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hTERT Antibody

Rabbit Polyclonal
JCYIA Product
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25 µL
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hTERT Antibody Properties

Anti-Telomerase catalytic subunit (RABBIT) Antibody - 600-401-252S
Target Species
Known Cross Reactivity
ELISA : 1:10,000 - 1:50,000
IF Microscopy : 1:500
Western Blot : 1:500
Immunohistochemistry: 1:500
Other Dilution: IP 2µL per mg lysate
Physical State
Liquid (sterile filtered)
Shipping Condition
Dry Ice
1.0 mg/mL by UV absorbance at 280 nm
0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2
0.01% (w/v) Sodium Azide
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hTERT Antibody Description

Telomerase is a reverse transcriptase that adds telomeric repeats (TTAGGG)n to chromosomal ends, compensating for the telomere shortening that occurs with DNA replication.  In normal human somatic cells, telomerase is repressed and telomeres progressively shorten, leading to limited lifespan and senescence.  Reactivation of telomerase activity is associated with human cancer and cell immortalization.  Approximately 85% of human cancers, including breast, prostate, stomach, bladder, colon, and liver cancer, have telomerase activity, whereas most normal somatic cells do not.  The specificity of telomerase to human cancer has led to investigations of telomerase activity and expression as a tumor marker.  For example, the presence of telomerase activity in human urine has been identified as a marker for human bladder carcinoma.  Human telomerase consists of three major subunits:  a catalytic protein subunit called hTERT (for human TElomerase Reverse Transcriptase), a template RNA called hTR, and telomerase-associated protein (TEP-1).   TERT and hTR are minimally required to reconstitute telomerase activity in vitro.  In human cells, hTR is constitutively expressed.  TERT transcription is a primary mechanism for regulation of telomerase activity.
rabbit anti-TERT antibody, rabbit anti-Telomerase catalytic subunit antibody, hTERT, Telomerase reverse transcriptase, HEST2, Telomerase-associated protein 2, TP2, EST2, TCS1, TRT
This affinity purified antibody was prepared from whole rabbit serum produced by repeated immunizations with a synthetic peptide corresponding to a region near the carboxy terminal end of hTERT (accession number AF018167).
Immunogen Type
Storage Condition
Store vial at -20° C or below prior to opening. This vial contains a relatively low volume of reagent (25 µL). To minimize loss of volume dilute 1:10 by adding 225 µL of the buffer stated above directly to the vial. Recap, mix thoroughly and briefly centrifuge to collect the volume at the bottom of the vial. Use this intermediate dilution when calculating final dilutions as recommended below. Store the vial at -20°C or below after dilution. Avoid cycles of freezing and thawing.
Application Note
This affinity purified antibody has been tested for use in immunoblotting, immunoprecipitation, and immunofluorescence microscopy.   In these assays, the antibody detects ectopically-expressed hTERT and high levels of endogenous hTERT.   Although it has been reported that this antibody reacts with mouse TERT (mTERT) (see Drissi, et al. 2001), the binding to mTERT is considerably weaker and less specific than the binding to hTERT (not shown).   A SY5Y cell nuclear extract can be used as a positive control. To detect TERT, fix cells in 2% paraformaldehyde (in PBS) for 10'. Wash the slides twice in PBS for 5' each. Permeabilize the cells in 0.5% NP-40 for 10'. Wash as before in PBS. Block the cells using PBG buffer (0.2% cold water fish gelatin (Sigma G-7765) and 0.5% BSA in PBS) for 20' at room temperature. Incubate in primary antibody (diluted in PBG) for 1-2 hours at RT or overnight at 4ºC. Wash the slides three times in PBG for 5' each. Incubate with secondary antibody (diluted in PBG) for 1 hour at RT in the dark. Wash the slides three times in PBG for 5' each. Mount in DAPI-containing medium. In immunoblot assays, whole cell or nuclear extracts were loaded at a concentration of 100 µg protein per well. A working dilution of 1:500 anti-TERT antibody was used followed by a 1:3,000 dilution of horseradish peroxidase- conjugated goat anti-rabbit IgG as the secondary antibody. For immunofluorescence microscopy staining, a working dilution of 1:500 was used followed by a 1:200 dilution of rhodamine-conjugated donkey anti-rabbit IgG as a secondary antibody. Immunoprecipitation was performed using 20 µL of protein A beads and 2 µL of the anti-TERT serum per 1mg protein from cell lysate. A working dilution of 1:500 is also suggested for immunohistochemistry.
This antiserum primarily detects hTERT, but several non-specific bands appear on immunoblots.  In immunofluorescence microscopy assays, staining with anti-TERT-16 was specific to the nuclei of cells with ectopic TERT expression.
Disclaimer Note-General
This product is for research use only and is not intended for therapeutic or diagnostic applications. Please contact a technical service representative for more information. All products of animal origin manufactured by Rockland Immunochemicals are derived from starting materials of North American origin. Collection was performed in United States Department of Agriculture (USDA) inspected facilities and all materials have been inspected and certified to be free of disease and suitable for exportation. All properties listed are typical characteristics and are not specifications. All suggestions and data are offered in good faith but without guarantee as conditions and methods of use of our products are beyond our control. All claims must be made within 30 days following the date of delivery. The prospective user must determine the suitability of our materials before adopting them on a commercial scale. Suggested uses of our products are not recommendations to use our products in violation of any patent or as a license under any patent of Rockland Immunochemicals, Inc. If you require a commercial license to use this material and do not have one, then return this material, unopened to: Rockland Inc., P.O. BOX 5199, Limerick, Pennsylvania, USA.
General Reference
Drissi, R., Zindy, F., Roussel, M. F. and Cleveland, J.L. (2001) c-MYC-mediated regulation of telomerase activity is disabled in immortalized cells. J. Biol. Chem. 276(32): 29994-30001. Shay, J.W., Zou, Y., Hiyama, E. and Wright, W.E. (2001) Telomerase and cancer. Hum. Mol. Genet. 10: 677-685. Hiyama, E., Hiyama, K., Yokoyama, T. and Shay, J.W. (2001) Immunohistochemical detection of telomerase (hTERT) protein in human cancer tissues and a subset of cells in normal tissues. Neoplasia 3:17-26.
Specific Reference
Wu, Y.L., et al. (2006) Immunodetection of human telomerase reverse-transcriptase (hTERT) re-appraised: nucleolin and telomerase cross paths. J.Cell Sci. 119: 2797-2806.
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Submitted On
11/27/2012 05:29:01 PM
Mouse C57 Black
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