Anti-Kv11.1 (HERG)-Extracellular
- 貨號 Cat. No.
- APC-109
- 規格 Size
- 50 μl 0.2ml
Description
Anti-Kv11.1 (HERG)-Extracellular
| Product#: | APC-109 |
| Sizes: |
| 50 ml |
| 0.2 ml |
| Host: |
| Rabbit |
| Epitope: |
| Peptide AFLLKETEEGPPATEC corresponding to residues 430-445 of human KV11.1. |
 |
| Putative epitope location: |
Extracellular, between S1 and S2 domains. |
| Homology: |
Rat, mouse ?11 out of 16 residues identical; dog, rabbit-15 out of 16 residues identical. |
| Reactivity Confirmed: |
| Human. |
Applications:
| Western Blotting: |
 | Western blotting of HEK-Kv11.1 transfected cells. 1. Anti-Kv11.1-extracellular antibody (1:200). 2. Anti-Kv11.1-extracellular antibody, preincubated with the control peptide antigen. |
| Immunohistochemistry: |
 |
| Staining of Kv11.1 in rat heart using Anti-Kv11.1 (HERG) extracellular antibody (#APC-109). (A) Transversal section of the atrium wall; note that arterial smooth muscle fibers were not stained (green arrow) (B) Longitudinal section of the myocardium (C) Section showing myocardium and endocardium (red arrow); note that the Purkinje fibers show a pale stain (blue arrow). Black arrow shows always myocytes. DAB product is brown and the counterstain is cresyl violet. |
| Immunocytochemistry: |
| Intact live HEK-KV11.1 transfected cells. |
 |
Live intact HEK-Kv11.1 transfected cells were incubated with anti-Kv11.1-extracellular (1:25) (left panel) or with Kv11.1-extracellular preincubated with the control antigen (right panel). The Kv11.1 was visualized with a goat-anti-rabbit-Alexa 555 antibody (red staining). Nuclei of the living cells were stained with the cell permeable dye Hoechst 33342 (blue staining). Note that not all cells are stained, indicating that not all the Kv11.1 channels are expressed at the cell membrane at the moment of staining. Indirect Flow Cytometry: |
 |
FACS analysis of live intact K562 (human chronic myelogenous leukemia) cells (2-8 mg antibody /1x106cells): K562 cells + Goat-anti-Rabbit-FITC (green line). K562 cells + anti- KV11.1-extracellular + Goat-anti-Rabbit-FITC (black line). |
| References: |
| 1. Curran, M.E. et al. (1995) Cell 80, 795. |
| 2. Sanguinetti, M.C. et al. (1995) Cell 81, 299. |
| 3. Pardo, L.A. et al. (2004) Physiology 19, 285. |
The KV11.1 (HERG) channel is a member of the ether-a-go-go (EAG) subfamily of voltage-dependent K+ channels that includes the related proteins KV11.2 and KV11.3 (erg2 and erg3). KV11.1 possess the signature structure of the voltage-dependent K+ channels: six membrane-spanning domains and intracellular N and C termini.
The KV11.1 current is characterized by strong inward rectification with slow activation and very rapid inactivation kinetics. The channel is expressed in the brain and heart (where it underlies the IKr current) and has a central role in mediating repolarization of action potentials.
Mutations in the KV11.1 channel cause inherited long QT syndrome (LQTS) or abnormalities in the repolarization of the heart that are associated with life-threatening arrhythmias and sudden death. All the identified KV11.1 mutations produce loss of function of the channel via several cellular mechanisms ranging from alterations of gating properties, alterations of channel permeability/selectivity and alterations in intracellular channel trafficking that decreases the number of channels that reach the cell membrane. Lately drug-induced forms of LQTS have been reported for a wide range of non-cardiac drugs including antihistamines, psychoactive agents and antimicrobials. All these drugs potently block the KV11.1 channel as an unintended side effect, prompting regulatory drug agencies to issue recommendations for the testing of new drugs for their potential KV11.1 blocking effect.
Mutations in the KV11.1 channel cause inherited long QT syndrome (LQTS) or abnormalities in the repolarization of the heart that are associated with life-threatening arrhythmias and sudden death. All the identified KV11.1 mutations produce loss of function of the channel via several cellular mechanisms ranging from alterations of gating properties, alterations of channel permeability/selectivity and alterations in intracellular channel trafficking that decreases the number of channels that reach the cell membrane. Lately drug-induced forms of LQTS have been reported for a wide range of non-cardiac drugs including antihistamines, psychoactive agents and antimicrobials. All these drugs potently block the KV11.1 channel as an unintended side effect, prompting regulatory drug agencies to issue recommendations for the testing of new drugs for their potential KV11.1 blocking effect.
In addition, KV11.1 expression was found to be upregulated in several tumor cell lines of different histogenesis suggesting that it confers the cells some advantage in cell proliferation. Indeed, in several studies it has been shown that inhibition of the KV11.1 current leads to a decrease in tumor cell proliferation.
We have now developed a novel anti-KV11.1 antibody directed against an extracellular epitope of the human channel. This antibody has been extensively tested in applications using intact living cells such as flow cytometry and immunocytochemistry as well as Western blotting. This antibody is a unique and invaluable tool to researchers looking into mutations affecting KV11.1 trafficking or testing KV11.1 expression in patients with hematopoietic malignancies among many other potential uses. In the near future, we hope to release a fluorescent-labeled version of this antibody.