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Human telomerase reverse transcriptase (hTERT) is the catalytic subunit of the telomerase. It is also responsible for addition of TTAGGG repeats to the telomere ends of the chromosome, which is important in maintaining cell immortality. In most normal human cells the expression of hTERT is very low. On the other hand, greater than 90 % of human tumors of different pathology and origins have been shown to upregulate telomerase expression, making hTERT a cancer-associated target.
References
Product Information
Format
Purified
Control
Human lymph node tissue lysate
Presentation
Purified mouse monoclonal IgMκ in buffer containing PBS with 0.05% sodium azide.
Anti-TERT (human) Antibody, clone 2C4 is an antibody against TERT (human) for use in WB, IC & IP.
Key Applications
Western Blotting
Immunocytochemistry
Immunoprecipitation
Application Notes
Immunoprecipitation Analysis: A representative lot was used by an independent laboratory to detect TERT in HeLa cells (Masutomi, K., et al. (2003). Cell, Vol. 114:241–253).
Immunocytochemistry Analysis: A representative lot was used by an independent laboratory to detect TERT in HeLa cells, BJ and WI-38 fibroblasts (Masutomi, K., et al. (2003). Cell, Vol. 114:241–253).
Biological Information
Immunogen
Full length recombinant protein corresponding to human TERT.
Telomerase is a ribonucleoprotein polymerase that maintains telomere ends by addition of the telomere repeat TTAGGG. The enzyme consists of a protein component with reverse transcriptase activity, encoded by this gene, and an RNA component which serves as a template for the telomere repeat. Telomerase expression plays a role in cellular senescence, as it is normally repressed in postnatal somatic cells resulting in progressive shortening of telomeres. Deregulation of telomerase expression in somatic cells may be involved in oncogenesis. Studies in mouse suggest that telomerase also participates in chromosomal repair, since de novo synthesis of telomere repeats may occur at double-stranded breaks. Alternatively spliced variants encoding different isoforms of telomerase reverse transcriptase have been identified; the full-length sequence of some variants has not been determined. Alternative splicing at this locus is thought to be one mechanism of regulation of telomerase activity. [provided by RefSeq].
FUNCTION: 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.
SUBUNIT STRUCTURE: Homodimer; dimerization is required to produce a functional complex. Oligomer; can form oligomers in the absence of the telomerase RNA template component (TERC). Catalytic subunit of the telomerase holoenzyme complex composed minimally of TERT and TERC. The telomerase complex is composed of TERT, DKC1, WDR79/TCAB1, NOP10, NHP2, GAR1, TEP1, EST1A, POT1 and a telomerase RNA template component (TERC). The molecular chaperone HSP90/P23 complex is required for correct assembly and stabilization of the active telomerase. Interacts directly with HSP90A and PTGES3. Interacts with HSPA1A; the interaction occurs in the absence of TERC and dissociates once the complex has formed. Interacts with RAN; the interaction promotes nuclear export of TERT. Interacts with XPO1. Interacts with PTPN11; the interaction retains TERT in the nucleus. Interacts with NCL (via RRM1 and C-terminal RRM4/Arg/Gly-rich domains); the interaction is important for nucleolar localization of TERT. Interacts with SMARCA4 (via the bromodomain); the interaction regulates Wnt-mediated signaling. Interacts with MCRS1 (isoform MCRS2); the interaction inhibits in vitro telomerase activity. Interacts with PIF1; the interaction has no effect on the elongation activity of TERT.
SUBCELLULAR LOCATION: Nucleus › nucleolus. Nucleus › nucleoplasm. Nucleus. Chromosome › telomere. Cytoplasm. Note: Shuttling between nuclear and cytoplasm depends on cell cycle, phosphorylation states, transformation and DNA damage. Diffuse localization in the nucleoplasm. Enriched in nucleoli of certain cell types. Translocated to the cytoplasm via nuclear pores in a CRM1/RAN-dependent manner involving oxidative stress-mediated phosphorylation at Tyr-707. Dephosphorylation at this site by SHP2 retains TERT in the nucleus. Translocated to the nucleus by phosphorylation by AKT.
TISSUE SPECIFICITY: Expressed at a high level in thymocyte subpopulations, at an intermediate level in tonsil T lymphocytes, and at a low to undetectable level in peripheral blood T lymphocytes.
INDUCTION: Activated by cytotoxic events and down-regulated during aging. In peripheral T lymphocytes, induced By CD3 and by PMA/ionomycin. Inhibited by herbimycin B.
DOMAIN: The primer grip sequence in the RT domain is required for telomerase activity and for stable association with short telomeric primers.
The RNA-interacting domain 1 (RD1)/N-terminal extension (NTE) is required for interaction with the pseudoknot-template domain of each of TERC dimers. It contains anchor sites that bind primer nucleotides upstream of the RNA-DNA hybrid and is thus an essential determinant of repeat addition processivity.
The RNA-interacting domain 2 (RD2) is essential for both interaction with the CR4-CR5 domain of TERC and for DNA sythesis.
PTM: Ubiquitinated, leading to proteasomal degradation.
Phosphorylation at Tyr-707 under oxidative stress leads to translocation of TERT to the cytoplasm and reduces its antiapoptotic activity. Dephosphorylated by SHP2/PTPN11 leading to nuclear retention. Phosphorylation by the AKT pathway promotes nuclear location.
INVOLVEMENT IN DISEASE Note=Activation of telomerase has been implicated in cell immortalization and cancer cell pathogenesis.
Defects in TERT are associated with susceptibilty to aplastic anemia (AA) [MIM:609135]. AA is a rare disease in which the reduction of the circulating blood cells results from damage to the stem cell pool in bone marrow. In most patients, the stem cell lesion is caused by an autoimmune attack. T-lymphocytes, activated by an endogenous or exogenous, and most often unknown antigenic stimulus, secrete cytokines, including IFN-gamma, which would in turn be able to suppress hematopoiesis.
Note=Genetic variations in TERT are associated with coronary artery disease (CAD).
Defects in TERT are a cause of dyskeratosis congenita autosomal dominant (ADDKC) [MIM:127550]; also known as dyskeratosis congenita Scoggins type. ADDKC is a rare, progressive bone marrow failure syndrome characterized by the triad of reticulated skin hyperpigmentation, nail dystrophy, and mucosal leukoplakia. Early mortality is often associated with bone marrow failure, infections, fatal pulmonary complications, or malignancy.
Defects in TERT are a cause of susceptibility to pulmonary fibrosis idiopathic (IPF) [MIM:178500]. Pulmonary fibrosis is a lung disease characterized by shortness of breath, radiographically evident diffuse pulmonary infiltrates, and varying degrees of inflammation and fibrosis on biopsy. It results in acute lung injury with subsequent scarring and endstage lung disease.
SEQUENCE SMILARITIES: Belongs to the reverse transcriptase family. Telomerase subfamily.
Contains 1 reverse transcriptase domain.
Molecular Weight
~90 kDa observed. Three isoforms exist for human TERT: Isoform 1 at 127 kDa, Isoform 2 at 90 kDa, and Isoform 3 at 120 kDa.
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Quality Assurance
Evaluated by Western Blot in human lymph node tissue lysate.
Western Blot Analysis: A 1:2,000 dilution of this antibody detected TERT in 10 µg of human lymph node tissue lysate.
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
