|Calculated MW||79228 Da|
|Homology||Mouse- 13/14 amino acid residues identical; human- 9/14 amino acid residues identical.|
|Other Names||cGMP-gated cation channel alpha-1, Cyclic nucleotide-gated cation channel 1, Cyclic nucleotide-gated channel alpha-1, CNG channel alpha-1, CNG-1, CNG1, Cyclic nucleotide-gated channel, photoreceptor, Rod photoreceptor cGMP-gated channel subunit alpha, Cnga1, Cncg, Cncg1|
|Related products for control experiments||Control peptide antigen (supplied with the antibody free of charge).|
|Target/Specificity||Peptide (C)NDNGSLSEESENED, corresponding to amino acid residues 41-54 of rat CNGA1 (Accession Q62927). 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 channels1. In rod photoreceptors, functional channels are composed of three CNGA1 subunits and one CNGB1 subunit3. Mutations in either of CNGA1 or CNGB1 genes are responsible for the onset of retinitis pigmentosa, a progressive degeneration of rod and cone receptors which is presented in part by night blindness3-4. As no knock out CNGA1 model systems exist, a transgenic mice line with lowered CNGA1 protein levels demonstrated symptoms which are reminiscent of retinitis pigmentosa, in agreement with the fact that a lack of CNGA1 is responsible for retinitis pigmentosa3. Abgent is pleased to offer a highly specific antibody directed against an intracellular epitope of rat CNGA1 channel. Anti-CNGA1 antibody (#AG1110) can be used in western blot analysis. It has been designed to recognize CNGA1 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. Mazzolini, M. et al. (2010) Pflugers Arch. – Eur. J. Physiol. 459, 547. 4. Biel, M. and Michalakis, S. (2007) Mol. Neurobiol. 35, 266.
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