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|Tested species reactivity||Bovine, Sheep|
|Published species reactivity||Pig, Mouse|
|Host / Isotype||Rabbit / IgG|
|Immunogen||Synthetic Peptide: K(18) L K E D A E K D A R T V K(31) C|
|Purification||Antigen affinity chromatography|
|Storage buffer||PBS with 1mg/ml BSA|
|Contains||0.05% sodium azide|
|Storage Conditions||-20° C, Avoid Freeze/Thaw Cycles|
|Tested Applications||Dilution *|
|Western Blot (WB)||1 µg/ml|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
|Western Blot (WB)||See 2 publications below|
PA1-724 detects rod transducin alpha (Tr alpha) from bovine outer rod segments and sheep retinal extract.
PA1-724 has been successfully used in Western blot procedures. By Western blot, this antibody detects an ~38 kDa protein representing Tr alpha from sheep retinal extract.
The PA1-724 immunizing peptide corresponds to amino acid residues 18-31 from human Tr alpha. This peptide (Cat. # PEP-153) is available for use in neutralization and control experiments.
Vision involves the conversion of light into electrochemical signals that are processed by the retina and subsequently sent to and interpreted by the brain. The process of converting light into an electrochemical signal begins when the membrane-bound protein, rhodopsin, absorbs light within the retina. Photoexcitation of rhodopsin causes the cytoplasmic surface of the protein to become catalytically active. In the active state, rhodopsin activates transducin, a GTP binding protein. Once activated, transducin promotes the hydrolysis of cGMP by phosphodiesterase (PDE). The decrease of intracellular cGMP concentration causes the ion channels within the outer segment of the rod or cone to close, thus causing membrane hyperpolarization and, eventually, signal transmission. Rhodopsin activity is believed to be shut off by phosphorylation followed by binding of the soluble protein, arrestin.
Transducin, once activated by rhodopsin, promotes the hydrolysis of cGMP by PDE. The subunit composition of transducin differs between different photoreceptor cells. Rod transducin consists of rod transducin alpha (Tr alpha), T beta, and T gamma. Cone transducin is composed of cone transducin alpha (Tc alpha), T beta and T gamma. Differential transducin subunit composition of transducin is believed to be responsible for the different light sensitivities between photoreceptive cells.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Structural and functional protein network analyses predict novel signaling functions for rhodopsin.
PA1-724 was used in western blot to investigate the multiple roles of rhodopsin in the visual system
|Kiel C,Vogt A,Campagna A,Chatr-aryamontri A,Swiatek-de Lange M,Beer M,Bolz S,Mack AF,Kinkl N,Cesareni G,Serrano L,Ueffing M||Molecular systems biology (7:null)||2011|
Phototransduction in transgenic mice after targeted deletion of the rod transducin alpha -subunit.
PA1-724 was used in western blot to investigate transducin subunits' functional specificity in phototransduction
|Calvert PD,Krasnoperova NV,Lyubarsky AL,Isayama T,Nicoló M,Kosaras B,Wong G,Gannon KS,Margolskee RF,Sidman RL,Pugh EN,Makino CL,Lem J||Proceedings of the National Academy of Sciences of the United States of America (97:13913)||2000|
G protein subunit alpha transducin 1; Guanine nucleotide-binding protein G(t) subunit alpha-1; Tr alpha; Transducin alpha-1 chain