|Tested species reactivity||Bovine, Mouse, Sheep|
|Published species reactivity||Mouse, Human|
|Host / Isotype||Rabbit / IgG|
|Immunogen||Synthetic Peptide: C E(347) V A T E V P F R L M H P Q P E D(363)|
|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)||2 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.
PA1-731 detects recombinant bovine and sheep visual arrestin.
PA1-731 has been successfully used in immunofluorescence and Western blot procedures. By Western blot this antibody detects an ~57 kDa protein representing recombinant bovine and sheep visual arrestin. This antibody also detects a lower molecular weight protein which could correspond to degradation product.
The PA1-731 immunizing peptide corresponds to amino acid residues 2-18 from rat visual arrestin. This peptide (Cat. # PEP-155) 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 to an electrochemical signal begins when the membrane-bound protein, rhodopsin, absorbs light within the retina. In the active state, rhodopsin activates transducin, a GTP binding protein that promotes the hydrolysis of cGMP by phosphodiesterase (PDE). The decrease of intracellular cGMP concentrations causes the ion channels within the outer segment of the rod or cone to close, thus causing membrane hyperpolarization and, eventually, signal transmission. Rhodopsin and quote;s activity is believed to be shut off by its phosphorylation followed by binding of the soluble protein arrestin. Arrestins are cytosolic proteins that are involved in G protein-coupled receptor (GPCR) desensitization. Arrestin binding to activated GPCRs is phosphorylation dependent and, once bound, uncouple the GPCR from the associated heterotrimeric G proteins. There are currently 4 known mammalian isoforms, beta-arrestin1 (arrestin2), beta-arrestin2 (arrestin3), visual arrestin (arrestin1), and cone arrestin. The beta- isoforms are ubiquitously expressed and are known to interact with acetylcholine and adrenergic receptors. Visual and cone arrestins are found to interact directly with transducin.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Identification of a VxP Targeting Signal in the Flagellar Na+ /K+ -ATPase.
PA1-731 was used in western blot to study Na(+) /K(+) -ATPase trafficking in photoreceptors
|Laird JG,Pan Y,Modestou M,Yamaguchi DM,Song H,Sokolov M,Baker SA||Traffic (Copenhagen, Denmark) (16:1239)||2015|
Exchange of Cone for Rod Phosphodiesterase 6 Catalytic Subunits in Rod Photoreceptors Mimics in Part Features of Light Adaptation.
PA1-731 was used in western blot to study the role of cGMP phosphodiesterase 6 in rod and cone receptors
|Majumder A,Pahlberg J,Muradov H,Boyd KK,Sampath AP,Artemyev NO||The Journal of neuroscience : the official journal of the Society for Neuroscience (35:9225)||2015|
Splice isoforms of phosducin-like protein control the expression of heterotrimeric G proteins.
PA1-731 was used in western blot to study the modulation of heterotrimeric G-protein expression by splice variants of phosducin-like protein
|Gao X,Sinha S,Belcastro M,Woodard C,Ramamurthy V,Stoilov P,Sokolov M||The Journal of biological chemistry (288:25760)||2013|
Phosducin-like protein 1 is essential for G-protein assembly and signaling in retinal rod photoreceptors.
PA1-731 was used in western blot to study the role of the co-chaperone phosducin-like protein-1 in the assembly of retinal rod photoreceptor G-proteins
|Lai CW,Kolesnikov AV,Frederick JM,Blake DR,Jiang L,Stewart JS,Chen CK,Barrow JR,Baehr W,Kefalov VJ,Willardson BM||The Journal of neuroscience : the official journal of the Society for Neuroscience (33:7941)||2013|
High levels of retinal membrane docosahexaenoic acid increase susceptibility to stress-induced degeneration.
PA1-731 was used in western blot to study the effect of retinal membrane docosahexaenoic acid on stress-induced retinal degeneration in mice.
|Tanito M,Brush RS,Elliott MH,Wicker LD,Henry KR,Anderson RE||Journal of lipid research (50:807)||2009|
Overexpression of rhodopsin alters the structure and photoresponse of rod photoreceptors.
PA1-731 was used in western blot to study how rhodopsin's overexpression affects the structure and photoresponse of rod photoreceptors
|Wen XH,Shen L,Brush RS,Michaud N,Al-Ubaidi MR,Gurevich VV,Hamm HE,Lem J,Dibenedetto E,Anderson RE,Makino CL||Biophysical journal (96:939)||2009|
N-terminal fatty acylation of transducin profoundly influences its localization and the kinetics of photoresponse in rods.
PA1-731 was used in western blot to investigate the functional significance of N-terminal fatty acylation of transducin
|Kerov V,Rubin WW,Natochin M,Melling NA,Burns ME,Artemyev NO||The Journal of neuroscience : the official journal of the Society for Neuroscience (27:10270)||2007|
Dlic1 deficiency impairs ciliogenesis of photoreceptors by destabilizing dynein.
PA1-731 was used in immunohistochemistry to study the role of dynein destabilization in the mechanism by which Dlic1 deficiency impairs photoreceptor ciliogenesis
|Kong S,Du X,Du X,Peng C,Wu Y,Li H,Jin X,Hou L,Deng K,Xu T,Tao W||Cell research (23:835)||2013|
Differential CRX and OTX2 expression in human retina and retinoblastoma.
PA1-731 was used in immunohistochemistry to study the CRX and OTX2 expression profiles in normal and cancerous retina cells
|Glubrecht DD,Kim JH,Russell L,Bamforth JS,Godbout R||Journal of neurochemistry (111:250)||2009|
GC1 deletion prevents light-dependent arrestin translocation in mouse cone photoreceptor cells.
PA1-731 was used in immunohistochemistry to study the effect of guanylate cyclase 1 on arrestin translocation in mouse cone photoreceptor cells.
|Coleman JE,Semple-Rowland SL||Investigative ophthalmology and visual science (46:12)||2005|