|Calculated MW||65675 Da|
|Homology||Mouse- identical; human- 15/18 amino acid residues identical.|
|Other Names||Cyclic nucleotide-gated cation channel alpha-4, Cyclic nucleotide-gated channel alpha-4, CNG channel alpha-4, CNG-4, CNG4, Cyclic nucleotide-gated olfactory channel subunit OCNC2, Cnga4, Cgn2|
|Related products for control experiments||Control peptide antigen (supplied with the antibody free of charge).|
|Target/Specificity||Peptide (C) SQDGKVKTTESTPPAPTK, corresponding to amino acid residues 2-19 of rat CNGA4 (Accession Q64359). Intracellular, N-terminus.|
|Peptide Confirmation||Confirmed by amino acid analysis.|
|Format||Affinity purified antibody, lyophilized powder|
|Reconstitution||50 µl or 0.2 ml deionized water, depending on the sample size.|
|Antibody Concentration After Reconstitution||0.8 mg/ml.|
|Buffer After Reconstitution||Phosphate buffered saline (PBS), pH 7.4, 1% BSA, 0.05% NaN3.|
|Storage Before Reconstitution||Lyophilized powder can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C.|
|Storage After Reconstitution||The reconstituted solution can be stored at 4ºC for up to 2 weeks. For longer periods, small aliquots should be stored at -20ºC or below. Avoid multiple freezing and thawing. The further dilutions should be made using a carrier protein such as BSA (1%). Centrifuge all antibody preparations before use (10000 × g 5 min).|
|Control Antigen Storage Before Reconstitution||Lyophilized powder can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C.|
|Control Antigen Reconstitution||100 µl water.|
|Control Antigen Storage After Reconstitution||-20ºC.|
|Preadsorption Control||1 µg peptide per 1 µg antibody.|
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Provided below are standard protocols that you may find useful for product applications.
Cyclic Nucleotide-Gated (CNG) channels belong to the superfamily of voltage-gated ion channels. Although permeable to various ions such as the monovalent Na+ and K+ ions, and the divalent Ca2+ ion, they are gated by the intracellular binding of the cyclic nucleotides cAMP and cGMP and not by voltage per se (CNGs bind preferably to cGMP)1. Six channels form this subfamily: The A subunit (CNGA1-4) and the B subunit (CNGB1 and CNGB3). Functional entities are formed by the assembly of four subunits. Each subunit consists of six membrane spanning domains, where the fourth transmembrane domain is highly positively charged, a pore domain between transmembrane domains five and six, and intracellular N- and C-termini. The cyclic nucleotide binding domain is located in the C-terminal region and is responsible for the channel gating upon cyclic nucleotide binding1. These channels are highly expressed in retinal photoreceptors and olfactory neurons where their role has been extensively studied2. CNG channels have also been detected in brain, testis and kidney although their role in these tissues has yet to be unraveled2. When heterologously expressed all subunits with exception of CNGA4, CNGB1 and CNGB3 can form functional homomeric channels. In olfactory sensory neurons, CNG channels which are formed by two CNGA2, one CNGA4 subunits and an isoform of CNGB1, are activated by the binding of cAMP, whose levels increase in response to the binding of odorant molecules to their respective receptors1,3. CNGA4 knockout mice are fertile and morphologically similar to their wild type littermates4,5. In these mice, the olfactory bulb and epithelium are developed but these mice display defects in odor adaptation, and at the molecular level, they are less sensitive to cAMP activation6. Abgent is pleased to offer a highly specific antibody directed against an intracellular epitope of rat CNGA4 channel. Anti-CNGA4 antibody (#AG1109) can be used in western blot and immunohistochemical applications. It has been designed to recognize CNGA4 from human, rat and mouse samples.
References 1. Biel, M. (2009) J. Biol. Chem. 284, 9017. 2. Kaupp, U.B. and Seifert, R. (2002) Physiol. Rev. 82, 769. 3. Zheng, T. and Zagotta, W.N. (2004) Neuron 42, 411. 4. Munger, S.D. et al. (2001) Science 294, 2172. 5. Kelliher, K.R. et al. (2003) Proc. Natl. Acad. Sci. U.S.A. 100, 4299. 6. Biel, M. and Michalakis, S. (2007) Mol. Neurobiol. 35, 266.
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