Render Target: SSR
Render Timestamp: 2024-11-14T22:47:28.718Z
Commit: 3c1f305a63297e594ac8d7bb5424007d592d68be
XML generation date: 2024-09-30 01:53:33.362
Product last modified at: 2024-10-22T11:45:09.003Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

hERG1a (D1Y2J) Rabbit mAb #12889

Filter:
  • WB

    Supporting Data

    REACTIVITY H R
    SENSITIVITY Endogenous
    MW (kDa) 135, 155
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 
    • R-Rat 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    hERG1a (D1Y2J) Rabbit mAb recognizes endogenous levels of both mature and immature hERG1a protein. This antibody cross-reacts with proteins of unknown origin at 65 and 42 kDa in some cell lines. This antibody does not recognize hERG1b protein.

    Species Reactivity:

    Human, Rat

    The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.

    Species predicted to react based on 100% sequence homology:

    Monkey

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ala223 of human hERG1a protein.

    Background

    hERG1(human ether-a-go-go-related gene potassium channel 1) is a voltage gated potassium channel alpha-subunit which mediates the rapidly activating component of the delayed rectifying potassium current in heart (IKr) (1,2). The hERG channel is composed of two subunits, 1a and 1b, which differ at amino terminus due to alternative splicing. Native hERG channels are heteromers of hERG1a with hERG1b. Both subunits contribute to IKr current (3-6).

    Blockade of hERG currents induced by compounds or mutation of hERG encoding gene-KCNH2 causes ventricular arrhythmias associated with inherited and acquired long QT syndrome and cardiomyocyte apoptosis (7-10). Therefore, hERG channel is a primary target for the development of class III antiarrhythmic agents (11,12). The hERG channel is also inhibited by a variety of non-antiarrhythmic compounds, which result in side effects. Consequently, hERG channel blockage is a common counter screen when selecting therapeutic agents for various diseases (11,13,14).

    Research studies have implicated hERG in cancer cell survival (15). In normal human adult tissue, hERG is expressed in heart, brain, myometrium, pancreas, and hematopoietic progenitors (16,17). hERG is expressed in various cancer cell lines of epithelial, neuronal, leukemic, and connective tissue origin but not in corresponding normal cells (18-22). Furthermore, hERG expression is associated with enhanced cancer cell proliferation, invasiveness, and poor prognosis (23,24).
    1. Warmke, J.W. and Ganetzky, B. (1994) Proc Natl Acad Sci U S A 91, 3438-42.
    2. Sanguinetti, M.C. and Tristani-Firouzi, M. (2006) Nature 440, 463-9.
    3. Lees-Miller, J.P. et al. (1997) Circ Res 81, 719-26.
    4. London, B. et al. (1997) Circ Res 81, 870-8.
    5. Lees-Miller, J.P. et al. (2003) Mol Cell Biol 23, 1856-62.
    6. Sale, H. et al. (2008) Circ Res 103, e81-95.
    7. Curran, M.E. et al. (1995) Cell 80, 795-803.
    8. Itoh, T. et al. (1998) Hum Genet 102, 435-9.
    9. González-Juanatey, J.R. et al. (2003) Circulation 107, 127-31.
    10. Gong, Q. et al. (2006) J Biol Chem 281, 4069-74.
    11. Thomas, D. et al. (2006) Curr Pharm Des 12, 2271-83.
    12. Staudacher, I. et al. (2010) Curr Opin Drug Discov Devel 13, 23-30.
    13. Wible, B.A. et al. (2005) J Pharmacol Toxicol Methods 52, 136-45.
    14. Yang, B.F. et al. (2004) Acta Pharmacol Sin 25, 554-60.
    15. Jehle, J. et al. (2011) Cell Death Dis 2, e193.
    16. Pond, A.L. et al. (2000) J Biol Chem 275, 5997-6006.
    17. Rosati, B. et al. (2000) FASEB J 14, 2601-10.
    18. Smith, G.A. et al. (2002) J Biol Chem 277, 18528-34.
    19. Lastraioli, E. et al. (2004) Cancer Res 64, 606-11.
    20. Masi, A. et al. (2005) Br J Cancer 93, 781-92.
    21. Lin, H. et al. (2007) J Cell Physiol 212, 137-47.
    22. Gong, J.H. et al. (2010) Oncol Rep 23, 1747-56.
    23. Ding, X.W. et al. (2008) J Surg Oncol 97, 57-62.
    24. Shao, X.D. et al. (2008) Cancer Biol Ther 7, 45-50.
    For Research Use Only. Not For Use In Diagnostic Procedures.
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