Application Note
*Optimal dilutions/concentrations should be determined by the researcher.
Application |
Recommended Dilution |
1:250 |
Assay dependent |
Not tested in other applications.
Product Note
This antibody is specific for KCNQ5 and does not detect KCNQ1, KCNQ2, KCNQ3 or KCNQ4.
Form
Liquid
Buffer
PBS, 0.1% BSA
Preservative
0.05% Sodium azide
Storage
Store as concentrated solution. Centrifuge briefly prior to opening vial. For short-term storage (1-2 weeks), store at 4ºC. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.
Concentration
1 mg/ml (Please refer to the vial label for the specific concentration.)
Antigen Species
Human
Immunogen
Synthetic peptide corresponding to residues C(880) K A G E S T D A L S L P H V K L K(897) of human KCNQ5 protein.
Purification
Purified by antigen-affinity chromatography
Conjugation
Unconjugated
RRID
AB_11178183
Note
For laboratory research use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.
Purchasers shall not, and agree not to enable third parties to, analyze, copy, reverse engineer or otherwise attempt to determine the structure or sequence of the product.
Synonyms
potassium voltage-gated channel subfamily Q member 5 , Kcnq5l
Background
KCNQs are members of the voltage-dependent non-inactivating potassium channel family. Currently there are five known KNCQs (KCNQ1-5) found in the central nervous system. Studies have shown that KCNQ3 and KCNQ5 form heteromultimers that, when formed, substantially increase the M-current. Inhibition of M-current controls neuron excitability throughout the nervous system as well as the responsiveness to synaptic inputs. Genetic mutations in these proteins have been linked to disorders such as benign familial neonatal convulsions (BFNC), deafness, neuropathic pain and epilepsy. Voltage-dependent potassium channels are key regulators of the resting membrane potential and modulate the excitability of electrically active cells. The channels are usually tetrameric and can interact with auxiliary subunits that enhance or modify currents mediated by the pore-forming subunits.
Database
Research Area