable for ICC/IF and reacts with Human samples. Cited in 1 publication. Immunogen corresponding to Synthetic Peptide within Human TERT pS227.

View Alternative Names

EST2, TCS1, TRT, TERT, Telomerase reverse transcriptase, HEST2, Telomerase catalytic subunit, Telomerase-associated protein 2, TP2

1 Images
Immunocytochemistry/ Immunofluorescence - Anti-Telomerase reverse transcriptase (phospho S227) antibody (AB111584)
  • ICC/IF

Unknown

Immunocytochemistry/ Immunofluorescence - Anti-Telomerase reverse transcriptase (phospho S227) antibody (AB111584)

Immunofluorescence analysis of Telomerase reverse transcriptase (phospho S227) in HuvEc cells, using ab111584 at a 1/100 dilution. The image on the right is treated with the synthesized peptide.

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

ICC/IF

applications

Immunogen

Synthetic Peptide within Human TERT pS227. The exact immunogen used to generate this antibody is proprietary information.

O14746

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "ICCIF" : {"fullname" : "Immunocytochemistry/ Immunofluorescence", "shortname":"ICC/IF"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Human": { "ICCIF-species-checked": "testedAndGuaranteed", "ICCIF-species-dilution-info": "1/100 - 1/500", "ICCIF-species-notes": "<p></p>" } } }

Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Purification notes
ab111584 is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific phosphopeptide. The antibody against non-phosphopeptide was removed by chromatography using non-phosphopeptide corresponding to the phosphorylation.
Storage buffer
pH: 7.4 Preservative: 0.02% Sodium azide Constituents: PBS, 50% Glycerol (glycerin, glycerine), 0.88% Sodium chloride
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Storage information
Stable for 12 months at -20°C

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Telomerase reverse transcriptase also known as TERT is an enzyme with a molecular mass of about 127 kDa. It functions as a catalytic subunit of the telomerase complex which extends telomeres by adding the nucleotide sequence "TTAGGG" to the ends of chromosomes. TERT operates with a telomerase RNA component (TERC) to synthesize DNA using an RNA template a process called reverse transcription. TERT is expressed in embryonic tissues adult stem cells and cancer cells where rapid cell division occurs.
Biological function summary

TERT plays an important role in maintaining telomere length essential for protecting chromosome stability. The protein forms part of the telomerase holoenzyme complex working together with TERC to perform its function. Telomerase activity allows cells to bypass the Hayflick limit preventing senescence and enhancing replication potential. In addition to telomere maintenance TERT influences gene regulation and cellular proliferation.

Pathways

TERT holds significance in the telomere maintenance and signaling pathways. Telomere maintenance ensures genomic integrity and cellular longevity a process fundamental for tissue homeostasis and regeneration. TERT interacts with proteins such as dyskerin and TERC within these pathways. Its regulatory roles in these pathways also reveal interactions with other key proteins like hypothesized targets in the DNA damage response.

The upregulation of TERT is associated with cancer and degenerative diseases. Increased telomerase activity is a common feature in many cancers leading to uncontrolled cell proliferation. Additionally mutations in TERT and its associated components can contribute to disorders like dyskeratosis congenita a rare genetic condition resulting in bone marrow failure. In these conditions TERT interaction with proteins involved in chromosomal maintenance and repair becomes important for understanding disease mechanisms.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. Active in progenitor and cancer cells. Inactive, or very low activity, in normal somatic cells. Catalytic component of the teleromerase holoenzyme complex whose main activity is the elongation of telomeres by acting as a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. Catalyzes the RNA-dependent extension of 3'-chromosomal termini with the 6-nucleotide telomeric repeat unit, 5'-TTAGGG-3'. The catalytic cycle involves primer binding, primer extension and release of product once the template boundary has been reached or nascent product translocation followed by further extension. More active on substrates containing 2 or 3 telomeric repeats. Telomerase activity is regulated by a number of factors including telomerase complex-associated proteins, chaperones and polypeptide modifiers. Modulates Wnt signaling. Plays important roles in aging and antiapoptosis.
See full target information TERT pS227

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

EMBO molecular medicine 15:e17836 PubMed37766669

2023

Propionate reinforces epithelial identity and reduces aggressiveness of lung carcinoma.

Applications

Unspecified application

Species

Unspecified reactive species

Vignesh Ramesh,Paradesi Naidu Gollavilli,Luisa Pinna,Mohammad Aarif Siddiqui,Adriana Martinez Turtos,Francesca Napoli,Yasmin Antonelli,Aldo Leal-Egaña,Jesper Foged Havelund,Simon Toftholm Jakobsen,Elisa Le Boiteux,Marco Volante,Nils Joakim Faergeman,Ole N Jensen,Rasmus Siersbaek,Kumar Somyajit,Paolo Ceppi
View all publications

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